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Conserved domains on  [gi|1914779978|ref|NP_001374560|]
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focal adhesion kinase 1 isoform 15 [Homo sapiens]

Protein Classification

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 ...
420-689 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: 586.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd05056      1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd05056     81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 659
Cdd:cd05056    161 SYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 240
                          250       260       270
                   ....*....|....*....|....*....|
gi 1914779978  660 MTKCWAYDPSRRPRFTELKAQLSTILEEEK 689
Cdd:cd05056    241 MTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
Focal_AT pfam03623
Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in ...
924-1053 5.07e-74

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: 240.25  E-value: 5.07e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  924 NLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLG 1003
Cdd:pfam03623    1 DLDRTNDKVYECVTRVVKAVMQLSQEVQTAKPDEYVDLVKNVGLELRNLLTSVDELLPILPASSHREIEMAQKLLNKDLA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978 1004 ELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKM 1053
Cdd:pfam03623   81 ELINKMKLAQQYSITTLDEEYRKQMLTAAHTLAMDAKNLLDVVDSARLRA 130
FERM_N_2 pfam18038
FERM N-terminal domain; This entry represents the FERM N-terminal domain found in focal ...
35-130 1.88e-51

FERM N-terminal domain; This entry represents the FERM N-terminal domain found in focal adhesion kinases.


:

Pssm-ID: 436229  Cd Length: 99  Bit Score: 175.72  E-value: 1.88e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   35 RVLKVFHYFESNSEPTtWASIIRHGDATDVRGIIQKI---VDSHKV-KHVACYGFRLSHLRSEEVHWLHVDMGVSSVREK 110
Cdd:pfam18038    1 RILKVCHYSESNNEGK-WFKLIRCGDATDVRGIIQKIlssGRIGPViRHVSCYGLRLKHLKSDEVHWLHPDMTVSEVREK 79
                           90       100
                   ....*....|....*....|
gi 1914779978  111 YELAHPPEEWKYELRIRYLP 130
Cdd:pfam18038   80 YEQQHPEAEWRYDLRIRYLP 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
36-258 1.33e-39

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 145.52  E-value: 1.33e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978    36 VLKVFHYFESNSEpttwasiIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKyelah 115
Cdd:smart00295    1 VLKVYLLDGTTLE-------FEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVK----- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   116 pPEEWKYELRIRYLPKgFLNQFTEDKPTLNFFYQQVKSDYMLEIAdQVDQEIALKLGCLEIRRSYWEMRGNALEkksnye 195
Cdd:smart00295   69 -SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRL-PCPEEEALLLAALALQAEFGDYDEELHD------ 139
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978   196 vLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECF 258
Cdd:smart00295  140 -LRGELSLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
254-328 4.42e-34

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: 126.59  E-value: 4.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  254 DKECFKCALGSSWIISVELAIGPEEGISYLTDKGCN------------------------------------PLTVTAPS 297
Cdd:cd13190      1 DQEIFKCALGSGWSIPVDLVIGPEVGISYLTDKGSApthladfeqiqsiqtsksedkdgkallqlkiagasePLSITCSS 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1914779978  298 LTIAENMADLIDGYCRLVNGTSQSFIIRPQK 328
Cdd:cd13190     81 LATAESLADLIDGYCRLVNQTDSSLIIRPEK 111
 
Name Accession Description Interval E-value
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
420-689 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: 586.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd05056      1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd05056     81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 659
Cdd:cd05056    161 SYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 240
                          250       260       270
                   ....*....|....*....|....*....|
gi 1914779978  660 MTKCWAYDPSRRPRFTELKAQLSTILEEEK 689
Cdd:cd05056    241 MTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
427-681 1.35e-131

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: 398.79  E-value: 1.35e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 504
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLkGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGePLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYK 583
Cdd:pfam07714   81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDiYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:pfam07714  161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQC 240
                          250
                   ....*....|....*...
gi 1914779978  664 WAYDPSRRPRFTELKAQL 681
Cdd:pfam07714  241 WAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
427-681 3.00e-125

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 382.26  E-value: 3.00e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   427 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 504
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEePLYIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 584
Cdd:smart00219   81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   585 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 664
Cdd:smart00219  161 RGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCW 240
                           250
                    ....*....|....*..
gi 1914779978   665 AYDPSRRPRFTELKAQL 681
Cdd:smart00219  241 AEDPEDRPTFSELVEIL 257
Focal_AT pfam03623
Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in ...
924-1053 5.07e-74

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: 240.25  E-value: 5.07e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  924 NLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLG 1003
Cdd:pfam03623    1 DLDRTNDKVYECVTRVVKAVMQLSQEVQTAKPDEYVDLVKNVGLELRNLLTSVDELLPILPASSHREIEMAQKLLNKDLA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978 1004 ELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKM 1053
Cdd:pfam03623   81 ELINKMKLAQQYSITTLDEEYRKQMLTAAHTLAMDAKNLLDVVDSARLRA 130
FERM_N_2 pfam18038
FERM N-terminal domain; This entry represents the FERM N-terminal domain found in focal ...
35-130 1.88e-51

FERM N-terminal domain; This entry represents the FERM N-terminal domain found in focal adhesion kinases.


Pssm-ID: 436229  Cd Length: 99  Bit Score: 175.72  E-value: 1.88e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   35 RVLKVFHYFESNSEPTtWASIIRHGDATDVRGIIQKI---VDSHKV-KHVACYGFRLSHLRSEEVHWLHVDMGVSSVREK 110
Cdd:pfam18038    1 RILKVCHYSESNNEGK-WFKLIRCGDATDVRGIIQKIlssGRIGPViRHVSCYGLRLKHLKSDEVHWLHPDMTVSEVREK 79
                           90       100
                   ....*....|....*....|
gi 1914779978  111 YELAHPPEEWKYELRIRYLP 130
Cdd:pfam18038   80 YEQQHPEAEWRYDLRIRYLP 99
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
421-731 2.78e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 2.78e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 498
Cdd:COG0515      3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRP---VALKVLRPelAADPEARERFRREARALARLNHPNIVRVYDVGEED 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PV-WIIMELCTlGE-LRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 576
Cdd:COG0515     80 GRpYLVMEYVE-GEsLADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTYYKAS--KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPMP---PN 651
Cdd:COG0515    158 GGATLTQTGtvVGTPG--YMAPEQARGEPVDPRSDVYSLGVTLYE-LLTGRPPFDGDSPAELLRAHLREPPPPPSelrPD 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRS 730
Cdd:COG0515    235 LPPALDAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 314

                   .
gi 1914779978  731 S 731
Cdd:COG0515    315 A 315
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
36-258 1.33e-39

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 145.52  E-value: 1.33e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978    36 VLKVFHYFESNSEpttwasiIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKyelah 115
Cdd:smart00295    1 VLKVYLLDGTTLE-------FEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVK----- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   116 pPEEWKYELRIRYLPKgFLNQFTEDKPTLNFFYQQVKSDYMLEIAdQVDQEIALKLGCLEIRRSYWEMRGNALEkksnye 195
Cdd:smart00295   69 -SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRL-PCPEEEALLLAALALQAEFGDYDEELHD------ 139
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978   196 vLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECF 258
Cdd:smart00295  140 -LRGELSLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
254-328 4.42e-34

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: 126.59  E-value: 4.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  254 DKECFKCALGSSWIISVELAIGPEEGISYLTDKGCN------------------------------------PLTVTAPS 297
Cdd:cd13190      1 DQEIFKCALGSGWSIPVDLVIGPEVGISYLTDKGSApthladfeqiqsiqtsksedkdgkallqlkiagasePLSITCSS 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1914779978  298 LTIAENMADLIDGYCRLVNGTSQSFIIRPQK 328
Cdd:cd13190     81 LATAESLADLIDGYCRLVNQTDSSLIIRPEK 111
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
451-721 2.01e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 86.61  E-value: 2.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  451 NPALAVAIKTCKNCTSDSVREKFL------------QEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ 517
Cdd:PTZ00267    78 NPTTAAFVATRGSDPKEKVVAKFVmlnderqaayarSELHCLAACDHFGIVKHFDDFkSDDKLLLIMEYGSGGDLNKQIK 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  518 VR-KYSLDLAS--LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKW 593
Cdd:PTZ00267   158 QRlKEHLPFQEyeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDvASSFCGTPYY 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  594 MAPESINFRRFTSASDVWMFGVCMWEIL-MHgvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:PTZ00267   238 LAPELWERKRYSKKADMWSLGVILYELLtLH--RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRP 315
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  673 R-----FTELKAQLSTILEE-----EKAQQEERMRMESRRQatvswdsgGSDEAPPKPS 721
Cdd:PTZ00267   316 TtqqllHTEFLKYVANLFQDivrhsETISPHDREEILRQLQ--------ESGERAPPPS 366
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
143-248 8.88e-17

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). 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, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 76.52  E-value: 8.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  143 TLNFFYQQVKSDYMLEIAdQVDQEIALKLGCLEIRRSYwemrGNalekKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRK 222
Cdd:cd14473      1 TRYLLYLQVKRDILEGRL-PCSEETAALLAALALQAEY----GD----YDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEK 71
                           90       100
                   ....*....|....*....|....*.
gi 1914779978  223 LIQQTFRQFANLNREESILKFFEILS 248
Cdd:cd14473     72 RIVELHKKLRGLSPAEAKLKYLKIAR 97
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
425-738 3.05e-15

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 80.22  E-value: 3.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHqgiymspenpaLA--------VAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGV 494
Cdd:NF033483     7 GRYEIGERIGRGGMAEVY-----------LAkdtrldrdVAVKVLRPdlARDPEFVARFRREAQSAASLSHPNIVSVYDV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITENPV-WIIMEL---CTLGEL---RSFLQVRKySLDLASLILyayqlsTALAYLESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:NF033483    76 GEDGGIpYIVMEYvdgRTLKDYireHGPLSPEE-AVEIMIQIL------SALEHAHRNGIVHRDIKPQNILITKDGRVKV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDST-----------YYkaskgklpikwMAPE-----SINFRrftsaSDVWMFGVCMWEILMhGVKPFQGv 631
Cdd:NF033483   149 TDFGIARALSSTTmtqtnsvlgtvHY-----------LSPEqarggTVDAR-----SDIYSLGIVLYEMLT-GRPPFDG- 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  632 knndvigriEN---------GERLPMP----PNCPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAqQEERMR 697
Cdd:NF033483   211 ---------DSpvsvaykhvQEDPPPPselnPGIPQSLDAVVLKATAKDPDDRYQsAAEMRADLETALSGQRL-NAPKFA 280
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  698 MESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSP 738
Cdd:NF033483   281 PDSDDDRTKVLPPIPPAPAPTAAEPPEDPDDDGEGGEPADD 321
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
143-248 5.29e-12

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 63.83  E-value: 5.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  143 TLNFFYQQVKSDYMLEIADqVDQEIALKLGCLEIRRSYwemrGNALEKKSNYEVLekdvGLKRFFPKSLLDSVKAKTLRK 222
Cdd:pfam00373   11 TRHLLYLQAKDDILEGRLP-CSEEEALLLAALQLQAEF----GDYQPSSHTSEYL----SLESFLPKQLLRKMKSKELEK 81
                           90       100
                   ....*....|....*....|....*.
gi 1914779978  223 LIQQTFRQFANLNREESILKFFEILS 248
Cdd:pfam00373   82 RVLEAHKNLRGLSAEEAKLKYLQIAQ 107
 
Name Accession Description Interval E-value
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
420-689 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: 586.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd05056      1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd05056     81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 659
Cdd:cd05056    161 SYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 240
                          250       260       270
                   ....*....|....*....|....*....|
gi 1914779978  660 MTKCWAYDPSRRPRFTELKAQLSTILEEEK 689
Cdd:cd05056    241 MTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
427-681 1.35e-131

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: 398.79  E-value: 1.35e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 504
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLkGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGePLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYK 583
Cdd:pfam07714   81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDiYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:pfam07714  161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQC 240
                          250
                   ....*....|....*...
gi 1914779978  664 WAYDPSRRPRFTELKAQL 681
Cdd:pfam07714  241 WAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
427-681 3.00e-125

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 382.26  E-value: 3.00e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   427 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 504
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEePLYIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 584
Cdd:smart00219   81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   585 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 664
Cdd:smart00219  161 RGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCW 240
                           250
                    ....*....|....*..
gi 1914779978   665 AYDPSRRPRFTELKAQL 681
Cdd:smart00219  241 AEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
427-681 6.88e-124

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: 378.82  E-value: 6.88e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   427 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIM 504
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLkGKGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEeEPLMIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   505 ELCTLGELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 583
Cdd:smart00221   81 EYMPGGDLLDYLRKnRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYK 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   584 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:smart00221  161 VKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQC 240
                           250
                    ....*....|....*...
gi 1914779978   664 WAYDPSRRPRFTELKAQL 681
Cdd:smart00221  241 WAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
431-681 3.66e-123

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: 376.88  E-value: 3.66e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCTL 509
Cdd:cd00192      1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEeEPLYLVMEYMEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRK--------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd00192     81 GDLLDFLRKSRpvfpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 Y-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLM 660
Cdd:cd00192    161 YrKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELYELM 240
                          250       260
                   ....*....|....*....|.
gi 1914779978  661 TKCWAYDPSRRPRFTELKAQL 681
Cdd:cd00192    241 LSCWQLDPEDRPTFSELVERL 261
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
433-686 6.42e-97

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: 6.42e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 512
Cdd:cd05060      3 LGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLMLVMELAPLGPL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  513 RSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYKA-SKGKLP 590
Cdd:cd05060     83 LKYLKKRR-EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGaGSDYYRAtTAGRWP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  591 IKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSR 670
Cdd:cd05060    162 LKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKYRPED 241
                          250
                   ....*....|....*.
gi 1914779978  671 RPRFTELKAQLSTILE 686
Cdd:cd05060    242 RPTFSELESTFRRDPE 257
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
433-682 4.15e-87

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: 4.15e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLG 510
Cdd:cd05040      3 LGDGSFGVVRRGEWTTPSGKVIQVAVKCLKsdVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVTELAPLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM--EDSTYYKASKGK 588
Cdd:cd05040     83 SLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALpqNEDHYVMQEHRK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE-NGERLPMPPNCPPTLYSLMTKCWAYD 667
Cdd:cd05040    163 VPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDkEGERLERPDDCPQDIYNVMLQCWAHK 242
                          250
                   ....*....|....*
gi 1914779978  668 PSRRPRFTELKAQLS 682
Cdd:cd05040    243 PADRPTFVALRDFLP 257
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
427-682 1.91e-85

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: 276.95  E-value: 1.91e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIME 505
Cdd:cd05033      6 VTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKsRPVMIVTE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-TYYKA 584
Cdd:cd05033     86 YMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSeATYTT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd05033    166 KGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQLMLDCW 245
                          250
                   ....*....|....*...
gi 1914779978  665 AYDPSRRPRFTELKAQLS 682
Cdd:cd05033    246 QKDRNERPTFSQIVSTLD 263
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
420-682 4.86e-85

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: 276.15  E-value: 4.86e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-T 496
Cdd:cd05032      1 WELPREKITLIRELGQGSFGMVYEGLAkgVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVsT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGELRSFL--------QVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:cd05032     81 GQPTLVVMELMAKGDLKSYLrsrrpeaeNNPGLgPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 646
Cdd:cd05032    161 GDFGMTRDIYETDYYrKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGHL 240
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  647 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 682
Cdd:cd05032    241 DLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
420-681 1.96e-84

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: 274.28  E-value: 1.96e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVIT-EN 498
Cdd:cd05068      3 WEIDRKSLKLLRKLGSGQFGEVWEGLW----NNTTPVAVKTLKPGTMDP--EDFLREAQIMKKLRHPKLIQLYAVCTlEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd05068     77 PIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 STYYKASKG-KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05068    157 EDEYEAREGaKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQLY 236
                          250       260
                   ....*....|....*....|....
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05068    237 DIMLECWKADPMERPTFETLQWKL 260
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
433-681 1.89e-82

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: 268.16  E-value: 1.89e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 511
Cdd:cd05041      3 IGRGNFGDVYRGVLKPDN---TEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKqPIMIVMELVPGGS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRyMEDSTYYKASKG--KL 589
Cdd:cd05041     80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR-EEEDGEYTVSDGlkQI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPS 669
Cdd:cd05041    159 PIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYDPE 238
                          250
                   ....*....|..
gi 1914779978  670 RRPRFTELKAQL 681
Cdd:cd05041    239 NRPSFSEIYNEL 250
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
431-681 2.66e-82

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: 267.61  E-value: 2.66e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTL 509
Cdd:cd05034      1 KKLGAGQFGEVWMGVW----NGTTKVAVKTLKPGTMSP--EAFLQEAQIMKKLRHDKLVQLYAVCSdEEPIYIVTELMSK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd05034     75 GSLLDYLRTgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05034    155 FPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKKEP 234
                          250
                   ....*....|...
gi 1914779978  669 SRRPRFTELKAQL 681
Cdd:cd05034    235 EERPTFEYLQSFL 247
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
420-684 1.08e-80

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: 1.08e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 498
Cdd:cd05039      1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQK-----VAVKCLKD--DSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEgN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05039     74 GLYIVTEYMAKGSLVDYLRSRGRAvITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEAS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTyykaSKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05039    154 SNQ----DGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPEGCPPEVY 229
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd05039    230 KVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
433-681 2.35e-79

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: 2.35e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGI---YMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCT 508
Cdd:cd05044      3 LGSGAFGEVFEGTakdILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNdPQYIILELME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYS------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYMED 578
Cdd:cd05044     83 GGDLLSYLRAARPTaftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDyrerVVKIGDFGLARDIYK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 STYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05044    163 NDYYrKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDDLY 242
                          250       260
                   ....*....|....*....|....
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05044    243 ELMLRCWSTDPEERPSFARILEQL 266
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
426-685 5.52e-79

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: 259.65  E-value: 5.52e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM 504
Cdd:cd05057      8 ELEKGKVLGSGAFGTVYKGVWIPEgEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQLIT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYK 583
Cdd:cd05057     88 QLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDvDEKEYH 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:cd05057    168 AEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTIDVYMVLVKC 247
                          250       260
                   ....*....|....*....|..
gi 1914779978  664 WAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05057    248 WMIDAESRPTFKELANEFSKMA 269
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
430-683 2.27e-77

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: 254.16  E-value: 2.27e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIyMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 508
Cdd:cd05085      1 GELLGKGNFGEVYKGT-LKDKTP---VAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQrQPIYIVMELVP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd05085     77 GGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05085    157 IPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDYNP 236
                          250
                   ....*....|....*
gi 1914779978  669 SRRPRFTELKAQLST 683
Cdd:cd05085    237 ENRPKFSELQKELAA 251
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
430-681 3.45e-76

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: 251.00  E-value: 3.45e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 508
Cdd:cd05084      1 GERIGRGNFGEVFSGRLRADNTP---VAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQkQPIYIVMELVQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYykASKG- 587
Cdd:cd05084     78 GGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVY--AATGg 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 --KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 665
Cdd:cd05084    156 mkQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWE 235
                          250
                   ....*....|....*.
gi 1914779978  666 YDPSRRPRFTELKAQL 681
Cdd:cd05084    236 YDPRKRPSFSTVHQDL 251
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
421-683 8.41e-76

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: 8.41e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-E 497
Cdd:cd05048      1 EIPLSAVRFLEELGEGAFGKVYKGelLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTkE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQVR---------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 562
Cdd:cd05048     81 QPQCMLFEYMAHGDLHEFLVRHsphsdvgvssdddgtASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  563 DCVKLGDFGLSRYMEDSTYYKA-SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE 641
Cdd:cd05048    161 LTVKISDFGLSRDIYSSDYYRVqSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMIR 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  642 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 683
Cdd:cd05048    241 SRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLRT 282
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
433-681 1.04e-75

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: 1.04e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpALAVAIKTCKNCTSD-SVREKFLQEALTMRQFDHPHIVKLIGvITENPVW-IIMELCTLG 510
Cdd:cd05116      3 LGSGNFGTVKKGYYQMKKV-VKTVAVKILKNEANDpALKDELLREANVMQQLDNPYIVRMIG-ICEAESWmLVMEMAELG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-SKGK 588
Cdd:cd05116     81 PLNKFLQKNRHVTE-KNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALrADENYYKAqTHGK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05116    160 WPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCWTYDV 239
                          250
                   ....*....|...
gi 1914779978  669 SRRPRFTELKAQL 681
Cdd:cd05116    240 DERPGFAAVELRL 252
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
420-684 1.74e-75

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: 1.74e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVIT-EN 498
Cdd:cd05052      1 WEIERTDITMKHKLGGGQYGEVYEGVW---KKYNLTVAVKTLKEDTMEV--EEFLKEAAVMKEIKHPNLVQLLGVCTrEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVR-KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05052     76 PFYIITEFMPYGNLLDYLRECnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05052    156 GDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCPPKVY 235
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd05052    236 ELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
433-685 6.42e-75

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: 248.84  E-value: 6.42e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT---ENPVWIIMELCT 508
Cdd:cd05038     12 LGEGHFGSVELCRYDPLgDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCEspgRRSLRLIMEYLP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-SK 586
Cdd:cd05038     92 SGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLpEDKEYYYVkEP 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHG-------------VKPFQGVKN-NDVIGRIENGERLPMPPNC 652
Cdd:cd05038    172 GESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqsppalflrmIGIAQGQMIvTRLLELLKSGERLPRPPSC 251
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05038    252 PDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
427-685 4.83e-74

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: 245.93  E-value: 4.83e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIME 505
Cdd:cd05065      6 VKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSrPVMIITE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS----TY 581
Cdd:cd05065     86 FMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDtsdpTY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMT 661
Cdd:cd05065    166 TSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPTALHQLML 245
                          250       260
                   ....*....|....*....|....
gi 1914779978  662 KCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05065    246 DCWQKDRNLRPKFGQIVNTLDKMI 269
Focal_AT pfam03623
Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in ...
924-1053 5.07e-74

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: 240.25  E-value: 5.07e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  924 NLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLG 1003
Cdd:pfam03623    1 DLDRTNDKVYECVTRVVKAVMQLSQEVQTAKPDEYVDLVKNVGLELRNLLTSVDELLPILPASSHREIEMAQKLLNKDLA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978 1004 ELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKM 1053
Cdd:pfam03623   81 ELINKMKLAQQYSITTLDEEYRKQMLTAAHTLAMDAKNLLDVVDSARLRA 130
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
422-685 6.86e-74

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: 245.16  E-value: 6.86e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PV 500
Cdd:cd05066      1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSkPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED-- 578
Cdd:cd05066     81 MIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDdp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYS 658
Cdd:cd05066    161 EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQ 240
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  659 LMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05066    241 LMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
433-698 1.24e-73

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: 1.24e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 512
Cdd:cd05115     12 LGSGNFGCVKKGVY-KMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEALMLVMEMASGGPL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  513 RSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-SKGKLP 590
Cdd:cd05115     91 NKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgADDSYYKArSAGKWP 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  591 IKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSR 670
Cdd:cd05115    171 LKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWED 250
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  671 RPRFtelkaqlstileeekAQQEERMRM 698
Cdd:cd05115    251 RPNF---------------LTVEQRMRT 263
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
421-686 1.32e-72

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: 241.91  E-value: 1.32e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITE 497
Cdd:cd05036      2 EVPRKNLTLIRALGQGAFGEVYEGTVsgMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVcFQR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFL-QVRKY-----SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLG 568
Cdd:cd05036     82 LPRFILLELMAGGDLKSFLrENRPRpeqpsSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGpgrVAKIG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  569 DFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLP 647
Cdd:cd05036    162 DFGMARDIYRADYYrKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRMD 241
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  648 MPPNCPPTLYSLMTKCWAYDPSRRPRFTelkaqlsTILE 686
Cdd:cd05036    242 PPKNCPGPVYRIMTQCWQHIPEDRPNFS-------TILE 273
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
420-684 2.85e-72

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: 240.41  E-value: 2.85e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSpenpALAVAIKTCKNcTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN- 498
Cdd:cd05148      1 WERPREEFTLERKLGSGYFGEVWEGLWKN----RVRVAIKILKS-DDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGe 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05148     76 PVYIITELMEKGSLLAFLRSPEgQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKgKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05148    156 EDVYLSSDK-KIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIY 234
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd05148    235 KIMLECWAAEPEDRPSFKALREELDNI 261
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
429-681 1.33e-71

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: 238.50  E-value: 1.33e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSpenpALAVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELC 507
Cdd:cd05059      8 FLKELGSGQFGVVHLGKWRG----KIDVAIKMIKEGSMS--EDDFIEEAKVMMKLSHPKLVQLYGVCTKQrPIFIVTEYM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd05059     82 ANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSVGT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYD 667
Cdd:cd05059    162 KFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEK 241
                          250
                   ....*....|....
gi 1914779978  668 PSRRPRFTELKAQL 681
Cdd:cd05059    242 PEERPTFKILLSQL 255
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
414-685 3.23e-71

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: 3.23e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  414 IDEARDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENP---ALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIV 489
Cdd:cd05053      1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKpneVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  490 KLIGVITEN-PVWIIMELCTLGELRSFLQVR-----KYSLD----------LASLILYAYQLSTALAYLESKRFVHRDIA 553
Cdd:cd05053     81 NLLGACTQDgPLYVVVEYASKGNLREFLRARrppgeEASPDdprvpeeqltQKDLVSFAYQVARGMEYLASKKCIHRDLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  554 ARNVLVSSNDCVKLGDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK 632
Cdd:cd05053    161 ARNVLVTEDNVMKIADFGLARDIHHIDYYrKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIP 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  633 NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05053    241 VEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRIL 293
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
421-685 3.93e-71

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: 3.93e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NP 499
Cdd:cd05063      1 EIHPSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKfKP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED- 578
Cdd:cd05063     81 AMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 -STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05063    161 pEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVY 240
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05063    241 QLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
419-681 2.43e-70

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: 235.17  E-value: 2.43e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITEN 498
Cdd:cd05067      1 EWEVPRETLKLVERLGAGQFGEVWMGYY----NGHTKVAIKSLKQGSMSP--DAFLAEANLMKQLQHQRLVRLYAVVTQE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05067     75 PIYIITEYMENGSLVDFLKTPSgIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05067    155 DNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELY 234
                          250       260
                   ....*....|....*....|....
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05067    235 QLMRLCWKERPEDRPTFEYLRSVL 258
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
419-685 9.14e-69

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: 232.93  E-value: 9.14e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRERIELGRCIGEGQFGDV--HQGIYMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMRQFD-HPHIVKLIG 493
Cdd:cd05099      6 KWEFPRDRLVLGKPLGEGCFGQVvrAEAYGIDKSRPdqTVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIINLLG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 VIT-ENPVWIIMELCTLGELRSFLQVRK-----YSLDLA----------SLILYAYQLSTALAYLESKRFVHRDIAARNV 557
Cdd:cd05099     86 VCTqEGPLYVIVEYAAKGNLREFLRARRppgpdYTFDITkvpeeqlsfkDLVSCAYQVARGMEYLESRRCIHRDLAARNV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  558 LVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDV 636
Cdd:cd05099    166 LVTEDNVMKIADFGLARGVHDIDYYKkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEEL 245
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  637 IGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05099    246 FKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
420-677 9.83e-69

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: 231.78  E-value: 9.83e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE 497
Cdd:cd05061      1 WEVSREKITLLRELGQGSFGMVYEGNArdIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 -NPVWIIMELCTLGELRSFLQVRKYSLD---------LASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:cd05061     81 gQPTLVVMELMAHGDLKSYLRSLRPEAEnnpgrppptLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 646
Cdd:cd05061    161 GDFGMTRDIYETDYYrKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYL 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  647 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd05061    241 DQPDNCPERVTDLMRMCWQFNPKMRPTFLEI 271
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
420-694 1.78e-68

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: 1.78e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSdSVrEKFLQEALTMRQFDHPHIVKLIGVIT-EN 498
Cdd:cd05072      2 WEIPRESIKLVKKLGAGQFGEVWMGYY----NNSTKVAVKTLKPGTM-SV-QAFLEEANLMKTLQHDKLVRLYAVVTkEE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05072     76 PIYIITEYMAKGSLLDFLKSDEGGkVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05072    156 DNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDELY 235
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEE 694
Cdd:cd05072    236 DIMKTCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQ 272
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
433-677 3.61e-68

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: 228.58  E-value: 3.61e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKT-CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPV-WIIMELCTLG 510
Cdd:cd13999      1 IGSGSFGEVYKGKWRGTD-----VAIKKlKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPlCIVTEYMPGG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK-GKL 589
Cdd:cd13999     76 SLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVvGTP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 piKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd13999    156 --RWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAaAVVQKGLRPPIPPDCPPELSKLIKRCWNEDP 232

                   ....*....
gi 1914779978  669 SRRPRFTEL 677
Cdd:cd13999    233 EKRPSFSEI 241
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
421-677 3.64e-68

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: 230.10  E-value: 3.64e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE- 497
Cdd:cd05050      1 EYPRNNIEYVRDIGQGAFGRVFQARApgLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVg 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQ----------------VRKYSLD-----LASLILYAYQLSTALAYLESKRFVHRDIAARN 556
Cdd:cd05050     81 KPMCLLFEYMAYGDLNEFLRhrspraqcslshstssARKCGLNplplsCTEQLCIAKQVAAGMAYLSERKFVHRDLATRN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  557 VLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK-LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNND 635
Cdd:cd05050    161 CLVGENMVVKIADFGLSRNIYSADYYKASENDaIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  636 VIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd05050    241 VIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
421-685 3.80e-68

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: 229.43  E-value: 3.80e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NP 499
Cdd:cd05064      1 ELDNKSIKIERILGTGRFGELCRGCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRgNT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGlsRYMED- 578
Cdd:cd05064     81 MMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFR--RLQEDk 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 -STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05064    159 sEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAPRNCPNLLH 238
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05064    239 QLMLDCWQKERGERPRFSQIHSILSKMV 266
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
431-700 8.63e-68

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: 230.29  E-value: 8.63e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTL 509
Cdd:cd05108     13 KVLGSGAFGTVYKGLWIPEgEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGK 588
Cdd:cd05108     93 GCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLgAEEKEYHAEGGK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05108    173 VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDA 252
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  669 SRRPRFTELKAQLSTILEEEK----AQQEERMRMES 700
Cdd:cd05108    253 DSRPKFRELIIEFSKMARDPQrylvIQGDERMHLPS 288
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
426-687 2.25e-67

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: 2.25e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIyMSPENPALAVAIKTCKN--CTSDSVrEKFLQEALTMRQFDHPHIVKLIGVITEN----- 498
Cdd:cd05075      1 KLALGKTLGEGEFGSVMEGQ-LNQDDSVLKVAVKTMKIaiCTRSEM-EDFLSEAVCMKEFDHPNVMRLIGVCLQNteseg 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 ---PVwIIMELCTLGELRSFLQVRKYS-----LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDF 570
Cdd:cd05075     79 ypsPV-VILPFMKHGDLHSFLLYSRLGdcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  571 GLSRYMEDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMP 649
Cdd:cd05075    158 GLSKKIYNGDYYRQGRiSKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQP 237
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1914779978  650 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEE 687
Cdd:cd05075    238 PDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
431-684 3.28e-67

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: 3.28e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTL 509
Cdd:cd05109     13 KVLGSGAFGTVYKGIWIPDgENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQLVTQLMPY 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYKASKGK 588
Cdd:cd05109     93 GCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDiDETEYHADGGK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05109    173 VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDS 252
                          250
                   ....*....|....*.
gi 1914779978  669 SRRPRFTELKAQLSTI 684
Cdd:cd05109    253 ECRPRFRELVDEFSRM 268
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
418-685 1.29e-66

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: 225.57  E-value: 1.29e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  418 RDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCK---NCTSDSvrEKFLQEALTMRQFDHPHIVKLIGV 494
Cdd:cd05074      2 KDVLIQEQQFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKadiFSSSDI--EEFLREAACMKEFDHPNVIKLIGV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITEN------PV-WIIMELCTLGELRSFLQVRK-----YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 562
Cdd:cd05074     80 SLRSrakgrlPIpMVILPFMKHGDLHTFLLMSRigeepFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNEN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  563 DCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE 641
Cdd:cd05074    160 MTVCVADFGLSKKIYSGDYYRqGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLI 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1914779978  642 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05074    240 KGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
429-685 1.41e-66

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: 1.41e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCK--NCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVITE--------N 498
Cdd:cd05035      3 LGKILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKvdIHTYSEI-EEFLSEAACMKDFDHPNVMRLIGVCFTasdlnkppS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVwIIMELCTLGELRSFLQVRK-----YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd05035     82 PM-VILPFMKHGDLHSYLLYSRlgglpEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNC 652
Cdd:cd05035    161 RKIYSGDYYRQGRiSKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRLKQPEDC 240
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05035    241 LDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
421-681 6.53e-66

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: 223.50  E-value: 6.53e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 498
Cdd:cd05049      1 HIKRDTIVLKRELGEGAFGKVFLGecYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWI-IMELCTLGELRSFLQ-------------VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 564
Cdd:cd05049     81 DPLLmVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  565 VKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENG 643
Cdd:cd05049    161 VKIGDFGMSRDIYSTDYYRvGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECITQG 240
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1914779978  644 ERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05049    241 RLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRL 278
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
431-687 6.98e-66

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: 222.73  E-value: 6.98e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI--TENPVWIIMELCT 508
Cdd:cd05058      1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIClpSEGSPLVVLPYMK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK-- 586
Cdd:cd05058     81 HGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNht 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 -GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 665
Cdd:cd05058    161 gAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                          250       260
                   ....*....|....*....|..
gi 1914779978  666 YDPSRRPRFTELKAQLSTILEE 687
Cdd:cd05058    241 PKPEMRPTFSELVSRISQIFST 262
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
425-683 2.43e-65

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: 220.90  E-value: 2.43e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKnCtsDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM 504
Cdd:cd05083      6 QKLTLGEIIGEGEFGAVLQGEYMGQK-----VAVKNIK-C--DVTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLYIVM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymedSTYYK 583
Cdd:cd05083     78 ELMSKGNLVNFLRSRGRALvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK----VGSMG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:cd05083    154 VDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSC 233
                          250       260
                   ....*....|....*....|
gi 1914779978  664 WAYDPSRRPRFTELKAQLST 683
Cdd:cd05083    234 WEAEPGKRPSFKKLREKLEK 253
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
418-700 1.15e-64

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: 221.09  E-value: 1.15e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  418 RDYEIQRERIelgrcIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT 496
Cdd:cd05110      5 KETELKRVKV-----LGSGAFGTVYKGIWVPEgETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 576
Cdd:cd05110     80 SPTIQLVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 E-DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPT 655
Cdd:cd05110    160 EgDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTID 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  656 LYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEK----AQQEERMRMES 700
Cdd:cd05110    240 VYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQrylvIQGDDRMKLPS 288
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
419-686 1.26e-64

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: 220.19  E-value: 1.26e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE 497
Cdd:cd14204      1 DVMIDRNLLSLGKVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKlDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 -------NPVwIIMELCTLGELRSFLQVRKYSLD-----LASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV 565
Cdd:cd14204     81 vgsqripKPM-VILPFMKYGDLHSFLLRSRLGSGpqhvpLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  566 KLGDFGLSRYMEDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGE 644
Cdd:cd14204    160 CVADFGLSKKIYSGDYYRQGRiAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGH 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  645 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14204    240 RLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLE 281
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
421-677 1.75e-64

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: 220.29  E-value: 1.75e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVH-------------QGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPH 487
Cdd:cd05051      1 EFPREKLEFVEKLGEGQFGEVHlceanglsdltsdDFIGNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  488 IVKLIGVITENPVW-IIMELCTLGELRSFLQVR-----------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAAR 555
Cdd:cd05051     81 IVRLLGVCTRDEPLcMIVEYMENGDLNQFLQKHeaetqgasatnSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  556 NVLVSSNDCVKLGDFGLSRYMEDSTYYKAsKGK--LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVK-PFQGVK 632
Cdd:cd05051    161 NCLVGPNYTIKIADFGMSRNLYSGDYYRI-EGRavLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKEqPYEHLT 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  633 NNDVigrIEN--------GER--LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd05051    240 DEQV---IENageffrddGMEvyLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
428-681 2.29e-64

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: 219.50  E-value: 2.29e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCigegQFGDVHQG-IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIME 505
Cdd:cd05090     12 ELGEC----AFGKIYKGhLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTqEQPVCMLFE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVR----------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 569
Cdd:cd05090     88 FMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  570 FGLSRYMEDSTYYKA-SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPM 648
Cdd:cd05090    168 LGLSREIYSSDYYRVqNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPC 247
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1914779978  649 PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05090    248 SEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
420-684 6.79e-64

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: 6.79e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNctsDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd05082      1 WALNMKELKLLQTIGKGEFGDVMLGDYRGNK-----VAVKCIKN---DATAQAFLAEASVMTQLRHSNLVQLLGVIVEEK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 --VWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRym 576
Cdd:cd05082     73 ggLYIVTEYMAKGSLVDYLRSRGRSvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTyyKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTL 656
Cdd:cd05082    151 EASS--TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAV 228
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd05082    229 YDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
421-683 7.08e-64

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: 7.08e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-E 497
Cdd:cd05091      2 EINLSAVRFMEELGEDRFGKVYKGhlFGTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTkE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQVR---------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 562
Cdd:cd05091     82 QPMSMIFSYCSHGDLHEFLVMRsphsdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  563 DCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE 641
Cdd:cd05091    162 LNVKISDLGLFREVYAADYYKlMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIR 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  642 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 683
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 ...
433-681 3.46e-63

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: 214.78  E-value: 3.46e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 512
Cdd:cd14203      3 LGQGCFGEVWMGTW----NGTTKVAIKTLKPGTMSP--EAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  513 RSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd14203     77 LDFLKDGEgKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 KWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd14203    157 KWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEER 236
                          250
                   ....*....|
gi 1914779978  672 PRFTELKAQL 681
Cdd:cd14203    237 PTFEYLQSFL 246
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
420-677 9.46e-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: 211.82  E-value: 9.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE 497
Cdd:cd05062      1 WEVAREKITMSRELGQGSFGMVYEGIAkgVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 -NPVWIIMELCTLGELRSFLQVRKYSLD---------LASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:cd05062     81 gQPTLVIMELMTRGDLKSYLRSLRPEMEnnpvqappsLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 646
Cdd:cd05062    161 GDFGMTRDIYETDYYrKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLL 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  647 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd05062    241 DKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
420-677 1.14e-61

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: 212.35  E-value: 1.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVIT 496
Cdd:cd05055     30 WEFPRNNLSFGKTLGAGAFGKVVEATAygLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACT 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 EN-PVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd05055    110 IGgPILVITEYCCYGDLLNFLRRKRESfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 -YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNC 652
Cdd:cd05055    190 dIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMPvDSKFYKLIKEGYRMAQPEHA 269
                          250       260
                   ....*....|....*....|....*
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd05055    270 PAEIYDIMKTCWDADPLKRPTFKQI 294
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
433-682 1.64e-61

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: 1.64e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalaVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 511
Cdd:cd05112     12 IGSGQFGLVHLGYWLNKDK----VAIKTIREGAMS--EEDFIEEAEVMMKLSHPKLVQLYGVCLEQaPICLVFEFMEHGC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd05112     86 LSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFPV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 KWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05112    166 KWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERPEDR 245
                          250
                   ....*....|.
gi 1914779978  672 PRFTELKAQLS 682
Cdd:cd05112    246 PSFSLLLRQLA 256
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
428-679 2.38e-61

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 209.69  E-value: 2.38e-61
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   428 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:smart00220    2 EILEKLGEGSFGKVYLARDKKTGKL---VAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFeDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   507 CTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:smart00220   79 CEGGDLFDLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   587 GKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPP---NCPPTLYSLMTKC 663
Cdd:smart00220  158 GTPE--YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKIGKPKPPFPPpewDISPEAKDLIRKL 234
                           250
                    ....*....|....*.
gi 1914779978   664 WAYDPSRRPRFTELKA 679
Cdd:smart00220  235 LVKDPEKRLTAEEALQ 250
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
416-681 1.91e-60

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: 207.57  E-value: 1.91e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  416 EARDYEIQRERIELGRCIGEGQFGDVhqgiYMSPENPALAVAIKTCKNCTSdSVrEKFLQEALTMRQFDHPHIVKLIGVI 495
Cdd:cd05073      2 EKDAWEIPRESLKLEKKLGAGQFGEV----WMATYNKHTKVAVKTMKPGSM-SV-EAFLAEANVMKTLQHDKLVKLHAVV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd05073     76 TKEPIYIITEFMAKGSLLDFLKSDEGSkQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLAR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPP 654
Cdd:cd05073    156 VIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPE 235
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  655 TLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05073    236 ELYNIMMRCWKNRPEERPTFEYIQSVL 262
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
422-681 1.29e-59

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: 1.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVH--QGIYMSPENPALAVAIKTCKNCTsDSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 498
Cdd:cd05092      2 IKRRDIVLKWELGEGAFGKVFlaECHNLLPEQDKMLVAVKALKEAT-ESARQDFQREAELLTVLQHQHIVRFYGVCTEgE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQ--------------VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 564
Cdd:cd05092     81 PLIMVFEYMRHGDLNRFLRshgpdakildggegQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  565 VKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENG 643
Cdd:cd05092    161 VKIGDFGMSRDIYSTDYYRvGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQG 240
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1914779978  644 ERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05092    241 RELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRL 278
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
426-685 2.40e-59

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: 205.58  E-value: 2.40e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPA--LAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWI 502
Cdd:cd05045      1 NLVLGKTLGEGEFGKVVKATAFRLKGRAgyTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDgPLLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLQV-RKY----------------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV 559
Cdd:cd05045     81 IVEYAKYGSLRSFLREsRKVgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  560 SSNDCVKLGDFGLSR--YMEDStYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVI 637
Cdd:cd05045    161 AEGRKMKISDFGLSRdvYEEDS-YVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLF 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1914779978  638 GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05045    240 NLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
420-693 6.74e-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: 203.77  E-value: 6.74e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd05071      4 WEIPRESLRLEVKLGQGCFGEVWMGTW----NGTTRVAIKTLKPGTMSP--EAFLQEAQVMKKLRHEKLVQLYAVVSEEP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFL--QVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05071     78 IYIVTEYMSKGSLLDFLkgEMGKY-LRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 657
Cdd:cd05071    157 DNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLH 236
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQE 693
Cdd:cd05071    237 DLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQ 272
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
408-685 1.03e-58

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 204.48  E-value: 1.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  408 PSKSYGIDEARDYEIQRERIELGRCIGEGQFGDV--HQGIYMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMRQF 483
Cdd:cd05101      7 GVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVvmAEAVGIDKDKPkeAVTVAVKMLKDDATEKDLSDLVSEMEMMKMI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  484 -DHPHIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-----YSLDLA----------SLILYAYQLSTALAYLESKR 546
Cdd:cd05101     87 gKHKNIINLLGACTQDgPLYVIVEYASKGNLREYLRARRppgmeYSYDINrvpeeqmtfkDLVSCTYQLARGMEYLASQK 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  547 FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGV 625
Cdd:cd05101    167 CIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGG 246
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  626 KPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05101    247 SPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
433-681 1.28e-58

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: 200.57  E-value: 1.28e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 511
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKK---VAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVfETENFLYLVMEYCEGGS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGKLP 590
Cdd:cd00180     78 LKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLdSDDSLLKTTGGTTP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  591 IKWMAPESINFRRFTSASDVWMFGVCMWEIlmhgvkpfqgvknndvigriengerlpmppncpPTLYSLMTKCWAYDPSR 670
Cdd:cd00180    158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPKK 204
                          250
                   ....*....|.
gi 1914779978  671 RPRFTELKAQL 681
Cdd:cd00180    205 RPSAKELLEHL 215
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
420-692 1.30e-58

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: 203.71  E-value: 1.30e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDV--HQGIYMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGV 494
Cdd:cd05098      8 WELPRDRLVLGKPLGEGCFGQVvlAEAIGLDKDKPnrVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITEN-PVWIIMELCTLGELRSFLQVRK-----YS----------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL 558
Cdd:cd05098     88 CTQDgPLYVIVEYASKGNLREYLQARRppgmeYCynpshnpeeqLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  559 VSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVI 637
Cdd:cd05098    168 VTEDNVMKIADFGLARDIHHIDYYKkTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELF 247
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  638 GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQ 692
Cdd:cd05098    248 KLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQE 302
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
430-682 1.58e-58

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: 202.88  E-value: 1.58e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIYMsPENPALA--VAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELC 507
Cdd:cd05111     12 LKVLGSGVFGTVHKGIWI-PEGDSIKipVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQLVTQLL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR--YMEDSTYYkAS 585
Cdd:cd05111     91 PLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADllYPDDKKYF-YS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 665
Cdd:cd05111    170 EAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWM 249
                          250
                   ....*....|....*..
gi 1914779978  666 YDPSRRPRFTELKAQLS 682
Cdd:cd05111    250 IDENIRPTFKELANEFT 266
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
420-693 1.25e-57

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: 199.91  E-value: 1.25e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd05070      4 WEIPRESLQLIKRLGNGQFGEVWMGTW----NGNTKVAIKTLKPGTMSP--ESFLEEAQIMKKLKHDKLVQLYAVVSEEP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd05070     78 IYIVTEYMSKGSLLDFLKDGEgRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIED 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYS 658
Cdd:cd05070    158 NEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHE 237
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1914779978  659 LMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQE 693
Cdd:cd05070    238 LMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQ 272
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
420-685 2.93e-57

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: 201.02  E-value: 2.93e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQ----GIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGV 494
Cdd:cd05100      7 WELSRTRLTLGKPLGEGCFGQVVMaeaiGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITEN-PVWIIMELCTLGELRSFLQVRK-----YSLD----------LASLILYAYQLSTALAYLESKRFVHRDIAARNVL 558
Cdd:cd05100     87 CTQDgPLYVLVEYASKGNLREYLRARRppgmdYSFDtcklpeeqltFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  559 VSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVI 637
Cdd:cd05100    167 VTEDNVMKIADFGLARDVHNIDYYKkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1914779978  638 GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05100    247 KLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVL 294
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
417-693 3.88e-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: 198.76  E-value: 3.88e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  417 ARD-YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVI 495
Cdd:cd05069      3 AKDaWEIPRESLRLDVKLGQGCFGEVWMGTW----NGTTKVAIKTLKPGTMMP--EAFLQEAQIMKKLRHDKLVPLYAVV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQVR--KYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd05069     77 SEEPIYIVTEFMGKGSLLDFLKEGdgKY-LKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCP 653
Cdd:cd05069    156 RLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCP 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  654 PTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQE 693
Cdd:cd05069    236 ESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQ 275
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
420-682 3.99e-57

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: 199.64  E-value: 3.99e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQ----GIYMSPEnpALAVAIKTCKNCTSDSVREKFLQEaltMRQFDH--PH--IVKL 491
Cdd:cd05054      2 WEFPRDRLKLGKPLGRGAFGKVIQasafGIDKSAT--CRTVAVKMLKEGATASEHKALMTE---LKILIHigHHlnVVNL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  492 IGVIT--ENPVWIIMELCTLGELRSFLQVR-------------------------KYSLDLASLILYAYQLSTALAYLES 544
Cdd:cd05054     77 LGACTkpGGPLMVIVEFCKFGNLSNYLRSKreefvpyrdkgardveeeedddelyKEPLTLEDLICYSFQVARGMEFLAS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  545 KRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMH 623
Cdd:cd05054    157 RKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSL 236
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  624 GVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 682
Cdd:cd05054    237 GASPYPGVQmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKLG 296
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
433-682 8.38e-57

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: 197.69  E-value: 8.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiYMSP---ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 508
Cdd:cd05046     13 LGRGEFGEVFLA-KAKGieeEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREaEPHYMILEYTD 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLAS--------LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 580
Cdd:cd05046     92 LGDLKQFLRATKSKDEKLKppplstkqKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYNSE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSL 659
Cdd:cd05046    172 YYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGKlELPVPEGCPSRLYKL 251
                          250       260
                   ....*....|....*....|...
gi 1914779978  660 MTKCWAYDPSRRPRFTELKAQLS 682
Cdd:cd05046    252 MTRCWAVNPKDRPSFSELVSALG 274
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
422-685 1.12e-56

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: 196.64  E-value: 1.12e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVHQGIYMSPENpalaVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVIT-ENPV 500
Cdd:cd05113      1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYD----VAIKMIKEGSMS--EDEFIEEAKVMMNLSHEKLVQLYGVCTkQRPI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 580
Cdd:cd05113     75 FIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLM 660
Cdd:cd05113    155 YTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIM 234
                          250       260
                   ....*....|....*....|....*
gi 1914779978  661 TKCWAYDPSRRPRFTELkaqLSTIL 685
Cdd:cd05113    235 YSCWHEKADERPTFKIL---LSNIL 256
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
422-682 9.11e-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: 194.98  E-value: 9.11e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN--P 499
Cdd:cd05043      3 VSRERVTLSDLLQEGTFGRIFHGILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDgeK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKY-------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd05043     83 PMVLYPYMNWGNLKLFLQQCRLseannpqALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNAL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGK-LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPN 651
Cdd:cd05043    163 SRDLFPMDYHCLGDNEnRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPIN 242
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 682
Cdd:cd05043    243 CPDELFAVMACCWALDPEERPSFQQLVQCLT 273
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
431-686 3.86e-55

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 192.38  E-value: 3.86e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSpenpALAVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTL 509
Cdd:cd05114     10 KELGSGLFGVVRLGKWRA----QYKVAIKAIRE--GAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQkPIYIVTEFMEN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 589
Cdd:cd05114     84 GCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKF 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPS 669
Cdd:cd05114    164 PVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWHEKPE 243
                          250
                   ....*....|....*..
gi 1914779978  670 RRPRFTELKAQLSTILE 686
Cdd:cd05114    244 GRPTFADLLRTITEIAE 260
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
423-686 2.59e-53

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: 188.18  E-value: 2.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  423 QRERIELGRCIGEGQFGDVHQGIYmSPENPALA--VAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE--- 497
Cdd:cd05080      2 HKRYLKKIRDLGEGHFGKVSLYCY-DPTNDGTGemVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgg 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM- 576
Cdd:cd05080     81 KSLQLIMEYVPLGSLRDYLP--KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVp 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHG-------------VKPFQGVKNN-DVIGRIE 641
Cdd:cd05080    159 EGHEYYRVREdGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCdssqspptkflemIGIAQGQMTVvRLIELLE 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  642 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd05080    239 RGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
433-684 3.66e-53

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: 187.53  E-value: 3.66e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmSP--ENPALAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELC 507
Cdd:cd14205     12 LGKGNFGSVEMCRY-DPlqDNTGEVVAVKKLQHSTEEHLRD-FEREIEILKSLQHDNIVKYKGVCysaGRRNLRLIMEYL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASK 586
Cdd:cd14205     90 PYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLpQDKEYYKVKE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 -GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKP------FQGVKNNDVIGR---------IENGERLPMPP 650
Cdd:cd14205    170 pGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSksppaeFMRMIGNDKQGQmivfhlielLKNNGRLPRPD 249
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1914779978  651 NCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14205    250 GCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
422-684 4.20e-53

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: 4.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVH--QGIYMSPENPALAVAIKTCKNcTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 498
Cdd:cd05093      2 IKRHNIVLKRELGEGAFGKVFlaECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEgD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRK------------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 566
Cdd:cd05093     81 PLIMVFEYMKHGDLNKFLRAHGpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  567 LGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER 645
Cdd:cd05093    161 IGDFGMSRDVYSTDYYRvGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 240
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  646 LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd05093    241 LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNL 279
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
420-687 7.11e-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: 185.95  E-value: 7.11e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVIT 496
Cdd:cd05102      2 WEFPRDRLRLGKVLGHGAFGKVVEAsaFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 E--NPVWIIMELCTLGELRSFL-------------------QVR------------------------------------ 519
Cdd:cd05102     82 KpnGPLMVIVEFCKYGNLSNFLrakregfspyrersprtrsQVRsmveavradrrsrqgsdrvasftestsstnqprqev 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  520 ----KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGKLPIKWM 594
Cdd:cd05102    162 ddlwQSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGSARLPLKWM 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  595 APESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPR 673
Cdd:cd05102    242 APESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPT 321
                          330
                   ....*....|....
gi 1914779978  674 FTELKAQLSTILEE 687
Cdd:cd05102    322 FSDLVEILGDLLQE 335
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
421-683 1.28e-51

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: 1.28e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVH--------QGIYMSP----ENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHI 488
Cdd:cd05097      1 EFPRQQLRLKEKLGEGQFGEVHlceaeglaEFLGEGApefdGQPVL-VAVKMLRADVTKTARNDFLKEIKIMSRLKNPNI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  489 VKLIGV-ITENPVWIIMELCTLGELRSFLQVRKY-----------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARN 556
Cdd:cd05097     80 IRLLGVcVSDDPLCMITEYMENGDLNQFLSQREIestfthannipSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  557 VLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL-MHGVKPFQGVKNN 634
Cdd:cd05097    160 CLVGNHYTIKIADFGMSRNLYSGDYYRiQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFtLCKEQPYSLLSDE 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  635 DVigrIEN-GE---------RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 683
Cdd:cd05097    240 QV---IENtGEffrnqgrqiYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
FERM_N_2 pfam18038
FERM N-terminal domain; This entry represents the FERM N-terminal domain found in focal ...
35-130 1.88e-51

FERM N-terminal domain; This entry represents the FERM N-terminal domain found in focal adhesion kinases.


Pssm-ID: 436229  Cd Length: 99  Bit Score: 175.72  E-value: 1.88e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   35 RVLKVFHYFESNSEPTtWASIIRHGDATDVRGIIQKI---VDSHKV-KHVACYGFRLSHLRSEEVHWLHVDMGVSSVREK 110
Cdd:pfam18038    1 RILKVCHYSESNNEGK-WFKLIRCGDATDVRGIIQKIlssGRIGPViRHVSCYGLRLKHLKSDEVHWLHPDMTVSEVREK 79
                           90       100
                   ....*....|....*....|
gi 1914779978  111 YELAHPPEEWKYELRIRYLP 130
Cdd:pfam18038   80 YEQQHPEAEWRYDLRIRYLP 99
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
420-684 2.06e-51

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: 2.06e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQ----GIYMSPEnpALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHP-HIVKLIGV 494
Cdd:cd14207      2 WEFARERLKLGKSLGRGAFGKVVQasafGIKKSPT--CRVVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLLGA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITEN--PVWIIMELCTLGELRSFLQVR----------------------------------------------------- 519
Cdd:cd14207     80 CTKSggPLMVIVEYCKYGNLSNYLKSKrdffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedksl 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  520 --------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA 584
Cdd:cd14207    160 sdveeeeedsgdfyKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIyKNPDYVRK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:cd14207    240 GDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQiDEDFCSKLKEGIRMRAPEFATSEIYQIMLDC 319
                          330       340
                   ....*....|....*....|.
gi 1914779978  664 WAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14207    320 WQGDPNERPRFSELVERLGDL 340
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
431-685 2.17e-51

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: 182.44  E-value: 2.17e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYmSPE--NPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE---NPVWIIME 505
Cdd:cd05079     10 RDLGEGHFGKVELCRY-DPEgdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdggNGIKLIME 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd05079     89 FLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHG-------------VKPFQG-VKNNDVIGRIENGERLPMP 649
Cdd:cd05079    169 KDDLdsPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCdsesspmtlflkmIGPTHGqMTVTRLVRVLEEGKRLPRP 248
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  650 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05079    249 PNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
422-681 1.84e-50

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: 180.21  E-value: 1.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVH--QGIYMSPENPALAVAIKTCKNCTSdSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 498
Cdd:cd05094      2 IKRRDIVLKRELGEGAFGKVFlaECYNLSPTKDKMLVAVKTLKDPTL-AARKDFQREAELLTNLQHDHIVKFYGVCGDgD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVR---------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND 563
Cdd:cd05094     81 PLIMVFEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  564 CVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIEN 642
Cdd:cd05094    161 LVKIGDFGMSRDVYSTDYYRvGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 240
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  643 GERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05094    241 GRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKIL 279
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
421-682 2.25e-50

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: 180.52  E-value: 2.25e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIYMSPEN-------------PALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPH 487
Cdd:cd05096      1 KFPRGHLLFKEKLGEGQFGEVHLCEVVNPQDlptlqfpfnvrkgRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  488 IVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKY------------------SLDLASLILYAYQLSTALAYLESKRFV 548
Cdd:cd05096     81 IIRLLGVcVDEDPLCMITEYMENGDLNQFLSSHHLddkeengndavppahclpAISYSSLLHVALQIASGMKYLSSLNFV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS-KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMH-GVK 626
Cdd:cd05096    161 HRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQgRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKEQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  627 PFQGVKNNDVI---GRI--ENGER--LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 682
Cdd:cd05096    241 PYGELTDEQVIenaGEFfrDQGRQvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFLT 303
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
421-681 1.22e-49

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: 1.22e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVH----QGIY----------MSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHP 486
Cdd:cd05095      1 EFPRKLLTFKEKLGEGQFGEVHlceaEGMEkfmdkdfaleVSENQPVL-VAVKMLRADANKNARNDFLKEIKIMSRLKDP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  487 HIVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKYSLDLAS-----------LILYAYQLSTALAYLESKRFVHRDIAA 554
Cdd:cd05095     80 NIIRLLAVcITDDPLCMITEYMENGDLNQFLSRQQPEGQLALpsnaltvsysdLRFMAAQIASGMKYLSSLNFVHRDLAT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  555 RNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL-MHGVKPFQGVK 632
Cdd:cd05095    160 RNCLVGKNYTIKIADFGMSRNLYSGDYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLtFCREQPYSQLS 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  633 NNDVigrIEN-GE---------RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
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 ...
433-681 1.38e-49

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: 1.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmSP--ENPALAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELC 507
Cdd:cd05081     12 LGKGNFGSVELCRY-DPlgDNTGALVAVKQLQHSGPDQQRD-FQREIQILKALHSDFIVKYRGVSygpGRRSLRLVMEYL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-S 585
Cdd:cd05081     90 PSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpLDKDYYVVrE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEI----------------LMHGVKPFQGVKNndVIGRIENGERLPMP 649
Cdd:cd05081    170 PGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELftycdkscspsaeflrMMGCERDVPALCR--LLELLEEGQRLPAP 247
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  650 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd05081    248 PACPAEVHELMKLCWAPSPQDRPSFSALGPQL 279
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
420-686 2.04e-49

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: 2.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAL--AVAIKTCKNCTSDSVREKFLQEALTMRQFDHP-HIVKLIGVIT 496
Cdd:cd05103      2 WEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATcrTVAVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLLGACT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 E--NPVWIIMELCTLGELRSFLQVR------------------------------------------------------- 519
Cdd:cd05103     82 KpgGPLMVIVEFCKFGNLSAYLRSKrsefvpyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsdv 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  520 -----------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKG 587
Cdd:cd05103    162 eeeeagqedlyKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGDA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAY 666
Cdd:cd05103    242 RLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKiDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHG 321
                          330       340
                   ....*....|....*....|
gi 1914779978  667 DPSRRPRFTELKAQLSTILE 686
Cdd:cd05103    322 EPSQRPTFSELVEHLGNLLQ 341
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
433-686 1.30e-48

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: 1.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIyMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVITENP-VWIIMELCTLG 510
Cdd:cd05047      3 IGEGNFGQVLKAR-IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGyLYLAIEYAPHG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKY---------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 575
Cdd:cd05047     82 NLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEdsTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPT 655
Cdd:cd05047    162 QE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDE 239
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  656 LYSLMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd05047    240 VYDLMRQCWREKPYERPSFAQILVSLNRMLE 270
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
425-690 2.32e-48

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: 2.32e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIyMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGViTENP--VW 501
Cdd:cd05089      2 EDIKFEDVIGEGNFGQVIKAM-IKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGA-CENRgyLY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRKY---------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 566
Cdd:cd05089     80 IAIEYAPYGNLLDFLRKSRVletdpafakehgtasTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  567 LGDFGLSRYMEdsTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 646
Cdd:cd05089    160 IADFGLSRGEE--VYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRM 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1914779978  647 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKA 690
Cdd:cd05089    238 EKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKA 281
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
426-677 3.42e-48

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 172.32  E-value: 3.42e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGiyMSPENPALaVAIKT--CKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGV-ITENPVWI 502
Cdd:cd06606      1 RWKKGELLGKGSFGSVYLA--LNLDTGEL-MAVKEveLSGDSEEELEA-LEREIRILSSLKHPNIVRYLGTeRTENTLNI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLqvRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd06606     77 FLEYVPGGSLASLL--KKFgKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIAT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASK---GKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN-DVIGRIENGERLP-MPPNCPPTL 656
Cdd:cd06606    155 GEGTKslrGTPY--WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNPvAALFKIGSSGEPPpIPEHLSEEA 231
                          250       260
                   ....*....|....*....|.
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06606    232 KDFLRKCLQRDPKKRPTADEL 252
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
426-683 1.15e-46

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: 168.15  E-value: 1.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWI 502
Cdd:cd14014      1 RYRLVRLLGRGGMGEVYRARDTLLGRP---VAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDgRPYI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 582
Cdd:cd14014     78 VMEYVEGGSLADLLR-ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPMP---PNCPPTLYSL 659
Cdd:cd14014    157 QTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYE-LLTGRPPFDGDSPAAVLAKHLQEAPPPPSplnPDVPPALDAI 235
                          250       260
                   ....*....|....*....|....*
gi 1914779978  660 MTKCWAYDPSRRPR-FTELKAQLST 683
Cdd:cd14014    236 ILRALAKDPEERPQsAAELLAALRA 260
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
420-688 5.30e-46

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: 170.03  E-value: 5.30e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVIT 496
Cdd:cd05106     33 WEFPRDNLQFGKTLGAGAFGKVVEATAfgLGKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLgQHKNIVNLLGACT 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 EN-PVWIIMELCTLGELRSFLQ--------------------------------VRKYS--------------------- 522
Cdd:cd05106    113 HGgPVLVITEYCCYGDLLNFLRkkaetflnfvmalpeisetssdyknitlekkyIRSDSgfssqgsdtyvemrpvsssss 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  523 ----------------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKAS 585
Cdd:cd05106    193 qssdskdeedtedswpLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARdIMNDSNYVVKG 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd05106    273 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILvNSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCW 352
                          330       340
                   ....*....|....*....|....
gi 1914779978  665 AYDPSRRPRFTelkaQLSTILEEE 688
Cdd:cd05106    353 NLEPTERPTFS----QISQLIQRQ 372
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
420-685 1.02e-44

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: 167.12  E-value: 1.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFD-HPHIVKLIGVIT 496
Cdd:cd05105     32 WEFPRDGLVLGRILGSGAFGKVVEGTAygLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGpHLNIVNLLGACT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 EN-PVWIIMELCTLGELRSFL----------------------------------------------------------- 516
Cdd:cd05105    112 KSgPIYIITEYCFYGDLVNYLhknrdnflsrhpekpkkdldifginpadestrsyvilsfenkgdymdmkqadttqyvpm 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  517 ----QVRKYS--------------------------------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS 560
Cdd:cd05105    192 leikEASKYSdiqrsnydrpasykgsndsevknllsddgsegLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLA 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  561 SNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQG-VKNNDVIG 638
Cdd:cd05105    272 QGKIVKICDFGLARdIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGmIVDSTFYN 351
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1914779978  639 RIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05105    352 KIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
421-731 2.78e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 2.78e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 498
Cdd:COG0515      3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRP---VALKVLRPelAADPEARERFRREARALARLNHPNIVRVYDVGEED 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PV-WIIMELCTlGE-LRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 576
Cdd:COG0515     80 GRpYLVMEYVE-GEsLADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTYYKAS--KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPMP---PN 651
Cdd:COG0515    158 GGATLTQTGtvVGTPG--YMAPEQARGEPVDPRSDVYSLGVTLYE-LLTGRPPFDGDSPAELLRAHLREPPPPPSelrPD 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRS 730
Cdd:COG0515    235 LPPALDAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 314

                   .
gi 1914779978  731 S 731
Cdd:COG0515    315 A 315
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
433-686 3.06e-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: 3.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKnctSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTLGE 511
Cdd:cd14058      1 VGRGSFGVVCKARWRNQI-----VAVKIIE---SESEKKAFEVEVRQLSRVDHPNIIKLYGaCSNQKPVCLVMEYAEGGS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFL--QVRKYSLDLASLILYAYQLSTALAYLES---KRFVHRDIAARNVLVSSNDCV-KLGDFGLSRYMedSTYYKAS 585
Cdd:cd14058     73 LYNVLhgKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDI--STHMTNN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEIlMHGVKPFQGVKNND--VIGRIENGERLPMPPNCPPTLYSLMTKC 663
Cdd:cd14058    151 KGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEV-ITRRKPFDHIGGPAfrIMWAVHNGERPPLIKNCPKPIESLMTRC 227
                          250       260
                   ....*....|....*....|...
gi 1914779978  664 WAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14058    228 WSKDPEKRPSMKEIVKIMSHLMQ 250
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
428-679 1.40e-42

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: 156.14  E-value: 1.40e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYmspENPALAVAIKT-CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 505
Cdd:cd14003      3 ELGKTLGEGSFGKVKLARH---KLTGEKVAIKIiDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIeTENKIYLVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKY-SLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 584
Cdd:cd14003     80 YASGGELFDYIVNNGRlSEDEARRFFQ--QLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKLPikWMAPESINFRRF-TSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMTKC 663
Cdd:cd14003    158 FCGTPA--YAAPEVLLGRKYdGPKADVWSLGVILY-AMLTGYLPFDDDNDSKLFRKILKGK-YPIPSHLSPDARDLIRRM 233
                          250
                   ....*....|....*.
gi 1914779978  664 WAYDPSRRPRFTELKA 679
Cdd:cd14003    234 LVVDPSKRITIEEILN 249
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
422-689 1.64e-41

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: 154.77  E-value: 1.64e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELGRCIGEGQFGDVHQGiYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTM-RQFDHPHIVKLIGVITENP- 499
Cdd:cd05088      4 LEWNDIKFQDVIGEGNFGQVLKA-RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGy 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKY---------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 564
Cdd:cd05088     83 LYLAIEYAPHGNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  565 VKLGDFGLSRYMEdsTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGE 644
Cdd:cd05088    163 AKIADFGLSRGQE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  645 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEK 689
Cdd:cd05088    241 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERK 285
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
433-684 6.74e-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: 151.39  E-value: 6.74e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCK--NCTSDSV-REKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCT 508
Cdd:cd14061      2 IGVGGFGKVYRGIWRGEE-----VAVKAARqdPDEDISVtLENVRQEARLFWMLRHPNIIALRGVCLQPPnLCLVMEYAR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS--------SNDCVKLGDFGLSRYME 577
Cdd:cd14061     77 GGALNRVLA--GRKIPPHVLVDWAIQIARGMNYLHNEAPVpiiHRDLKSSNILILeaienedlENKTLKITDFGLAREWH 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE-NGERLPMPPNCPPTL 656
Cdd:cd14061    155 KTTRMSAAG---TYAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAvNKLTLPIPSTCPEPF 230
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14061    231 AQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
421-684 2.83e-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: 2.83e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDSVR---EKFLQEALTMRQFDHPHIVKLIGVITE 497
Cdd:cd14145      2 EIDFSELVLEEIIGIGGFGKVYRAIWIGDE-----VAVKAARHDPDEDISqtiENVRQEAKLFAMLKHPNIIALRGVCLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NP-VWIIMELCTLGELRSFLQVRKYSLDLasLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS--------SNDCV 565
Cdd:cd14145     77 EPnLCLVMEFARGGPLNRVLSGKRIPPDI--LVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILekvengdlSNKIL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  566 KLGDFGLSRYMEDSTYYKASKGklpIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGE 644
Cdd:cd14145    155 KITDFGLAREWHRTTKMSAAGT---YAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVAyGVAMNKL 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  645 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14145    231 SLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
429-677 3.28e-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: 3.28e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMspeNPALAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd06627      4 LGDLIGRGAFGSVYKGLNL---NTGEFVAIKQISlEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVkTKDSLYIILEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLqvRKYSLDLASLI-LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd06627     81 VENGSLASII--KKFGKFPESLVaVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 665
Cdd:cd06627    159 VVGTP-YWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDDHPPLPENISPELRDFLLQCFQ 236
                          250
                   ....*....|..
gi 1914779978  666 YDPSRRPRFTEL 677
Cdd:cd06627    237 KDPTLRPSAKEL 248
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
428-678 4.20e-40

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: 148.89  E-value: 4.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMEL 506
Cdd:cd05122      3 EILEKIGKGGFGVVYKARH---KKTGQIVAIKKINLESKEK-KESILNEIAILKKCKHPNIVKYYGsYLKKDELWIVMEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd05122     79 CSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTFV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQG---------VKNNDVIGriengerLPMPPNCPPTLY 657
Cdd:cd05122    159 GTPY--WMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKPPYSElppmkalflIATNGPPG-------LRNPKKWSKEFK 228
                          250       260
                   ....*....|....*....|.
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELK 678
Cdd:cd05122    229 DFLKKCLQKDPEKRPTAEQLL 249
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
36-258 1.33e-39

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 145.52  E-value: 1.33e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978    36 VLKVFHYFESNSEpttwasiIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKyelah 115
Cdd:smart00295    1 VLKVYLLDGTTLE-------FEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVK----- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978   116 pPEEWKYELRIRYLPKgFLNQFTEDKPTLNFFYQQVKSDYMLEIAdQVDQEIALKLGCLEIRRSYWEMRGNALEkksnye 195
Cdd:smart00295   69 -SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRL-PCPEEEALLLAALALQAEFGDYDEELHD------ 139
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978   196 vLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECF 258
Cdd:smart00295  140 -LRGELSLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
433-681 1.84e-39

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 146.49  E-value: 1.84e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKtcknctsdSVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELCTLGE 511
Cdd:cd14059      1 LGSGAQGAVFLGKFRGEE-----VAVK--------KVRDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYcILMEYCPYGQ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFL-QVRKYSLDLasLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlp 590
Cdd:cd14059     68 LYEVLrAGREITPSL--LVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGT-- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  591 IKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGERLPMPPNCPPTLYSLMTKCWAYDPS 669
Cdd:cd14059    144 VAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIwGVGSNSLQLPVPSTCPDGFKLLMKQCWNSKPR 222
                          250
                   ....*....|..
gi 1914779978  670 RRPRFTELKAQL 681
Cdd:cd14059    223 NRPSFRQILMHL 234
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
420-677 4.53e-39

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: 149.67  E-value: 4.53e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVIT 496
Cdd:cd05104     30 WEFPRDRLRFGKTLGAGAFGKVVEATAygLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLgNHINIVNLLGACT 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 -ENPVWIIMELCTLGELRSFLQVRKYS----------------------------------------------------- 522
Cdd:cd05104    110 vGGPTLVITEYCCYGDLLNFLRRKRDSficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvvptkadkrrgv 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  523 ---------------------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DST 580
Cdd:cd05104    190 rsgsyvdqdvtseileedelaLDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRnDSN 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSL 659
Cdd:cd05104    270 YVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPvDSKFYKMIKEGYRMDSPEFAPSEMYDI 349
                          330
                   ....*....|....*...
gi 1914779978  660 MTKCWAYDPSRRPRFTEL 677
Cdd:cd05104    350 MRSCWDADPLKRPTFKQI 367
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
420-685 1.85e-38

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: 148.62  E-value: 1.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFD-HPHIVKLIGVIT 496
Cdd:cd05107     32 WEMPRDNLVLGRTLGSGAFGRVVEATAhgLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLGpHLNIVNLLGACT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 EN-PVWIIMELCTLGELRSFLQVRKYS----------------------------------------LDLAS-------- 527
Cdd:cd05107    112 KGgPIYIITEYCRYGDLVDYLHRNKHTflqyyldknrddgslisggstplsqrkshvslgsesdggyMDMSKdesadyvp 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  528 -------------------------------------------------LILYAYQLSTALAYLESKRFVHRDIAARNVL 558
Cdd:cd05107    192 mqdmkgtvkyadiessnyespydqylpsapertrrdtlinespalsymdLVGFSYQVANGMEFLASKNCVHRDLAARNVL 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  559 VSSNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVI 637
Cdd:cd05107    272 ICEGKLVKICDFGLARdIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQF 351
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  638 -GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd05107    352 yNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
428-679 7.14e-37

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: 139.53  E-value: 7.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHqgiymspenpaLA--------VAIKT------CKNCTSDSVRekflQEALTMRQFDHPHIVKLIG 493
Cdd:cd14007      3 EIGKPLGKGKFGNVY-----------LArekksgfiVALKVisksqlQKSGLEHQLR----REIEIQSHLRHPNILRLYG 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 V-ITENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 571
Cdd:cd14007     68 YfEDKKRIYLILEYAPNGELYKELKkQKRFDEKEAAK--YIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  572 LSRYMEDS-------TY-YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENG 643
Cdd:cd14007    146 WSVHAPSNrrktfcgTLdY-----------LPPEMVEGKEYDYKVDIWSLGVLCYELL-VGKPPFESKSHQETYKRIQNV 213
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  644 ErLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKA 679
Cdd:cd14007    214 D-IKFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
419-672 8.47e-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: 139.52  E-value: 8.47e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHqgiymspenpaLAVAIKTCKNCT---------SDSVREKFLQEALTMRQFDHPHIV 489
Cdd:cd08215      1 KYEKIRV-------IGKGSFGSAY-----------LVRRKSDGKLYVlkeidlsnmSEKEREEALNEVKLLSKLKHPNIV 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  490 KLIGVITENPV-WIIMELCTLGELRSFLQVRKYSLDL--ASLILYAY-QLSTALAYLESKRFVHRDIAARNVLVSSNDCV 565
Cdd:cd08215     63 KYYESFEENGKlCIVMEYADGGDLAQKIKKQKKKGQPfpEEQILDWFvQICLALKYLHSRKILHRDLKTQNIFLTKDGVV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  566 KLGDFGLSRYMEDST----------YYkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMHgVKPFQGVKNND 635
Cdd:cd08215    143 KLGDFGISKVLESTTdlaktvvgtpYY-----------LSPELCENKPYNYKSDIWALGCVLYELCTL-KHPFEANNLPA 210
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1914779978  636 VIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd08215    211 LVYKIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRP 247
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
434-684 1.82e-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: 1.82e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  434 GEGQFGDVHQGIYMSPENpalAVAIKtcknctsdsvreKFLQ---EALTMRQFDHPHIVKLIGVITENPVW-IIMELCTL 509
Cdd:cd14060      2 GGGSFGSVYRAIWVSQDK---EVAVK------------KLLKiekEAEILSVLSHRNIIQFYGAILEAPNYgIVTEYASY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESK---RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd14060     67 GSLFDYLNSnESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 kGKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMHGVkPFQGVKNNDVIGRI-ENGERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd14060    147 -GTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREV-PFKGLEGLQVAWLVvEKNERPTIPSSCPRSFAELMRRCW 222
                          250       260
                   ....*....|....*....|
gi 1914779978  665 AYDPSRRPRFTELKAQLSTI 684
Cdd:cd14060    223 EADVKERPSFKQIIGILESM 242
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
433-682 1.99e-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: 139.32  E-value: 1.99e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVaIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 511
Cdd:cd14206      5 IGNGWFGKVILGEIFSDYTPAQVV-VKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETiPFLLIMEFCQLGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRK---------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR--YMEDsT 580
Cdd:cd14206     84 LKRYLRAQRkadgmtpdlPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHnnYKED-Y 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPIKWMAPESINFRRF-------TSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI--ENGERLPMPPN 651
Cdd:cd14206    163 YLTPDRLWIPLRWVAPELLDELHGnlivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVvrEQQMKLAKPRL 242
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1914779978  652 CPP---TLYSLMTKCWaYDPSRRPRFTELKAQLS 682
Cdd:cd14206    243 KLPyadYWYEIMQSCW-LPPSQRPSVEELHLQLS 275
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
425-684 2.66e-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: 2.66e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPenpalAVAIKTCK-------NCTSDSVRekflQEALTMRQFDHPHIVKLIGVITE 497
Cdd:cd14147      3 QELRLEEVIGIGGFGKVYRGSWRGE-----LVAVKAARqdpdediSVTAESVR----QEARLFAMLAHPNIIALKAVCLE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NP-VWIIMELCTLGELRSFLQVRKYSLDLasLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS---SNDC-----V 565
Cdd:cd14147     74 EPnLCLVMEYAAGGPLSRALAGRRVPPHV--LVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpiENDDmehktL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  566 KLGDFGLSRYMEDSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGE 644
Cdd:cd14147    152 KITDFGLAREWHKTTQMSAAG---TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAyGVAVNKL 227
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  645 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14147    228 TLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
427-674 5.38e-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: 5.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSD--SVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM 504
Cdd:cd05037      1 ITFHEHLGQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDhrDISESFFETASLMSQISHKHLVKLYGVCVADENIMVQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC------VKLGDFGLSRymed 578
Cdd:cd05037     81 EYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGVPI---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 sTYYKASKGKLPIKWMAPESI-NFRRFTS-ASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMpPNCPPtL 656
Cdd:cd05037    157 -TVLSREERVDRIPWIAPECLrNLQANLTiAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPA-PDCAE-L 233
                          250
                   ....*....|....*...
gi 1914779978  657 YSLMTKCWAYDPSRRPRF 674
Cdd:cd05037    234 AELIMQCWTYEPTKRPSF 251
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
433-684 6.51e-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: 6.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCK-------NCTSDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIM 504
Cdd:cd14148      2 IGVGGFGKVYKGLWRGEE-----VAVKAARqdpdediAVTAENVR----QEARLFWMLQHPNIIALRGVCLNPPhLCLVM 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLasLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS--------SNDCVKLGDFGLS 573
Cdd:cd14148     73 EYARGGALNRALAGKKVPPHV--LVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILepienddlSGKTLKITDFGLA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDV-IGRIENGERLPMPPNC 652
Cdd:cd14148    151 REWHKTTKMSAAG---TYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVaYGVAMNKLTLPIPSTC 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14148    227 PEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
433-684 1.30e-35

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: 1.30e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKN-------CTSDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIM 504
Cdd:cd14146      2 IGVGGFGKVYRATWKGQE-----VAVKAARQdpdedikATAESVR----QEAKLFSMLRHPNIIKLEGVCLEEPnLCLVM 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLAS--------LILYAYQLSTALAYLESKRFV---HRDIAARNVLVSS--------NDCV 565
Cdd:cd14146     73 EFARGGTLNRALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEkiehddicNKTL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  566 KLGDFGLSRYMEDSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGE 644
Cdd:cd14146    153 KITDFGLAREWHRTTKMSAAG---TYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAyGVAVNKL 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  645 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14146    229 TLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
428-672 3.09e-35

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: 134.91  E-value: 3.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIymSPENPALaVAIKT---CKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd05117      3 ELGKVLGRGSFGVVRLAV--HKKTGEE-YAVKIidkKKLKSED--EEMLRREIEILKRLDHPNIVKLYEVFeDDKNLYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELrsF---LQVRKYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRYME 577
Cdd:cd05117     78 MELCTGGEL--FdriVKKGSFSEREAAKIM--KQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIFE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLY 657
Cdd:cd05117    154 EGEKLKTVCGTP--YYVAPEVLKGKGYGKKCDIWSLGVILY-ILLCGYPPFYGETEQELFEKILKGK-YSFDSPEWKNVS 229
                          250
                   ....*....|....*....
gi 1914779978  658 S----LMTKCWAYDPSRRP 672
Cdd:cd05117    230 EeakdLIKRLLVVDPKKRL 248
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
433-678 6.78e-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: 134.22  E-value: 6.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCK-------------NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI---T 496
Cdd:cd14008      1 LGRGSFGKVKLALDTETGQL---YAIKIFNksrlrkrregkndRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIddpE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGEL---RSFLQVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd14008     78 SDKLYLVLEYCEGGPVmelDSGDRVPPLPEETARK--YFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDST-YYKASKGKlPIkWMAPESINFRRFT---SASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLPM 648
Cdd:cd14008    156 EMFEDGNdTLQKTAGT-PA-FLAPELCDGDSKTysgKAADIWALGVTLY-CLVFGRLPFNGDNILELYEAIQNQNdEFPI 232
                          250       260       270
                   ....*....|....*....|....*....|
gi 1914779978  649 PPNCPPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14008    233 PPELSPELKDLLRRMLEKDPEKRITLKEIK 262
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
254-328 4.42e-34

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: 126.59  E-value: 4.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  254 DKECFKCALGSSWIISVELAIGPEEGISYLTDKGCN------------------------------------PLTVTAPS 297
Cdd:cd13190      1 DQEIFKCALGSGWSIPVDLVIGPEVGISYLTDKGSApthladfeqiqsiqtsksedkdgkallqlkiagasePLSITCSS 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1914779978  298 LTIAENMADLIDGYCRLVNGTSQSFIIRPQK 328
Cdd:cd13190     81 LATAESLADLIDGYCRLVNQTDSSLIIRPEK 111
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
433-681 8.55e-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: 131.04  E-value: 8.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSV-REKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLG 510
Cdd:cd13978      1 LGSGGFGTVSKARHVSWF---GMVAIKCLHSSPNCIEeRKALLKEAEKMERARHSYVLPLLGVCVERrSLGLVMEYMENG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLE--SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd13978     78 SLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRRRGT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LP----IKWMAPESIN--FRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLPMPPNC-------PP 654
Cdd:cd13978    158 ENlggtPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLIMQIvSKGDRPSLDDIGrlkqienVQ 236
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  655 TLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd13978    237 ELISLMIRCWDGNPDARPTFLECLDRL 263
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
433-682 3.09e-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: 129.63  E-value: 3.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPAlAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 511
Cdd:cd05042      3 IGNGWFGKVLLGEIYSGTSVA-QVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAiPYLLVMEFCDLGD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSL----DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL--SRYMEDsTYYKAS 585
Cdd:cd05042     82 LKAYLRSEREHErgdsDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLahSRYKED-YIETDD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESIN--FRRF-----TSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI--ENGERLPMPPNCPP-- 654
Cdd:cd05042    161 KLWFPLRWTAPELVTefHDRLlvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVvrEQDTKLPKPQLELPys 240
                          250       260
                   ....*....|....*....|....*....
gi 1914779978  655 -TLYSLMTKCWaYDPSRRPRFTELKAQLS 682
Cdd:cd05042    241 dRWYEVLQFCW-LSPEQRPAAEDVHLLLT 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
433-677 8.25e-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: 127.72  E-value: 8.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKtcknCTSDSVREKFLQEAL-----TMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEV---VAIK----EISRKKLNKKLQENLeseiaILKSIKHPNIVRLYDVQkTEDFIYLVLEY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDSTYYK 583
Cdd:cd14009     74 CAGGDLSQYIRKRG-RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKIADFGFARSLQPASMAE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIE-NGERLPMP------PNCPPTL 656
Cdd:cd14009    153 TLCGS-PL-YMAPEILQFQKYDAKADLWSVGAILFEML-VGKPPFRGSNHVQLLRNIErSDAVIPFPiaaqlsPDCKDLL 229
                          250       260
                   ....*....|....*....|.
gi 1914779978  657 YSLMTKcwayDPSRRPRFTEL 677
Cdd:cd14009    230 RRLLRR----DPAERISFEEF 246
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
433-682 2.40e-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: 2.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPAlAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCTLGE 511
Cdd:cd05087      5 IGHGWFGKVFLGEVNSGLSST-QVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEvTPYLLVMEFCPLGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLA----SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS--RYMEDsTYYKAS 585
Cdd:cd05087     84 LKGYLRSCRAAESMApdplTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShcKYKED-YFVTAD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESIN-------FRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMP-PNCPPTL- 656
Cdd:cd05087    163 QLWVPLRWIAPELVDevhgnllVVDQTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTVREQQLKLPkPQLKLSLa 242
                          250       260
                   ....*....|....*....|....*....
gi 1914779978  657 ---YSLMTKCWaYDPSRRPRFTELKAQLS 682
Cdd:cd05087    243 erwYEVMQFCW-LQPEQRPTAEEVHLLLS 270
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
419-672 7.03e-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: 125.46  E-value: 7.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHQGIyMSPENpaLAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVI 495
Cdd:cd08224      1 NYEIEKK-------IGKGQFSVVYRAR-CLLDG--RLVALKKVQifEMMDAKARQDCLKEIDLLQQLNHPNIIKyLASFI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFL---QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd08224     71 ENNELNIVLELADAGDLSRLIkhfKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEilMHGVK-PFQGVKNN--DVIGRIENGERLPMP 649
Cdd:cd08224    151 GRFFSSKTTAAHSLVGTPY-YMSPERIREQGYDFKSDIWSLGCLLYE--MAALQsPFYGEKMNlySLCKKIEKCEYPPLP 227
                          250       260
                   ....*....|....*....|....
gi 1914779978  650 PNCPPT-LYSLMTKCWAYDPSRRP 672
Cdd:cd08224    228 ADLYSQeLRDLVAACIQPDPEKRP 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
427-677 1.97e-31

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: 124.24  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYmSPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIME 505
Cdd:cd06623      3 LERVKVLGQGSSGVVYKVRH-KPTG--KIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAfYKEGEISIVLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKY--SLDLASLilyAYQLSTALAYLESKR-FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 582
Cdd:cd06623     80 YMDGGSLADLLKKVGKipEPVLAYI---ARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KAS-KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE---NGERLPMPPN-CPPTLY 657
Cdd:cd06623    157 CNTfVGTVT--YMSPERIQGESYSYAADIWSLGLTLLECAL-GKFPFLPPGQPSFFELMQaicDGPPPSLPAEeFSPEFR 233
                          250       260
                   ....*....|....*....|
gi 1914779978  658 SLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06623    234 DFISACLQKDPKKRPSAAEL 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
430-677 6.58e-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: 6.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIymSPENPALaVAIKTCKNCTSDSVREKFL----QEALTMRQFDHPHIVKLIGVIT-ENPVWIIM 504
Cdd:cd06632      5 GQLLGSGSFGSVYEGF--NGDTGDF-FAVKEVSLVDDDKKSRESVkqleQEIALLSKLRHPNIVQYYGTEReEDNLYIFL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQvrKYSLDLASLI-LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 583
Cdd:cd06632     82 EYVPGGSIHKLLQ--RYGAFEEPVIrLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKlPIkWMAPESINFR--RFTSASDVWMFGVCMWEilMHGVKP----FQGVKnndVIGRIENGERLP-MPPNCPPTL 656
Cdd:cd06632    160 SFKGS-PY-WMAPEVIMQKnsGYGLAVDIWSLGCTVLE--MATGKPpwsqYEGVA---AIFKIGNSGELPpIPDHLSPDA 232
                          250       260
                   ....*....|....*....|.
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06632    233 KDFIRLCLQRDPEDRPTASQL 253
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
428-677 1.21e-30

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: 121.60  E-value: 1.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKflqEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd06612      6 DILEKLGEGSYGSVYKAIHKETGQV---VAIKVVPVEEDLQEIIK---EISILKQCDSPYIVKYYGSYfKNTDLWIVMEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd06612     80 CGAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgerlpMPPNC--PPTLYS-----L 659
Cdd:cd06612    160 IGTPF-WMAPEVIQEIGYNNKADIWSLGITAIE-MAEGKPPYSDIHPMRAIFMIPN-----KPPPTlsDPEKWSpefndF 232
                          250
                   ....*....|....*...
gi 1914779978  660 MTKCWAYDPSRRPRFTEL 677
Cdd:cd06612    233 VKKCLVKDPEERPSAIQL 250
Pkinase pfam00069
Protein kinase domain;
428-679 1.72e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 120.04  E-value: 1.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITENP-VWIIME 505
Cdd:pfam00069    2 EVLRKLGSGSFGTVYKAKHRDTGKI---VAIKKIKKEKIKKKKDKnILREIKILKKLNHPNIVRLYDAFEDKDnLYLVLE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYleskrfvhrdiaarnvlvssndcvklgdfGLSRYMEDSTYYkas 585
Cdd:pfam00069   79 YVEGGSLFDLLSEKGA-FSEREAKFIMKQILEGLES-----------------------------GSSLTTFVGTPW--- 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 kgklpikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPM--PPNCPPTLYSLMTKC 663
Cdd:pfam00069  126 -------YMAPEVLGGNPYGPKVDVWSLGCILYE-LLTGKPPFPGINGNEIYELIIDQPYAFPelPSNLSEEAKDLLKKL 197
                          250
                   ....*....|....*.
gi 1914779978  664 WAYDPSRRPRFTELKA 679
Cdd:pfam00069  198 LKKDPSKRLTATQALQ 213
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
425-677 1.75e-30

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: 121.97  E-value: 1.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWII 503
Cdd:cd06609      1 ELFTLLERIGKGSFGEVYKGIDKRTNQV---VAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGsKLWII 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 583
Cdd:cd06609     78 MEYCGGGSVLDLLKPGPLDETYIAFILR--EVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIengerlpmPPNCPPTL----YS- 658
Cdd:cd06609    156 NTFVGTPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVLFLI--------PKNNPPSLegnkFSk 225
                          250       260
                   ....*....|....*....|...
gi 1914779978  659 ----LMTKCWAYDPSRRPRFTEL 677
Cdd:cd06609    226 pfkdFVELCLNKDPKERPSAKEL 248
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
433-681 5.53e-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: 119.90  E-value: 5.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiYMSPENPALAVaIKTCKNCTSDSvreKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 511
Cdd:cd14065      1 LGKGFFGEVYK--VTHRETGKVMV-MKELKRFDEQR---SFLKEVKLMRRLSHPNILRFIGVcVKDNKLNFITEYVNGGT 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV---SSNDCVKLGDFGLSRYMEDstyYKASKG- 587
Cdd:cd14065     75 LEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPD---EKTKKPd 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 -KLPIK------WMAPESINFRRFTSASDVWMFGVCMWEILmhGVKPfqgvKNNDVIGRIEN------GERLPMPPNCPP 654
Cdd:cd14065    152 rKKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEII--GRVP----ADPDYLPRTMDfgldvrAFRTLYVPDCPP 225
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  655 TLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd14065    226 SFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
426-677 8.02e-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: 119.71  E-value: 8.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSpENPALAVA-IKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWII 503
Cdd:cd06626      1 RWQRGNKIGEGTFGKVYTAVNLD-TGELMAMKeIRFQDN--DPKTIKEIADEMKVLEGLDHPNLVRYYGVeVHREEVYIF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyYK 583
Cdd:cd06626     78 MEYCQEGTLEELLRHGRI-LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNT-TT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKL------PIkWMAPESINFRRFTS---ASDVWMFGVCMWEiLMHGVKPFQGVKNN-DVIGRIENGERLPMPPN-- 651
Cdd:cd06626    156 MAPGEVnslvgtPA-YMAPEVITGNKGEGhgrAADIWSLGCVVLE-MATGKRPWSELDNEwAIMYHVGMGHKPPIPDSlq 233
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06626    234 LSPEGKDFLSRCLESDPKKRPTASEL 259
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
433-685 8.82e-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: 8.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd14221      1 LGKGCFG---QAIKVTHRETGEVMVMKELIRFDEETQR-TFLKEVKVMRCLEHPNVLKFIGVLyKDKRLNFITEYIKGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd14221     77 LRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 K-------------WMAPESINFRRFTSASDVWMFGVCMWEIlmhgvkpfqgvknndvIGRIE-NGERLPM--------- 648
Cdd:cd14221    157 PdrkkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEI----------------IGRVNaDPDYLPRtmdfglnvr 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1914779978  649 -------PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd14221    221 gfldrycPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLR 264
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
433-681 4.57e-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: 4.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPenpalaVAIKTCkNCTS--DSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLG 510
Cdd:cd14062      1 IGSGSFGTVYKGRWHGD------VAVKKL-NVTDptPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYmedSTYYKASKGKL- 589
Cdd:cd14062     74 SLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATV---KTRWSGSQQFEq 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 ---PIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVI----GRienGERLP----MPPNCPPT 655
Cdd:cd14062    151 ptgSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYE-LLTGQLPYSHINNRDQIlfmvGR---GYLRPdlskVRSDTPKA 226
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  656 LYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd14062    227 LRRLMEDCIKFQRDERPLFPQILASL 252
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
425-672 4.63e-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: 117.97  E-value: 4.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIElgrCIGEGQFG------DVHQGIYmspenpalaVAIKTCKNCTSD------SVREkflqeALTMRQFDHPHIVKLI 492
Cdd:cd07829      2 EKLE---KLGEGTYGvvykakDKKTGEI---------VALKKIRLDNEEegipstALRE-----ISLLKELKHPNIVKLL 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  493 GVI-TENPVWIIMELCTLgELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 571
Cdd:cd07829     65 DVIhTENKLYLVFEYCDQ-DLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  572 LSRYMEdstyykaskgkLPIKWMAPESINF-----------RRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGR 639
Cdd:cd07829    144 LARAFG-----------IPLRTYTHEVVTLwyrapeillgsKHYSTAVDIWSVGCIFAELITG--KPlFPGDSEIDQLFK 210
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  640 I-------------------ENGERLPMPPNCP---------PTLYSLMTKCWAYDPSRRP 672
Cdd:cd07829    211 IfqilgtpteeswpgvtklpDYKPTFPKWPKNDlekvlprldPEGIDLLSKMLQYNPAKRI 271
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
425-672 9.90e-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: 9.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT----ENPV 500
Cdd:cd13979      3 EPLRLQEPLGSGGFGSVYKATYKGET-----VAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAETgtdfASLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS- 579
Cdd:cd13979     78 LIIMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGn 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 -TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPNCPPT--- 655
Cdd:cd13979    158 eVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQHVLYAVVAKDLRPDLSGLEDSEfgq 236
                          250
                   ....*....|....*...
gi 1914779978  656 -LYSLMTKCWAYDPSRRP 672
Cdd:cd13979    237 rLRSLISRCWSAQPAERP 254
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
426-679 2.36e-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: 2.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKnctsdsvREKFLQEAL---------TMRQFDHPHIVKLIGVI- 495
Cdd:cd14663      1 RYELGRTLGEGTFAKVKFARNTKTGES---VAIKIID-------KEQVAREGMveqikreiaIMKLLRHPNIVELHEVMa 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 575
Cdd:cd14663     71 TKTKIFFVMELVTGGELFSKI-AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEDstyyKASKGKL------PiKWMAPESINFRRFTSA-SDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGErLPM 648
Cdd:cd14663    150 SEQ----FRQDGLLhttcgtP-NYVAPEVLARRGYDGAkADIWSCGVILF-VLLAGYLPFDDENLMALYRKIMKGE-FEY 222
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  649 PPNCPPTLYSLMTKCWAYDPSRRPRFTELKA 679
Cdd:cd14663    223 PRWFSPGAKSLIKRILDPNPSTRITVEQIMA 253
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
419-687 4.91e-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: 114.77  E-value: 4.91e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRERIELGRCIGEGQFGDVHQGIYMSPenpalaVAIKTCkNCTSDSVRE--KFLQEALTMRQFDHPHIVKLIGVIT 496
Cdd:cd14151      2 DWEIPDGQITVGQRIGSGSFGTVYKGKWHGD------VAVKML-NVTAPTPQQlqAFKNEVGVLRKTRHVNILLFMGYST 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL---- 572
Cdd:cd14151     75 KPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvk 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGklpIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNND-VIGRIENGERLP- 647
Cdd:cd14151    155 SRWSGSHQFEQLSGS---ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYE-LMTGQLPYSNINNRDqIIFMVGRGYLSPd 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1914779978  648 ---MPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEE 687
Cdd:cd14151    231 lskVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
425-677 5.66e-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: 113.89  E-value: 5.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGiymSPENPALAVAIK-TCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 502
Cdd:cd14002      1 ENYHVLELIGEGSFGKVYKG---RRKYTGQVVALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFeTKKEFVV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELcTLGELRSFLQV-RKYSLDLASLIlyAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd14002     78 VTEY-AQGELFQILEDdGTLPEEEVRSI--AKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKAS-KGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFqgVKNN--DVIGRIENGE-RLP--MPPNCPPT 655
Cdd:cd14002    155 VLTSiKGT-PL-YMAPELVQEQPYDHTADLWSLGCILYE-LFVGQPPF--YTNSiyQLVQMIVKDPvKWPsnMSPEFKSF 229
                          250       260
                   ....*....|....*....|..
gi 1914779978  656 LYSLMTKcwayDPSRRPRFTEL 677
Cdd:cd14002    230 LQGLLNK----DPSKRLSWPDL 247
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
456-684 6.48e-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: 114.02  E-value: 6.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKtcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM-ELCTLGELRSFLQVRKYSLDLASLILYAYQ 534
Cdd:cd13992     28 VAIK--HITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVtEYCTRGSLQDVLLNREIKMDWMFKSSFIKD 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  535 LSTALAYLESKRF-VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIK--WMAPESIN----FRRFTSA 607
Cdd:cd13992    106 IVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKKllWTAPELLRgsllEVRGTQK 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  608 SDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENGERLPMPPN-------CPPTLYSLMTKCWAYDPSRRPRFTELKAQ 680
Cdd:cd13992    186 GDVYSFAIILYEIL-FRSDPFALEREVAIVEKVISGGNKPFRPElavlldeFPPRLVLLVKQCWAENPEKRPSFKQIKKT 264

                   ....
gi 1914779978  681 LSTI 684
Cdd:cd13992    265 LTEN 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
480-677 7.67e-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: 113.79  E-value: 7.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  480 MRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKY---SLDLASLILYAYQLSTALAY-----LESKRFV 548
Cdd:cd08217     53 LRELKHPNIVRYYDRIvdrANTTLYIVMEYCEGGDLAQLIKKCKKenqYIPEEFIWKIFTQLLLALYEchnrsVGGGKIL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDST----------YYkaskgklpikwMAPESINFRRFTSASDVWMFGVCMW 618
Cdd:cd08217    133 HRDLKPANIFLDSDNNVKLGDFGLARVLSHDSsfaktyvgtpYY-----------MSPELLNEQSYDEKSDIWSLGCLIY 201
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  619 EILMHGvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd08217    202 ELCALH-PPFQAANQLELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEEL 259
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
429-686 1.32e-27

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: 113.05  E-value: 1.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSPENPALaVAIKTC-KNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVITENP-VWIIME 505
Cdd:cd14080      4 LGKTIGEGSYSKVKLAEYTKSGLKEK-VACKIIdKKKAPKDFLEKFLpRELEILRKLRHPNIIQVYSIFERGSkVFIFME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd14080     83 YAEHGDLLEYIQKRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVLS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 K---GKLpiKWMAPESINFRRFT-SASDVWMFGVCMWeILMHGVKPFqgvknNDvigriengerlpmpPNCPPTLYSLMT 661
Cdd:cd14080    162 KtfcGSA--AYAAPEILQGIPYDpKKYDIWSLGVILY-IMLCGSMPF-----DD--------------SNIKKMLKDQQN 219
                          250       260
                   ....*....|....*....|....*
gi 1914779978  662 KCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14080    220 RKVRFPSSVKKLSPECKDLIDQLLE 244
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
433-672 1.83e-27

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: 113.04  E-value: 1.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQG-IYMspENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLG 510
Cdd:cd05086      5 IGNGWFGKVLLGeIYT--GTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAiPYLLVFEFCDLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFL--QVRKYSLDLASLIL--YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL--SRYMEDstYYKA 584
Cdd:cd05086     83 DLKTYLanQQEKLRGDSQIMLLqrMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRYKED--YIET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKL-PIKWMAPESINFRR-------FTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI--ENGERLPMPPNCPP 654
Cdd:cd05086    161 DDKKYaPLRWTAPELVTSFQdgllaaeQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVikERQVKLFKPHLEQP 240
                          250       260
                   ....*....|....*....|.
gi 1914779978  655 ---TLYSLMTKCWaYDPSRRP 672
Cdd:cd05086    241 ysdRWYEVLQFCW-LSPEKRP 260
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
433-686 2.67e-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: 2.67e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPenpaLAVAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 512
Cdd:cd14150      8 IGTGSFGTVFRGKWHGD----VAVKILKVTEPTPEQL-QAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGSSL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  513 RSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYmeDSTYYKASKGKLP-- 590
Cdd:cd14150     83 YRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATV--KTRWSGSQQVEQPsg 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  591 -IKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNND-VIGRIENGERLP----MPPNCPPTLYSLMT 661
Cdd:cd14150    161 sILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYE-LMSGTLPYSNINNRDqIIFMVGRGYLSPdlskLSSNCPKAMKRLLI 239
                          250       260
                   ....*....|....*....|....*
gi 1914779978  662 KCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14150    240 DCLKFKREERPLFPQILVSIELLQR 264
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
419-677 3.25e-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: 111.73  E-value: 3.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCkNCTSDSVREK--FLQEALTMRQFDHPHIVKLIGVIT 496
Cdd:cd08529      1 DFEILNK-------LGKGSFGVVYKVVRKVDGR---VYALKQI-DISRMSRKMReeAIDEARVLSKLNSPYVIKYYDSFV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 E-NPVWIIMELCTLGELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd08529     70 DkGKLNIVMEYAENGDLHSLIKSqRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPNCPP 654
Cdd:cd08529    150 ILSDTTNFAQTIVGTPY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILKIVRGKYPPISASYSQ 227
                          250       260
                   ....*....|....*....|...
gi 1914779978  655 TLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd08529    228 DLSQLIDSCLTKDYRQRPDTTEL 250
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
433-686 1.67e-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: 1.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKtCKNCT--SDSVREKFLQEALTMRQFDHPHIVKLIGVITEnPVWIIMELCTLG 510
Cdd:cd14025      4 VGSGGFGQVYKVRHKHWKT---WLAIK-CPPSLhvDDSERMELLEEAKKMEMAKFRHILPVYGICSE-PVGLVMEYMETG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYayQLSTALAYLESKR--FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd14025     79 SLEKLLASEPLPWELRFRIIH--ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHDLSRDG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 L--PIKWMAPESI--NFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKN-NDVIGRIENGER--LPMPPNCPPT----LY 657
Cdd:cd14025    157 LrgTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQK-KPFAGENNiLHIMVKVVKGHRpsLSPIPRQRPSecqqMI 235
                          250       260
                   ....*....|....*....|....*....
gi 1914779978  658 SLMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14025    236 CLMKRCWDQDPRKRPTFQDITSETENLLS 264
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
419-677 2.26e-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: 2.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 498
Cdd:cd06610      2 DYELIEV-------IGSGATAVVYAAYCLPKKE---KVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PV-WIIMELCTLGelrSFLQVRKYS-----LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd06610     72 DElWLVMPLLSGG---SLLDIMKSSyprggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLPIK---WMAPESIN-FRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgerlpm 648
Cdd:cd06610    149 SASLATGGDRTRKVRKTFVGtpcWMAPEVMEqVRGYDFKADIWSFGITAIE-LATGAAPYSKYPPMKVLMLTLQ------ 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  649 ppNCPPTL--------YS-----LMTKCWAYDPSRRPRFTEL 677
Cdd:cd06610    222 --NDPPSLetgadykkYSksfrkMISLCLQKDPSKRPTAEEL 261
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
433-684 2.38e-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: 2.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGE 511
Cdd:cd14222      1 LGKGFFG---QAIKVTHKATGKVMVMKELIRCDEET-QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKrLNLLTEFIEGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY---------MEDSTYY 582
Cdd:cd14222     77 LKDFLRADDP-FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveekkkppPDKPTTK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLPIK----------WMAPESINFRRFTSASDVWMFGVCMWEILMhgvkpfQGVKNNDVIGR-IENGERLPM--- 648
Cdd:cd14222    156 KRTLRKNDRKkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIG------QVYADPDCLPRtLDFGLNVRLfwe 229
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  649 ---PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14222    230 kfvPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEAL 268
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
426-677 2.89e-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: 2.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHqgiymspenpaLAVAIKTCKNC-------TSDSVREKFL--QEALTMRQFDHPHIVKLIGVIT 496
Cdd:cd08225      1 RYEIIKKIGEGSFGKIY-----------LAKAKSDSEHCvikeidlTKMPVKEKEAskKEVILLAKMKHPNIVTFFASFQ 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 EN-PVWIIMELCTLGELRSFLQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KLGDFGLS 573
Cdd:cd08225     70 ENgRLFIVMEYCDGGDLMKRINRQRGVLFSEDQILsWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHgvkPFQGVKNNDVIGRIENGERLPMPPN 651
Cdd:cd08225    150 RQLNDSMELAYTCVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELctLKH---PFEGNNLHQLVLKICQGYFAPISPN 225
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd08225    226 FSRDLRSLISQLFKVSPRDRPSITSI 251
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
427-678 3.22e-26

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 109.36  E-value: 3.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYMSpenpalAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 504
Cdd:cd14063      2 LEIKEVIGKGRFGRVHRGRWHG------DVAIKLLNiDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPhLAIVT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVkLGDFGLSRyMEDSTYYKA 584
Cdd:cd14063     76 SLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLFS-LSGLLQPGR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKL--PIKW---MAPE-----SINFRR-----FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERlpMP 649
Cdd:cd14063    154 REDTLviPNGWlcyLAPEiiralSPDLDFeeslpFTKASDVYAFGTVWYE-LLAGRWPFKEQPAESIIWQVGCGKK--QS 230
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  650 PN---CPPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14063    231 LSqldIGREVKDILMQCWAYDPEKRPTFSDLL 262
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
433-672 6.27e-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: 108.58  E-value: 6.27e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTL 509
Cdd:cd08228     10 IGRGQFSEVYRATCLLDRKP---VALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKyLDSFIEDNELNIVLELADA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLA---SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd08228     87 GDLSQMIKYFKKQKRLIperTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI-LMHgvKPFQGVKNN--DVIGRIENGERLPMP-PNCPPTLYSLMTK 662
Cdd:cd08228    167 VGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMaALQ--SPFYGDKMNlfSLCQKIEQCDYPPLPtEHYSEKLRELVSM 243
                          250
                   ....*....|
gi 1914779978  663 CWAYDPSRRP 672
Cdd:cd08228    244 CIYPDPDQRP 253
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
425-677 7.12e-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: 108.02  E-value: 7.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPenpALAVAIKTC--KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVW 501
Cdd:cd14099      1 KRYRRGKFLGKGGFAKCYEVTDMST---GKVYAGKVVpkSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEdEENVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd14099     78 ILLELCSNGSLMELLKRRKA-LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKLPiKWMAPESINFRRFTS-ASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSL 659
Cdd:cd14099    157 RKKTLCGTP-NYIAPEVLEKKKGHSfEVDIWSLGVILYTLLV-GKPPFETSDVKETYKRIKKNEySFPSHLSISDEAKDL 234
                          250
                   ....*....|....*...
gi 1914779978  660 MTKCWAYDPSRRPRFTEL 677
Cdd:cd14099    235 IRSMLQPDPTKRPSLDEI 252
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
433-672 9.32e-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: 107.32  E-value: 9.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKN---CTSDSVRE-KFLQEaLTMRQfDHPHIVKLIGVIT---ENPVWIIME 505
Cdd:cd05118      7 IGEGAFGTVWLARDKVTGE---KVAIKKIKNdfrHPKAALREiKLLKH-LNDVE-GHPNIVKLLDVFEhrgGNHLCLVFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LctLGE-LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-VKLGDFGLSRYMEDSTYYK 583
Cdd:cd05118     82 L--MGMnLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARSFTSPPYTP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKgklPIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIEngERLPmppncPPTLYSLMTK 662
Cdd:cd05118    160 YVA---TRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLT-GRPLFPGDSEVDQLAKIV--RLLG-----TPEALDLLSK 228
                          250
                   ....*....|
gi 1914779978  663 CWAYDPSRRP 672
Cdd:cd05118    229 MLKYDPAKRI 238
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
433-684 1.34e-25

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: 1.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNCtSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGE 511
Cdd:cd14154      1 LGKGFFG---QAIKVTHRETGEVMVMKELIRF-DEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKkLNLITEYIPGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED----STYYKASKG 587
Cdd:cd14154     77 LKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEerlpSGNMSPSET 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KLPIK---------------WMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNC 652
Cdd:cd14154    157 LRHLKspdrkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPRTKDFGLNVDSFREKFCAGC 236
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14154    237 PPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
471-676 1.56e-25

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: 107.20  E-value: 1.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  471 EKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVH 549
Cdd:cd14027     36 EALLEEGKMMNRLRHSRVVKLLGVILEEGKYsLVMEYMEKGNLMHVLK--KVSVPLSVKGRIILEIIEGMAYLHGKGVIH 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  550 RDIAARNVLVSSNDCVKLGDFGLS--------------RYMEDSTYYKASKGKLpiKWMAPESIN--FRRFTSASDVWMF 613
Cdd:cd14027    114 KDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehnEQREVDGTAKKNAGTL--YYMAPEHLNdvNAKPTEKSDVYSF 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  614 GVCMWEILMhGVKPFQGVKNND-VIGRIENGERlP----MPPNCPPTLYSLMTKCWAYDPSRRPRFTE 676
Cdd:cd14027    192 AIVLWAIFA-NKEPYENAINEDqIIMCIKSGNR-PdvddITEYCPREIIDLMKLCWEANPEARPTFPG 257
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
433-683 1.87e-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: 1.87e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPenpalAVAIKTCKNCT--SDSVREKFLQEALTMRQFDHPHIVKLIGVITENP--VWIIMELCT 508
Cdd:cd14064      1 IGSGSFGKVYKGRCRNK-----IVAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPsqFAIVTQYVS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLE--SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd14064     76 GGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPIKWMAPESIN-FRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE-NGERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd14064    156 QPGNLRWMAPEVFTqCTRYSIKADVFSYALCLWELLT-GEIPFAHLKPAAAAADMAyHHIRPPIGYSIPKPISSLLMRGW 234
                          250
                   ....*....|....*....
gi 1914779978  665 AYDPSRRPRFTELKAQLST 683
Cdd:cd14064    235 NAEPESRPSFVEIVALLEP 253
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
432-676 4.74e-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: 105.45  E-value: 4.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  432 CIGEGQFGDVHQGiyMSPENPALAVAIKtC--KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCT 508
Cdd:cd14121      2 KLGSGTYATVYKA--YRKSGAREVVAVK-CvsKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQwDEEHIYLIMEYCS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND--CVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd14121     79 GGDLSRFIRSRR-TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKPNDEAHSLR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPN------CPPTLYSLM 660
Cdd:cd14121    158 GS-PL-YMAPEMILKKKYDARVDLWSVGVILYECLF-GRAPFASRSFEELEEKIRSSKPIEIPTRpelsadCRDLLLRLL 234
                          250
                   ....*....|....*.
gi 1914779978  661 TKcwayDPSRRPRFTE 676
Cdd:cd14121    235 QR----DPDRRISFEE 246
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
428-644 6.11e-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: 6.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSP-ENPALAVAIKT-CKNctsdsvREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14095      3 DIGRVIGDGNFAVVKECRDKATdKEYALKIIDKAkCKG------KEHMIEnEVAILRRVKHPNIVQLIEEYdTDTELYLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYMED 578
Cdd:cd14095     77 MELVKGGDLfDAITSSTKFTERDASRMVT--DLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKE 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  579 --------STYykaskgklpikwMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNN--DVIGRIENGE 644
Cdd:cd14095    155 plftvcgtPTY------------VAPEILAETGYGLKVDIWAAGVITY-ILLCGFPPFRSPDRDqeELFDLILAGE 217
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
456-677 1.07e-24

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: 104.68  E-value: 1.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKtcknCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ---------VRKYSLDL 525
Cdd:cd14010     28 VAIK----CVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYeTSNHLWLVVEYCTGGDLETLLRqdgnlpessVRKFGRDL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  526 AslilyayqlsTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-------TYYKASKGKLPIK------ 592
Cdd:cd14010    104 V----------RGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEIlkelfgqFSDEGNVNKVSKKqakrgt 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  593 --WMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPN--CPPT------LYSLMTK 662
Cdd:cd14010    174 pyYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFVAESFTELVEKILNEDPPPPPPKvsSKPSpdfkslLKGLLEK 252
                          250
                   ....*....|....*
gi 1914779978  663 cwayDPSRRPRFTEL 677
Cdd:cd14010    253 ----DPAKRLSWDEL 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
433-677 1.79e-24

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: 104.44  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 511
Cdd:cd06611     13 LGDGAFGKVYKAQH---KETGLFAAAKIIQIESEEEL-EDFMVEIDILSECKHPNIVGLYEAyFYENKLWILIEFCDGGA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPi 591
Cdd:cd06611     89 LDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTP- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 KWMAPESINFRRFTSA-----SDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGErlpmppncPPTL---------- 656
Cdd:cd06611    168 YWMAPEVVACETFKDNpydykADIWSLGITLIE-LAQMEPPHHELNPMRVLLKILKSE--------PPTLdqpskwsssf 238
                          250       260
                   ....*....|....*....|.
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06611    239 NDFLKSCLVKDPDDRPTAAEL 259
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
431-680 2.15e-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: 2.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGdvhQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTL 509
Cdd:cd08219      6 RVVGEGSFG---RALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFeADGHLYIVMEYCDG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd08219     83 GDLMQKIKLQRGKLFPEDTILqWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTYVG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHgvkPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAY 666
Cdd:cd08219    163 TPY-YVPPEIWENMPYNNKSDIWSLGCILYELctLKH---PFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKR 238
                          250
                   ....*....|....
gi 1914779978  667 DPSRRPRFTELKAQ 680
Cdd:cd08219    239 NPRSRPSATTILSR 252
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
419-672 2.25e-24

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: 104.22  E-value: 2.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIqrerielGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKncTSDSVREK----FLQEALTMRQFDHPHIVKLIGv 494
Cdd:cd05581      2 DFKF-------GKPLGEGSYSTVVLAKEKETGKE---YAIKVLD--KRHIIKEKkvkyVTIEKEVLSRLAHPGIVKLYY- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 iT---ENPVWIIMELCTLGELRSFLqvRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDF 570
Cdd:cd05581     69 -TfqdESKLYFVLEYAPNGDLLEYI--RKYgSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDF 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  571 GLSRYMEDSTYYKASKGKLPIK----------------WMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNN 634
Cdd:cd05581    146 GTAKVLGPDSSPESTKGDADSQiaynqaraasfvgtaeYVSPELLNEKPAGKSSDLWALG-CIIYQMLTGKPPFRGSNEY 224
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1914779978  635 DVIGRIENGErLPMPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd05581    225 LTFQKIVKLE-YEFPENFPPDAKDLIQKLLVLDPSKRL 261
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
426-672 3.46e-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: 104.12  E-value: 3.46e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKtcknctsdsvreKFLQ-------EALTMRQFDHPHIVKLIG---VI 495
Cdd:cd14137      5 SYTIEKVIGSGSFGVVYQAKLLETGEV---VAIK------------KVLQdkryknrELQIMRRLKHPNIVKLKYffySS 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENP----VWIIMELC--TLGE-LRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KL 567
Cdd:cd14137     70 GEKKdevyLNLVMEYMpeTLYRvIRHYSKNKQT-IPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMED---------STYYKaskgklpikwmAPESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNND- 635
Cdd:cd14137    149 CDFGSAKRLVPgepnvsyicSRYYR-----------APELIfGATDYTTAIDIWSAGCVLAELLLG--QPlFPGESSVDq 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  636 ------VIG-----------------RIENGERLPM----PPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd14137    216 lveiikVLGtptreqikamnpnytefKFPQIKPHPWekvfPKRTPPDAIDLLSKILVYNPSKRL 279
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
430-677 5.23e-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: 5.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIY-MSPENPAL------AVAIKTCKnctsdsvREKFLQEALT-----MRQFDHPHIVKLIGV-IT 496
Cdd:cd06628      5 GALIGSGSFGSVYLGMNaSSGELMAVkqvelpSVSAENKD-------RKKSMLDALQreialLRELQHENIVQYLGSsSD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGELRSFLQvrKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 575
Cdd:cd06628     78 ANHLNIFLEYVPGGSVATLLN--NYGAFEESLVRnFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEDSTYYKASKGKLP-----IKWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPP 650
Cdd:cd06628    156 LEANSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLG-CLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPS 234
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  651 NCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06628    235 NISSEARDFLEKTFEIDHNKRPTADEL 261
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
428-672 5.41e-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: 103.00  E-value: 5.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKN-------CTSdsVRE-KFLQeALTmrqfDHPHIVKLIGVITEN- 498
Cdd:cd07830      2 KVIKQLGDGTFGSVYLARNKETGE---LVAIKKMKKkfysweeCMN--LREvKSLR-KLN----EHPNIVKLKEVFRENd 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMEL--CTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 576
Cdd:cd07830     72 ELYFVFEYmeGNLYQLMKDRKGKPFSESVIRSIIY--QILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDS---TYYKASkgklpiKWM-APEsINFRR--FTSASDVWMFGVCMWEILMhgVKP-FQGVKNNDVIGRI--------- 640
Cdd:cd07830    150 RSRppyTDYVST------RWYrAPE-ILLRStsYSSPVDIWALGCIMAELYT--LRPlFPGSSEIDQLYKIcsvlgtptk 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  641 ---ENGERL------------PMP-----PNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd07830    221 qdwPEGYKLasklgfrfpqfaPTSlhqliPNASPEAIDLIKDMLRWDPKKRP 272
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
415-684 5.62e-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: 103.19  E-value: 5.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  415 DEARDYEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGV 494
Cdd:cd14149      2 DSSYYWEIEASEVMLSTRIGSGSFGTVYKGKW----HGDVAVKILKVVDPTPEQF-QAFRNEVAVLRKTRHVNILLFMGY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd14149     77 MTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMED-STYYKASKGKLPIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNND-VIGRIENGERLP-- 647
Cdd:cd14149    157 VKSRwSGSQQVEQPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYE-LMTGELPYSHINNRDqIIFMVGRGYASPdl 235
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  648 --MPPNCPPTLYSLMTKCWAYDPSRRPRFTELkaqLSTI 684
Cdd:cd14149    236 skLYKNCPKAMKRLVADCIKKVKEERPLFPQI---LSSI 271
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
433-677 6.32e-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: 6.32e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL--CT 508
Cdd:cd07833      9 VGEGAYGVVLKC--RNKATGEI-VAIKKFKESEDDEdVKKTALREVKVLRQLRHENIVNLKEAFrRKGRLYLVFEYveRT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELrsfLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-----TYYK 583
Cdd:cd07833     86 LLEL---LEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARpasplTDYV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASkgklpiKWM-APE----SINFRRftsASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIEN---------------- 642
Cdd:cd07833    163 AT------RWYrAPEllvgDTNYGK---PVDVWAIGCIMAELLD-GEPLFPGDSDIDQLYLIQKclgplppshqelfssn 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  643 ----GERLPMPPN-----------CPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd07833    233 prfaGVAFPEPSQpeslerrypgkVSSPALDFLKACLRMDPKERLTCDEL 282
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
480-679 1.48e-23

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: 101.05  E-value: 1.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  480 MRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNV 557
Cdd:cd05123     47 LERVNHPFIVKLHYAFqTEEKLYLVLDYVPGGELFSHLSkEGRFPEERARF--YAAEIVLALEYLHSLGIIYRDLKPENI 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  558 LVSSNDCVKLGDFGLSRYME---DSTY-------YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMhGVKP 627
Cdd:cd05123    125 LLDSDGHIKLTDFGLAKELSsdgDRTYtfcgtpeY-----------LAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPP 192
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  628 FQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMTKCWAYDPSRR---PRFTELKA 679
Cdd:cd05123    193 FYAENRKEIYEKILKSP-LKFPEYVSPEAKSLISGLLQKDPTKRlgsGGAEEIKA 246
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
423-672 2.48e-23

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: 100.83  E-value: 2.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  423 QRERIELgRCIGEGQFGDVHQ------GIYMspenpalavAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-I 495
Cdd:cd13996      5 LNDFEEI-ELLGSGGFGSVYKvrnkvdGVTY---------AIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAwV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQVR--KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGL 572
Cdd:cd13996     75 EEPPLYIQMELCEGGTLRDWIDRRnsSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDlQVKIGDFGL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLPIK-------------WMAPESINFRRFTSASDVWMFGVCMWEIL------MHGVKPFQGVKN 633
Cdd:cd13996    155 ATSIGNQKRELNNLNNNNNGntsnnsvgigtplYASPEQLDGENYNEKADIYSLGIILFEMLhpfktaMERSTILTDLRN 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  634 ndvigriengerLPMPPNC---PPTLYSLMTKCWAYDPSRRP 672
Cdd:cd13996    235 ------------GILPESFkakHPKEADLIQSLLSKNPEERP 264
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
433-644 2.59e-23

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: 100.03  E-value: 2.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPenpALAVAIKTCKncTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 511
Cdd:cd14006      1 LGRGRFGVVKRCIEKAT---GREFAAKFIP--KRDKKKEAVLREISILNQLQHPRIIQLHEAyESPTELVLILELCSGGE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTYYKASKGKL 589
Cdd:cd14006     76 LLDRL-AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGEELKEIFGTP 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  590 piKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE 644
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 ...
473-674 3.45e-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: 100.40  E-value: 3.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  473 FLQEALTMRQFDHPHIVKLIGVITENPVWIIME-LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRD 551
Cdd:cd05077     55 FFETASMMRQVSHKHIVLLYGVCVRDVENIMVEeFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  552 IAARNVLVS----SNDC---VKLGDFGLSrymedSTYYKASKGKLPIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMH 623
Cdd:cd05077    135 VCTKNILLAregiDGECgpfIKLSDPGIP-----ITVLSRQECVERIPWIAPECVeDSKNLSIAADKWSFGTTLWEICYN 209
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  624 GVKPfqgVKNNDVI--GRIENGERLPMPPNCpPTLYSLMTKCWAYDPSRRPRF 674
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 ...
433-675 4.99e-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: 4.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTL 509
Cdd:cd08229     32 IGRGQFSEVYRATCLLDGVP---VALKKVQifDLMDAKARADCIKEIDLLKQLNHPNVIKYyASFIEDNELNIVLELADA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDL---ASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd08229    109 GDLSRMIKHFKKQKRLipeKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNN--DVIGRIENGERLPMPPN-CPPTLYSLMTKC 663
Cdd:cd08229    189 VGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQ-SPFYGDKMNlySLCKKIEQCDYPPLPSDhYSEELRQLVNMC 266
                          250
                   ....*....|..
gi 1914779978  664 WAYDPSRRPRFT 675
Cdd:cd08229    267 INPDPEKRPDIT 278
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
426-687 7.08e-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: 7.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPenpALAVAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14072      1 NYRLLKTIGKGNFAKVKLARHVLT---GREVAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIeTEKTLYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 583
Cdd:cd14072     78 MEYASGGEVFDYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPikWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLP--MPPNCPptlySL 659
Cdd:cd14072    157 TFCGSPP--YAAPELFQGKKYDGPEvDVWSLGVILY-TLVSGSLPFDGQNLKELRERVLRGKyRIPfyMSTDCE----NL 229
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  660 MTKCWAYDPSRRprftelkAQLSTILEE 687
Cdd:cd14072    230 LKKFLVLNPSKR-------GTLEQIMKD 250
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
429-628 7.66e-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: 7.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELC 507
Cdd:cd14079      6 LGKTLGVGSFGKVKLAEH-ELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIeTPTDIFMVMEYV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd14079     85 SGGELFDYI-VQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKTSCG 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  588 KlPiKWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd14079    164 S-P-NYAAPEVISGKLYAgPEVDVWSCGVILYALLC-GSLPF 202
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
425-672 9.87e-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: 98.88  E-value: 9.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVhqgiYMSPENPA---LAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPV 500
Cdd:cd14116      5 EDFEIGRPLGKGKFGNV----YLAREKQSkfiLALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDaTRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSt 580
Cdd:cd14116     81 YLILEYAPLGTVYRELQ-KLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 yyKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLM 660
Cdd:cd14116    159 --RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV-GKPPFEANTYQETYKRISRVE-FTFPDFVTEGARDLI 234
                          250
                   ....*....|..
gi 1914779978  661 TKCWAYDPSRRP 672
Cdd:cd14116    235 SRLLKHNPSQRP 246
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
433-677 1.01e-22

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 98.82  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKncTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTLGE 511
Cdd:cd06614      8 IGEGASGEVYKATDRATGK---EVAIKKMR--LRKQNKELIINEILIMKECKHPNIVDYYDsYLVGDELWVVMEYMDGGS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFlqVRKYSLDLA-SLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymedstyyKASKGKL 589
Cdd:cd06614     83 LTDI--ITQNPVRMNeSQIAYvCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAA--------QLTKEKS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PIK-------WMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKP----------FQGVKNNdvIGRIENGERLpmppnc 652
Cdd:cd06614    153 KRNsvvgtpyWMAPEVIKRKDYGPKVDIWSLGIMCIE-MAEGEPPyleepplralFLITTKG--IPPLKNPEKW------ 223
                          250       260
                   ....*....|....*....|....*
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06614    224 SPEFKDFLNKCLVKDPEKRPSAEEL 248
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
465-687 1.30e-22

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 98.32  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  465 TSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLE 543
Cdd:cd14155     27 TLSSNRANMLREVQLMNRLSHPNILRFMGVcVHQGQLHALTEYINGGNLEQLLDSNEP-LSWTVRVKLALDIARGLSYLH 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  544 SKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDstyYKASKGKLPI----KWMAPESINFRRFTSASDVWMFGVC 616
Cdd:cd14155    106 SKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPD---YSDGKEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGII 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  617 MWEIlmhgvkpfqgvknndvIGRIE-NGERLP--------------MPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd14155    183 LCEI----------------IARIQaDPDYLPrtedfgldydafqhMVGDCPPDFLQLAFNCCNMDPKSRPSFHDIVKTL 246

                   ....*.
gi 1914779978  682 STILEE 687
Cdd:cd14155    247 EEILEK 252
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
427-671 1.43e-22

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 99.19  E-value: 1.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCtsDSVREK----FLQEALTMRQFDHPHIVKLIGVIT-ENPVW 501
Cdd:cd05580      3 FEFLKTLGTGSFGRVRLVKHKDSGKY---YALKILKKA--KIIKLKqvehVLNEKRILSEVRHPFIVNLLGSFQdDRNLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 580
Cdd:cd05580     78 MVMEYVPGGELFSLLrRSGRFPNDVAKF--YAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 Y-------YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCP 653
Cdd:cd05580    156 YtlcgtpeY-----------LAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDENPMKIYEKILEG-KIRFPSFFD 222
                          250
                   ....*....|....*...
gi 1914779978  654 PTLYSLMTKCWAYDPSRR 671
Cdd:cd05580    223 PDAKDLIKRLLVVDLTKR 240
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
424-671 1.95e-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: 1.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVHQgiymSPENPALAVAIKTCKNctsDSVREK-----FLQEALTMRQFDHPHIVKLIGVI-TE 497
Cdd:cd14161      2 KHRYEFLETLGKGTYGRVKK----ARDSSGRLVAIKSIRK---DRIKDEqdllhIRREIEIMSSLNHPHIISVYEVFeNS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd14161     75 SKIVIVMEYASRGDLYDYISERQRLSELEARHFFR-QIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKlPIkWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLPMPPN--CP 653
Cdd:cd14161    154 QDKFLQTYCGS-PL-YASPEIVNGRPYIGPEvDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGAyREPTKPSdaCG 230
                          250
                   ....*....|....*...
gi 1914779978  654 PTLYSLMTkcwayDPSRR 671
Cdd:cd14161    231 LIRWLLMV-----NPERR 243
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
433-677 2.20e-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: 98.20  E-value: 2.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELctLGE 511
Cdd:cd06640     12 IGKGSFGEVFKGIDNRTQQ---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKGTKLWIIMEY--LGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06640     87 GSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPF 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPPTLYSLMTK--------C 663
Cdd:cd06640    167 -WMAPEVIQQSAYDSKADIWSLGITAIE-LAKGEPPNSDMHPMRVLFLI--------PKNNPPTLVGDFSKpfkefidaC 236
                          250
                   ....*....|....
gi 1914779978  664 WAYDPSRRPRFTEL 677
Cdd:cd06640    237 LNKDPSFRPTAKEL 250
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
433-678 2.32e-22

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


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 97.71  E-value: 2.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymspENPALA-VAIKTCKN-------CTSDSVRekflQEALTMRQFDHPHIVKLIGVITEN---PVW 501
Cdd:cd14119      1 LGEGSYGKVKEVL----DTETLCrRAVKILKKrklrripNGEANVK----REIQILRRLNHRNVIKLVDVLYNEekqKLY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG----LSRYME 577
Cdd:cd14119     73 MVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDLFAE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKaSKGKlPiKWMAPESINFRRFTS--ASDVWMFGVCMWEILMhGVKPFQGvknnDVIGR----IENGErLPMPPN 651
Cdd:cd14119    153 DDTCTT-SQGS-P-AFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTT-GKYPFEG----DNIYKlfenIGKGE-YTIPDD 223
                          250       260
                   ....*....|....*....|....*..
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14119    224 VDPDLQDLLRGMLEKDPEKRFTIEQIR 250
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
428-672 2.33e-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: 2.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIktckNCTSDSVREKFL--QEALTMRQFDHPHIV--KLIGVITENPVWII 503
Cdd:cd08223      3 QFLRVIGKGSYGEVWLVRHKRDRKQYVIKKL----NLKNASKRERKAaeQEAKLLSKLKHPNIVsyKESFEGEDGFLYIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 582
Cdd:cd08223     79 MGFCEGGDLYTRLKEQKgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHGvkpFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLM 660
Cdd:cd08223    159 ATTLIGTPY-YMSPELFSNKPYNHKSDVWALGCCVYEMatLKHA---FNAKDMNSLVYKILEGKLPPMPKQYSPELGELI 234
                          250
                   ....*....|..
gi 1914779978  661 TKCWAYDPSRRP 672
Cdd:cd08223    235 KAMLHQDPEKRP 246
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
425-644 2.65e-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: 2.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMspENPALAVAIKTCK------NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TE 497
Cdd:cd14096      1 ENYRLINKIGEGAFSNVYKAVPL--RNTGKPVAIKVVRkadlssDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQeSD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELrsFLQVRKY---SLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSSND----------- 563
Cdd:cd14096     79 EYYYIVLELADGGEI--FHQIVRLtyfSEDLSRHVI--TQVASAVKYLHEIGVVHRDIKPENLLFEPIPfipsivklrka 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  564 ----------------------CVKLGDFGLSRYMEDSTyykaskGKLP---IKWMAPESINFRRFTSASDVWMFGVCMW 618
Cdd:cd14096    155 dddetkvdegefipgvggggigIVKLADFGLSKQVWDSN------TKTPcgtVGYTAPEVVKDERYSKKVDMWALGCVLY 228
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  619 EILMhGVKPFQGVKNNDVIGRIENGE 644
Cdd:cd14096    229 TLLC-GFPPFYDESIETLTEKISRGD 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
429-672 3.40e-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: 97.20  E-value: 3.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMsPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd14070      6 IGRKLGEGSFAKVREGLHA-VTGEKVAIKVIDKKKAKKDSyVTKNLRREGRIQQMIRHPNITQLLDILeTENSYYLVMEL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK--A 584
Cdd:cd14070     85 CPGGNLMHRI-YDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDpfS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN--DVIGRIENGERLPMPPNCPPTLYSLMTK 662
Cdd:cd14070    164 TQCGSP-AYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVEPFSlrALHQKMVDKEMNPLPTDLSPGAISFLRS 241
                          250
                   ....*....|
gi 1914779978  663 CWAYDPSRRP 672
Cdd:cd14070    242 LLEPDPLKRP 251
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
428-677 3.68e-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: 97.64  E-value: 3.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-------- 499
Cdd:cd14048      9 EPIQCLGRGGFGVVFEAKNKVDDC---NYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPpegwqekm 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 ----VWIIMELCTLGELRSFLQVRK--YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd14048     86 devyLYIQMQLCRKENLKDWMNRRCtmESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYM----------EDSTYYKASKGKLPIK-WMAPESINFRRFTSASDVWMFGVCMWEILMhgvkPFQgvKNNDVIGRIEN 642
Cdd:cd14048    166 TAMdqgepeqtvlTPMPAYAKHTGQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELIY----SFS--TQMERIRTLTD 239
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1914779978  643 GERLPMPP---NCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14048    240 VRKLKFPAlftNKYPEERDMVQQMLSPSPSERPEAHEV 277
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
429-677 3.87e-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: 3.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQgIYMSPENPALAVA-IKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVIT-ENPVWIIME 505
Cdd:cd06625      4 QGKLLGQGAFGQVYL-CYDADTGRELAVKqVEIDPINTEASKEVKALEcEIQLLKNLQHERIVQYYGCLQdEKSLSIFME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSflQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME---DSTY 581
Cdd:cd06625     83 YMPGGSVKD--EIKAYgALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQticSSTG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhgVKP----FQGVKnndVIGRIENGERLP-MPPNCPPTL 656
Cdd:cd06625    161 MKSVTGT-PY-WMSPEVINGEGYGRKADIWSVGCTVVEMLT--TKPpwaeFEPMA---AIFKIATQPTNPqLPPHVSEDA 233
                          250       260
                   ....*....|....*....|.
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06625    234 RDFLSLIFVRNKKQRPSAEEL 254
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
420-653 4.95e-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: 4.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIelgrcIGEGQFGDVHQGIYMSPENpaLAVAIKtCKNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVIT-E 497
Cdd:cd14202      2 FEFSRKDL-----IGHGAFAVVFKGRHKEKHD--LEVAVK-CINKKNLAKSQTLLgKEIKILKELKHENIVALYDFQEiA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---------SNDCVKLG 568
Cdd:cd14202     74 NSVYLVMEYCNGGDLADYLHTMR-TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  569 DFGLSRYMEDSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLpm 648
Cdd:cd14202    153 DFGFARYLQNNMMAATLCGS-PM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSL-- 227

                   ....*
gi 1914779978  649 PPNCP 653
Cdd:cd14202    228 SPNIP 232
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
433-677 6.96e-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: 97.05  E-value: 6.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELctLGE 511
Cdd:cd06642     12 IGKGSFGEVYKGIDNRTKE---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGsYLKGTKLWIIMEY--LGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06642     87 GSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPF 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPPTLYSLMTK--------C 663
Cdd:cd06642    167 -WMAPEVIKQSAYDFKADIWSLGITAIE-LAKGEPPNSDLHPMRVLFLI--------PKNSPPTLEGQHSKpfkefveaC 236
                          250
                   ....*....|....
gi 1914779978  664 WAYDPSRRPRFTEL 677
Cdd:cd06642    237 LNKDPRFRPTAKEL 250
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
468-677 7.41e-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: 96.27  E-value: 7.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  468 SVREKFLQEALTMRqfdHPHIVKLIGV----ITENPVW---IIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALA 540
Cdd:cd14012     43 QLLEKELESLKKLR---HPNLVSYLAFsierRGRSDGWkvyLLTEYAPGGSLSELLD-SVGSVPLDTARRWTLQLLEALE 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  541 YLESKRFVHRDIAARNVLVSSNDC---VKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINF-RRFTSASDVWMFGVC 616
Cdd:cd14012    119 YLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMCSRGSLDEFKQTYWLPPELAQGsKSPTRKTDVWDLGLL 198
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  617 MWEILmhgvkpfQGVknnDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14012    199 FLQML-------FGL---DVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
433-677 9.10e-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: 96.19  E-value: 9.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiYMSPEnpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENpvwiimELCTL--- 509
Cdd:cd14066      1 IGSGGFGTVYKG-VLENG---TVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLES------DEKLLvye 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 ----GELRSFLQVRKYS--LDLASLILYAYQLSTALAYLESKRF---VHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDS 579
Cdd:cd14066     71 ympnGSLEDRLHCHKGSppLPWPQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIpPSE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI---------ENGERL--PM 648
Cdd:cd14066    151 SVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVDENRENASRKDLvewveskgkEELEDIldKR 229
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  649 PPNCPP-------TLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14066    230 LVDDDGveeeeveALLRLALLCTRSDPSLRPSMKEV 265
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
426-677 9.43e-22

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: 96.39  E-value: 9.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELgrcIGEGQFGDVHQGIYMSPENpalAVAIK-----TCKNCTSDSVRE-KFLQEaltMRQFDHPHIVKLIGVITENP 499
Cdd:cd06917      5 RLEL---VGRGSYGAVYRGYHVKTGR---VVALKvlnldTDDDDVSDIQKEvALLSQ---LKLGQPKNIIKYYGSYLKGP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 -VWIIMELCTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd06917     76 sLWIIMDYCEGGSIRTLMRAGPIAERYIAVIMR--EVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 STYYKASKGKLPIkWMAPESI-NFRRFTSASDVWMFGVCMWEIlMHGVKPFQGVKNNDVIGRIENGErlpmPPNCPPTLY 657
Cdd:cd06917    154 NSSKRSTFVGTPY-WMAPEVItEGKYYDTKADIWSLGITTYEM-ATGNPPYSDVDALRAVMLIPKSK----PPRLEGNGY 227
                          250       260
                   ....*....|....*....|....*
gi 1914779978  658 SLMTK-----CWAYDPSRRPRFTEL 677
Cdd:cd06917    228 SPLLKefvaaCLDEEPKDRLSADEL 252
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
427-679 9.58e-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: 9.58e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRcIGEGQFGDVHQgiyMSPENPALAVAIKTCKnCTSDSVREK-FLQEA-LTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd06616      9 KDLGE-IGRGAFGTVNK---MLHKPSGTIMAVKRIR-STVDEKEQKrLLMDLdVVMRSSDCPYIVKFYGALfREGDCWIC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLgelrsflqvrkySLDLASLILYAYQLST---------------ALAYL-ESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:cd06616     84 MELMDI------------SLDKFYKYVYEVLDSVipeeilgkiavatvkALNYLkEELKIIHRDVKPSNILLDRNGNIKL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDSTYYKASKGKLPikWMAPESINFRRFTSA----SDVWMFGVCMWEiLMHGVKPFQGVKNN-DVIGRIEN 642
Cdd:cd06616    152 CDFGISGQLVDSIAKTRDAGCRP--YMAPERIDPSASRDGydvrSDVWSLGITLYE-VATGKFPYPKWNSVfDQLTQVVK 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  643 GErlpmPPNCPPTL---YSLMTK-----CWAYDPSRRPRFTELKA 679
Cdd:cd06616    229 GD----PPILSNSEereFSPSFVnfvnlCLIKDESKRPKYKELLK 269
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
433-677 9.86e-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: 9.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTLGE 511
Cdd:cd06641     12 IGKGSFGEVFKGIDNRTQK---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKDTKLWIIMEYLGGGS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06641     89 ALDLLE--PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTPF 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPPTL---YS-----LMTKC 663
Cdd:cd06641    167 -WMAPEVIKQSAYDSKADIWSLGITAIE-LARGEPPHSELHPMKVLFLI--------PKNNPPTLegnYSkplkeFVEAC 236
                          250
                   ....*....|....
gi 1914779978  664 WAYDPSRRPRFTEL 677
Cdd:cd06641    237 LNKEPSFRPTAKEL 250
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
426-687 9.93e-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: 9.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 504
Cdd:cd14152      1 QIELGELIGQGRWGKVHRGRW----HGEVAIRLLEIDGNNQDHLK-LFKKEVMNYRQTRHENVVLFMGACMHPPhLAIIT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV--KLGDFGLSRYMEDSTyy 582
Cdd:cd14152     76 SFCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVQEGR-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLPIKW---MAPESI---------NFRRFTSASDVWMFGVcMWEILMHGVKPFQGVKNNDVIGRIENGE---RLP 647
Cdd:cd14152    154 RENELKLPHDWlcyLAPEIVremtpgkdeDCLPFSKAADVYAFGT-IWYELQARDWPLKNQPAEALIWQIGSGEgmkQVL 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  648 MPPNCPPTLYSLMTKCWAYDPSRRPRFTelkaQLSTILEE 687
Cdd:cd14152    233 TTISLGKEVTEILSACWAFDLEERPSFT----LLMDMLEK 268
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
430-644 1.09e-21

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: 96.08  E-value: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIYMSPENPAlavAIKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWIIMELC 507
Cdd:cd14097      6 GRKLGQGSFGVVIEATHKETQTKW---AIKKINREKAGSSAVKLLErEVDILKHVNHAHIIHLEEVFeTPKRMYLVMELC 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRK-YSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLVSSNDC-------VKLGDFGLS--RYME 577
Cdd:cd14097     83 EDGELKELLLRKGfFSENETRHIIQS--LASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSvqKYGL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  578 DSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE 644
Cdd:cd14097    161 GEDMLQETCGT-PI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRKGD 224
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
419-677 1.25e-21

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: 95.45  E-value: 1.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGV-ITE 497
Cdd:cd06613      1 DYELIQR-------IGSGTYGDVYKARNIATGE---LAAVKVIKLEPGDDFEI-IQQEISMLKECRHPNIVAYFGSyLRR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQVrkysLDLASLILYAY---QLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd06613     70 DKLWIVMEYCGGGSLQDIYQV----TGPLSELQIAYvcrETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDSTyykaSKGKLPIK---WMAPESINFRR---FTSASDVWMFGVC---MWEIL--MHGVKP----FQGVKNNDVIGR 639
Cdd:cd06613    146 QLTATI----AKRKSFIGtpyWMAPEVAAVERkggYDGKCDIWALGITaieLAELQppMFDLHPmralFLIPKSNFDPPK 221
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1914779978  640 IENGERLpmppncPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06613    222 LKDKEKW------SPDFHDFIKKCLTKNPKKRPTATKL 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
426-671 2.07e-21

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


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 94.76  E-value: 2.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKNC--TSDSVREKFLQEALTMRQFDHPHIVKLIGVItEN--PVW 501
Cdd:cd14073      2 RYELLETLGKGTYGKVKLAIERATGR---EVAIKSIKKDkiEDEQDMVRIRREIEIMSSLNHPHIIRIYEVF-ENkdKIV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd14073     78 IVMEYASGGELYDYISERR-RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKlPIkWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGERlpMPPNCPPTLYSLM 660
Cdd:cd14073    157 LQTFCGS-PL-YASPEIVNGTPYQGPEvDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQISSGDY--REPTQPSDASGLI 231
                          250
                   ....*....|.
gi 1914779978  661 TKCWAYDPSRR 671
Cdd:cd14073    232 RWMLTVNPKRR 242
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
473-682 2.63e-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: 94.99  E-value: 2.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  473 FLQEALTMRQFDHPHIVKLIGvITENPVWIIMELCTLGELRSFLQvrKYSLDLASLILY-----AYQLSTALAYLESKRF 547
Cdd:cd14000     57 LRQELTVLSHLHHPSIVYLLG-IGIHPLMLVLELAPLGSLDHLLQ--QDSRSFASLGRTlqqriALQVADGLRYLHSAMI 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDC-----VKLGDFGLSRYmedsTYYKASKGKLPIK-WMAPESINFR-RFTSASDVWMFGVCMWEI 620
Cdd:cd14000    134 IYRDLKSHNVLVWTLYPnsaiiIKIADYGISRQ----CCRMGAKGSEGTPgFRAPEIARGNvIYNEKVDVFSFGMLLYEI 209
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  621 LmHGVKPFQGVKNNDVIGRIENGERLPM-PPNC--PPTLYSLMTKCWAYDPSRRPRFTELKAQLS 682
Cdd:cd14000    210 L-SGGAPMVGHLKFPNEFDIHGGLRPPLkQYECapWPEVEVLMKKCWKENPQQRPTAVTVVSILN 273
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
433-683 4.72e-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: 4.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiYMSPENPALAVAIKTCkNCTS-----------DSVREKFLQEALTMRQFDHPHIVKLIGVITENP-V 500
Cdd:cd08528      8 LGSGAFGCVYK--VRKKSNGQTLLALKEI-NMTNpafgrteqerdKSVGDIISEVNIIKEQLRHPNIVRYYKTFLENDrL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMEL---CTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYL-ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY- 575
Cdd:cd08528     85 YIVMELiegAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQk 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPMPPNcppt 655
Cdd:cd08528    165 GPESSKMTSVVGT--ILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQ-PPFYSTNMLTLATKIVEAEYEPLPEG---- 237
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1914779978  656 LYS-----LMTKCWAYDPSRRPRFTELKAQLST 683
Cdd:cd08528    238 MYSdditfVIRSCLTPDPEARPDIVEVSSMISD 270
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
432-684 5.45e-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: 94.43  E-value: 5.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  432 CIGEGQFGDVHQGIYMspeNPALAVAIKTCKNCTSdSVREKFLQEALTMRqfdHPHIVKLI-----GVITENPVWIIMEL 506
Cdd:cd13998      2 VIGKGRFGEVWKASLK---NEPVAVKIFSSRDKQS-WFREKEIYRTPMLK---HENILQFIaaderDTALRTELWLVTAF 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRF---------VHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd13998     75 HPNGSL*DYL--SLHTIDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKSKNILVKNDGTCCIADFGLAVRLS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYY--KASKGKL-PIKWMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK----------PFQG-VKNNDVI 637
Cdd:cd13998    153 PSTGEedNANNGQVgTKRYMAPEvlegAINLRDFESfkRVDIYAMGLVLWEMASRCTDlfgiveeykpPFYSeVPNHPSF 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  638 GRI-ENGERLPMPPNCPP---------TLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd13998    233 EDMqEVVVRDKQRPNIPNrwlshpglqSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
431-677 7.82e-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: 93.61  E-value: 7.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENpalAVAIKTCK-----NCTSDSVRE--KFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 502
Cdd:cd14084     12 RTLGSGACGEVKLAYDKSTCK---KVAIKIINkrkftIGSRREINKprNIETEIEILKKLSHPCIIKIEDFFdAEDDYYI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDS 579
Cdd:cd14084     89 VLELMEGGELFDRV-VSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSKILGET 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKlpIKWMAPESINF---RRFTSASDVWMFGVCMWeILMHGVKPFQG-VKNNDVIGRIENGERLPMPP---NC 652
Cdd:cd14084    168 SLMKTLCGT--PTYLAPEVLRSfgtEGYTRAVDCWSLGVILF-ICLSGYPPFSEeYTQMSLKEQILSGKYTFIPKawkNV 244
                          250       260
                   ....*....|....*....|....*
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14084    245 SEEAKDLVKKMLVVDPSRRPSIEEA 269
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
433-677 8.17e-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: 93.56  E-value: 8.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVhQGIYMSPENPALAVaiKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGe 511
Cdd:cd06605      9 LGEGNGGVV-SKVRHRPSGQIMAV--KVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAfYSEGDISICMEYMDGG- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 lrSFLQVRKYSLDLASLIL--YAYQLSTALAYLESKR-FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyYKASKGK 588
Cdd:cd06605     85 --SLDKILKEVGRIPERILgkIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSL-AKTFVGT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIE------NGErlpmPPNCP-----PTLY 657
Cdd:cd06605    162 RS--YMAPERISGGKYTVKSDIWSLGLSLVE-LATGRFPYPPPNAKPSMMIFEllsyivDEP----PPLLPsgkfsPDFQ 234
                          250       260
                   ....*....|....*....|
gi 1914779978  658 SLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06605    235 DFVSQCLQKDPTERPSYKEL 254
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
427-674 9.88e-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: 93.04  E-value: 9.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYMSPENPA-------LAVAIKTCKNCTsdsvrEKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:cd14208      1 LTFMESLGKGSFTKIYRGLRTDEEDDErcetevlLKVMDPTHGNCQ-----ESFLEAASIMSQISHKHLVLLHGVCVGKD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASL--ILYAYQLSTALAYLESKRFVHRDIAARNVLVS------SNDCVKLGDFG 571
Cdd:cd14208     76 SIMVQEFVCHGALDLYLKKQQQKGPVAISwkLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSregdkgSPPFIKLSDPG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  572 LSRYMEDSTYYKASkgklpIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPP 650
Cdd:cd14208    156 VSIKVLDEELLAER-----IPWVAPECLsDPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPH 230
                          250       260
                   ....*....|....*....|....
gi 1914779978  651 NCppTLYSLMTKCWAYDPSRRPRF 674
Cdd:cd14208    231 WI--ELASLIQQCMSYNPLLRPSF 252
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
474-677 1.05e-20

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: 92.87  E-value: 1.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  474 LQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQ-VRKYSLDLA-SLIL-YAYQLSTALAYLESKRFVH 549
Cdd:cd08222     50 NREAKLLSKLDHPAIVKFHDSFVEKEsFCIVTEYCEGGDLDDKISeYKKSGTTIDeNQILdWFIQLLLAVQYMHERRILH 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  550 RDIAARNVLVsSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHGvkp 627
Cdd:cd08222    130 RDLKAKNIFL-KNNVIKVGDFGISRILMGTSDLATTFTGTPY-YMSPEVLKHEGYNSKSDIWSLGCILYEMccLKHA--- 204
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  628 FQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd08222    205 FDGQNLLSVMYKIVEGETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEI 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
426-672 1.12e-20

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 93.79  E-value: 1.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTS---------DSVRE-KFLQEaltmrqFDHPHIVKLIGVI 495
Cdd:cd07841      1 RYEKGKKLGEGTYAVVYKARDKETGRI---VAIKKIKLGERkeakdginfTALREiKLLQE------LKHPNIIGLLDVF 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENP-VWIIMELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd07841     72 GHKSnINLVFEFME-TDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDST----------YYKaskgklpikwmAPESInF--RRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-- 640
Cdd:cd07841    151 SFGSPNrkmthqvvtrWYR-----------APELL-FgaRHYGVGVDMWSVGCIFAE-LLLRVPFLPGDSDIDQLGKIfe 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  641 --------------------ENGERLPMP-----PNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd07841    218 algtpteenwpgvtslpdyvEFKPFPPTPlkqifPAASDDALDLLQRLLTLNPNKRI 274
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
433-677 1.57e-20

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: 1.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiyMSPENPALAVA--IKTckncTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTL 509
Cdd:cd06644     20 LGDGAFGKVYKA--KNKETGALAAAkvIET----KSEEELEDYMVEIEILATCNHPYIVKLLGAFYwDGKLWIMIEFCPG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 589
Cdd:cd06644     94 GAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGT 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PIkWMAPESINFRRFTSA-----SDVWMFGVCMWEILM-----HGVKPFQgvknndVIGRIENGE--RLPMPPNCPPTLY 657
Cdd:cd06644    174 PY-WMAPEVVMCETMKDTpydykADIWSLGITLIEMAQiepphHELNPMR------VLLKIAKSEppTLSQPSKWSMEFR 246
                          250       260
                   ....*....|....*....|
gi 1914779978  658 SLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06644    247 DFLKTALDKHPETRPSAAQL 266
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
473-674 1.66e-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: 1.66e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  473 FLQEALTMRQFDHPHIVKLIGVITENPVWIIM-ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRD 551
Cdd:cd05076     62 FFETASLMSQVSHTHLVFVHGVCVRGSENIMVeEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHGN 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  552 IAARNVLVS-------SNDCVKLGDFG-----LSRymEDSTYYkaskgklpIKWMAPESI-NFRRFTSASDVWMFGVCMW 618
Cdd:cd05076    142 VCAKNILLArlgleegTSPFIKLSDPGvglgvLSR--EERVER--------IPWIAPECVpGGNSLSTAADKWGFGATLL 211
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  619 EILMHGVKPFQGVKNNDVIGRIENGERLPmPPNCpPTLYSLMTKCWAYDPSRRPRF 674
Cdd:cd05076    212 EICFNGEAPLQSRTPSEKERFYQRQHRLP-EPSC-PELATLISQCLTYEPTQRPSF 265
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
429-679 1.70e-20

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: 92.39  E-value: 1.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSPENpALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIGVITENPV-WIIMELC 507
Cdd:cd14069      5 LVQTLGEGAFGEVFLAVNRNTEE-AVAVKFVDMKRAPGDC-PENIKKEVCIQKMLSHKNVVRFYGHRREGEFqYLFLEYA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELrsFLQVR-KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS---RYMEDSTYYK 583
Cdd:cd14069     83 SGGEL--FDKIEpDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfRYKGKERLLN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPikWMAPESINFRRF-TSASDVWMFGVCMWEILMhGVKPFQGVKNNDV--IGRIENGERLPMP-PNCPPTLYSL 659
Cdd:cd14069    161 KMCGTLP--YVAPELLAKKKYrAEPVDVWSCGIVLFAMLA-GELPWDQPSDSCQeySDWKENKKTYLTPwKKIDTAALSL 237
                          250       260
                   ....*....|....*....|
gi 1914779978  660 MTKCWAYDPSRRPRFTELKA 679
Cdd:cd14069    238 LRKILTENPNKRITIEDIKK 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
425-679 1.79e-20

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: 92.75  E-value: 1.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMspeNPALAVAIKTCKNcTSDSvREKFLQEALTMRQF-DHPHIVKLIGV-------IT 496
Cdd:cd06608      6 GIFELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMDI-IEDE-EEEIKLEINILRKFsNHPNIATFYGAfikkdppGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLG---ELRSFLQVRKYSL--DLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 571
Cdd:cd06608     81 DDQLWLVMEYCGGGsvtDLVKGLRKKGKRLkeEWIAYILR--ETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  572 LSRYMeDSTYYK--ASKGKlPIkWMAPESINF-----RRFTSASDVWMFGVCMWEiLMHGVKPFqgvknndvigrienGE 644
Cdd:cd06608    159 VSAQL-DSTLGRrnTFIGT-PY-WMAPEVIACdqqpdASYDARCDVWSLGITAIE-LADGKPPL--------------CD 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  645 RLPM------PPNCPPTLYS----------LMTKCWAYDPSRRPRFTELKA 679
Cdd:cd06608    221 MHPMralfkiPRNPPPTLKSpekwskefndFISECLIKNYEQRPFTEELLE 271
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
431-671 2.16e-20

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: 93.23  E-value: 2.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCT---SDSVREKFLQEALTmrQFDHPHIVKL-IGVITENPVWIIMEL 506
Cdd:cd05582      1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATlkvRDRVRTKMERDILA--DVNHPFIVKLhYAFQTEGKLYLILDF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTyyKAS 585
Cdd:cd05582     79 LRGGDLFTRLS-KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEK--KAY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCWA 665
Cdd:cd05582    156 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRALFK 233

                   ....*.
gi 1914779978  666 YDPSRR 671
Cdd:cd05582    234 RNPANR 239
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
436-674 2.48e-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: 91.93  E-value: 2.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  436 GQFGDVHQGIYMspenpaLAVAIKTCKNCTsdsvrEKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGELRS 514
Cdd:cd05078     24 GDYGQLHETEVL------LKVLDKAHRNYS-----ESFFEAASMMSQLSHKHLVLNYGVcVCGDENILVQEYVKFGSLDT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  515 FLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND--------CVKLGDFGLSRYMEDSTYYKASk 586
Cdd:cd05078     93 YLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIREEdrktgnppFIKLSDPGISITVLPKDILLER- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 gklpIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCppTLYSLMTKCWA 665
Cdd:cd05078    172 ----IPWVPPECIeNPKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWT--ELANLINNCMD 245

                   ....*....
gi 1914779978  666 YDPSRRPRF 674
Cdd:cd05078    246 YEPDHRPSF 254
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
430-677 2.99e-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: 91.72  E-value: 2.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFG------DVHQGIYMspenpalAVA-IKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVITENPV 500
Cdd:cd06630      5 GPLLGTGAFSscyqarDVKTGTLM-------AVKqVSFCRNSSSEQeeVVEAIREEIRMMARLNHPNIVRMLGATQHKSH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 W-IIMELCTLGELRSFLQvrKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV-SSNDCVKLGDFG-LSRYM 576
Cdd:cd06630     78 FnIFVEWMAGGSVASLLS--KYgAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVdSTGQRLRIADFGaAARLA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTYYKASKGKL--PIKWMAPESINFRRFTSASDVWMFGVCMweILMHGVKPFQGVKNND----VIGRIENGERLP-MP 649
Cdd:cd06630    156 SKGTGAGEFQGQLlgTIAFMAPEVLRGEQYGRSCDVWSVGCVI--IEMATAKPPWNAEKISnhlaLIFKIASATTPPpIP 233
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  650 PNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06630    234 EHLSPGLRDVTLRCLELQPEDRPPAREL 261
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
428-671 3.14e-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: 91.30  E-value: 3.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 505
Cdd:cd14071      3 DIERTIGKGNFAVVKLARHRITKT---EVAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMeTKDMLYLVTE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFL-QVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 584
Cdd:cd14071     80 YASNGEIFDYLaQHGRMSEKEARKKFW--QILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKLPikWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLP--MPPNCPptlySLM 660
Cdd:cd14071    158 WCGSPP--YAAPEVFEGKEYEGPQlDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVLSGRfRIPffMSTDCE----HLI 230
                          250
                   ....*....|.
gi 1914779978  661 TKCWAYDPSRR 671
Cdd:cd14071    231 RRMLVLDPSKR 241
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
433-663 3.34e-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: 3.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiyMSPENPALAVAiKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGE 511
Cdd:cd06643     13 LGDGAFGKVYKA--QNKETGILAAA-KVIDTKSEEEL-EDYMVEIDILASCDHPNIVKLLDAFYyENNLWILIEFCAGGA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06643     89 VDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGTPY 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 kWMAPESI-----NFRRFTSASDVWMFGVCMWEILM-----HGVKPFQgvknndVIGRIENGE--RLPMPPNCPPTLYSL 659
Cdd:cd06643    169 -WMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQiepphHELNPMR------VLLKIAKSEppTLAQPSRWSPEFKDF 241

                   ....
gi 1914779978  660 MTKC 663
Cdd:cd06643    242 LRKC 245
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
419-671 4.37e-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: 91.62  E-value: 4.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIqrerieLGRcIGEGQFGDVHQGIYM-SPENPALA-VAIKTCKNCTSDS-VRE-KFLQEALtmrqfDHPHIVKLIGV 494
Cdd:cd07832      1 RYKI------LGR-IGEGAHGIVFKAKDReTGETVALKkVALRKLEGGIPNQaLREiKALQACQ-----GHPYVVKLRDV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITENP-VWIIMELcTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd07832     69 FPHGTgFVLVFEY-MLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYM--EDSTYYKASKGKlpiKW-MAPESI-NFRRFTSASDVWMFGVCMWEILmHGVKPFQGvkNND------VI------ 637
Cdd:cd07832    148 RLFseEDPRLYSHQVAT---RWyRAPELLyGSRKYDEGVDLWAVGCIFAELL-NGSPLFPG--ENDieqlaiVLrtlgtp 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  638 --------------GRIENGERLPMP-----PNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd07832    222 nektwpeltslpdyNKITFPESKGIRleeifPDCSPEAIDLLKGLLVYNPKKR 274
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
433-672 4.51e-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: 91.56  E-value: 4.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVITENP---VWIIMELCT 508
Cdd:cd07831      7 IGEGTFSEVLKAQSRKTGK---YYAIKCMKKHFKSLEQVNNLREIQALRRLsPHPNILRLIEVLFDRKtgrLALVFELMD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LgELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSNDCVKLGDFGLSRymedSTYykaskGK 588
Cdd:cd07831     84 M-NLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCR----GIY-----SK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LP------IKWM-APESI-NFRRFTSASDVWMFGVCMWEILmhGVKP-FQGVKNNDVIGRIENGERLPMP---------- 649
Cdd:cd07831    153 PPyteyisTRWYrAPECLlTDGYYGPKMDIWAVGCVFFEIL--SLFPlFPGTNELDQIAKIHDVLGTPDAevlkkfrksr 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  650 ------------------PNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd07831    231 hmnynfpskkgtglrkllPNASAEGLDLLKKLLAYDPDERI 271
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
432-672 4.59e-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: 91.56  E-value: 4.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  432 CIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-------GVITEnpVWII 503
Cdd:cd14056      2 TIGKGRYGEVWLGKYRGEK-----VAVKIFSSRDEDSwFRETEIYQTVMLR---HENILGFIaadikstGSWTQ--LWLI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDFGLS-R 574
Cdd:cd14056     72 TEYHEHGSLYDYLQ--RNTLDTEEALRLAYSAASGLAHLHTEIVgtqgkpaiAHRDLKSKNILVKRDGTCCIADLGLAvR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDStyykaSKGKLPI-------KWMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK---------PFQGVK 632
Cdd:cd14056    150 YDSDT-----NTIDIPPnprvgtkRYMAPEvlddSINPKSFESfkMADIYSFGLVLWEIARRCEIggiaeeyqlPYFGMV 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  633 NND---------VIGRienGERLPMPP---NCP--PTLYSLMTKCWAYDPSRRP 672
Cdd:cd14056    225 PSDpsfeemrkvVCVE---KLRPPIPNrwkSDPvlRSMVKLMQECWSENPHARL 275
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
419-677 5.45e-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: 5.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRERIELGRcigeGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREkfLQEALTM-RQFDHPHIVKLIGVITE 497
Cdd:cd06624      6 EYDESGERVVLGK----GTFGVVYAARDLSTQ---VRIAIKEIPERDSREVQP--LHEEIALhSRLSHKNIVQYLGSVSE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVW-IIMELCTLGELRSFLQVRKYSL--DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS-NDCVKLGDFGLS 573
Cdd:cd06624     77 DGFFkIFMEQVPGGSLSALLRSKWGPLkdNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 -RYMEDSTYYKASKGKLpiKWMAPESIN--FRRFTSASDVWMFGVCMWEiLMHGVKPFqgvknndvigrIENGE------ 644
Cdd:cd06624    157 kRLAGINPCTETFTGTL--QYMAPEVIDkgQRGYGPPADIWSLGCTIIE-MATGKPPF-----------IELGEpqaamf 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  645 ---RLPMPPNCPPTLY----SLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06624    223 kvgMFKIHPEIPESLSeeakSFILRCFEPDPDKRATASDL 262
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
480-677 5.89e-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: 91.67  E-value: 5.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  480 MRQFDHPHIVKLIGV-ITENPVWIIMEL---CtlgeLRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFV-HRDIAA 554
Cdd:cd06618     68 LKSHDCPYIVKCYGYfITDSDVFICMELmstC----LDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHGViHRDVKP 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  555 RNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPikWMAPESI---NFRRFTSASDVWMFGVCMWEiLMHGVKPFQGV 631
Cdd:cd06618    144 SNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAA--YMAPERIdppDNPKYDIRADVWSLGISLVE-LATGQFPYRNC 220
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  632 KNN-DVIGRIENGE--RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06618    221 KTEfEVLTKILNEEppSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYREL 269
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
427-672 6.19e-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: 6.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRcIGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP---VWII 503
Cdd:cd06621      4 VELSS-LGEGAGGSVTKCRL---RNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQdssIGIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFL-QVRKYSLDLASLIL--YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS- 579
Cdd:cd06621     80 MEYCEGGSLDSIYkKVKKKGGRIGEKVLgkIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSl 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 -------TYYkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEIlMHGVKPF--QGVKNNDVIGRIENGERLPMP- 649
Cdd:cd06621    160 agtftgtSYY-----------MAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFppEGEPPLGPIELLSYIVNMPNPe 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  650 -PNCPP-------TLYSLMTKCWAYDPSRRP 672
Cdd:cd06621    228 lKDEPEngikwseSFKDFIEKCLEKDGTRRP 258
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
456-679 6.91e-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: 90.74  E-value: 6.91e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKTCKNctSDSVREKFLQEALTMR----QFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFLqvRKY-SLDLASLI 529
Cdd:cd05579     21 YAIKVIKK--RDMIRKNQVDSVLAERnilsQAQNPFVVKLYySFQGKKNLYLVMEYLPGGDLYSLL--ENVgALDEDVAR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  530 LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKASKGKLPIK-------------WMA 595
Cdd:cd05579     97 IYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVgLVRRQIKLSIQKKSNGApekedrrivgtpdYLA 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  596 PESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMP--PNCPPTLYSLMTKCWAYDPSRRP- 672
Cdd:cd05579    177 PEILLGQGHGKTVDWWSLGVILYEFLV-GIPPFHAETPEEIFQNILNG-KIEWPedPEVSDEAKDLISKLLTPDPEKRLg 254

                   ....*....
gi 1914779978  673 --RFTELKA 679
Cdd:cd05579    255 akGIEEIKN 263
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
424-677 7.16e-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: 90.76  E-value: 7.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVHQGIYM-SPENPALAVAIKTCknCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VW 501
Cdd:cd14187      6 RRRYVRGRFLGKGGFAKCYEITDAdTKEVFAGKIVPKSL--LLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDfVY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCtlgELRSFLQV--RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd14187     84 VVLELC---RRRSLLELhkRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSL 659
Cdd:cd14187    161 GERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNE-YSIPKHINPVAASL 237
                          250
                   ....*....|....*...
gi 1914779978  660 MTKCWAYDPSRRPRFTEL 677
Cdd:cd14187    238 IQKMLQTDPTARPTINEL 255
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
468-677 8.20e-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: 8.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  468 SVREKFLQEALTMRQFDHPHIVKLIGV-ITENP-VWIIMELCTLGELRSFLQVRK-YSLDLASLIlyAYQLSTALAYLES 544
Cdd:cd06620     45 SVRKQILRELQILHECHSPYIVSFYGAfLNENNnIIICMEYMDCGSLDKILKKKGpFPEEVLGKI--AVAVLEGLTYLYN 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  545 K-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS---TYYKASkgklpiKWMAPESINFRRFTSASDVWMFGVCMWEI 620
Cdd:cd06620    123 VhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSiadTFVGTS------TYMSPERIQGGKYSVKSDVWSLGLSIIEL 196
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  621 LMHGVkPFQGVKNN-----------DVIGRIENGE--RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06620    197 ALGEF-PFAGSNDDddgyngpmgilDLLQRIVNEPppRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLL 265
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
433-678 8.75e-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: 8.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIY-MSPENpalaVAIKTCKNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTL 509
Cdd:cd14075     10 LGSGNFSQVKLGIHqLTKEK----VAIKILDKTKLDQKTQRLLsREISSMEKLHHPNIIRLYEVVeTLSKLHLVMEYASG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 589
Cdd:cd14075     86 GELYTKISTEGKLSESEAKPLFA-QIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTFCGSP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PikWMAPEsinfrRFTSAS------DVWMFGVcMWEILMHGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKC 663
Cdd:cd14075    165 P--YAAPE-----LFKDEHyigiyvDIWALGV-LLYFMVTGVMPFRAETVAKLKKCILEG-TYTIPSYVSEPCQELIRGI 235
                          250
                   ....*....|....*
gi 1914779978  664 WAYDPSRRPRFTELK 678
Cdd:cd14075    236 LQPVPSDRYSIDEIK 250
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
433-629 9.57e-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: 9.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCKnctSDSVREK-FLQE-ALTMRQFDHPHIVKLIGVITENPVWII--MELCT 508
Cdd:cd13987      1 LGEGTYGKVLLAVHKGSGTK---MALKFVP---KPSTKLKdFLREyNISLELSVHPHIIKTYDVAFETEDYYVfaQEYAP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRyMEDSTyYKASK 586
Cdd:cd13987     75 YGDLFSIIPPQV-GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTR-RVGST-VKRVS 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  587 GKLPikWMAPESINFRRFTS-----ASDVWMFGV---CM------WEILMHGVKPFQ 629
Cdd:cd13987    152 GTIP--YTAPEVCEAKKNEGfvvdpSIDVWAFGVllfCCltgnfpWEKADSDDQFYE 206
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
419-660 1.73e-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: 1.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRERIelgrcIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekFLQEALTMRQFDHPHIVKLIGVI-TE 497
Cdd:cd14201      5 DFEYSRKDL-----VGHGAFAVVFKGRHRKKTDWEVAIKSINKKNLSKSQIL--LGKEIKILKELQHENIVALYDVQeMP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLQVrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---------SNDCVKLG 568
Cdd:cd14201     78 NSVFLVMEYCNGGDLADYLQA-KGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  569 DFGLSRYMEdSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERL-- 646
Cdd:cd14201    157 DFGFARYLQ-SNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCLV-GKPPFQANSPQDLRMFYEKNKNLqp 233
                          250
                   ....*....|....
gi 1914779978  647 PMPPNCPPTLYSLM 660
Cdd:cd14201    234 SIPRETSPYLADLL 247
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
425-630 1.78e-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: 89.67  E-value: 1.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSpenPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14183      6 ERYKVGRTIGDGNFAVVKECVERS---TGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMdMPTELYLV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGEL-RSFLQVRKYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMED 578
Cdd:cd14183     83 MELVKGGDLfDAITSTNKYTERDASGML--YNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDG 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  579 STYYKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQG 630
Cdd:cd14183    161 PLYTVCGTP----TYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRG 207
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
428-671 1.85e-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: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd14185      3 EIGRTIGDGNFAVVKE---CRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYeTEKEIYLILEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYMEDSTY 581
Cdd:cd14185     80 VRGGDLfDAIIESVKFTEHDAALMII--DLCEALVYIHSKHIVHRDLKPENLLVQHNPdkstTLKLADFGLAKYVTGPIF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNN--DVIGRIENGERLPMPP---NCPPTL 656
Cdd:cd14185    158 TVCGTP----TYVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFRSPERDqeELFQIIQLGHYEFLPPywdNISEAA 232
                          250
                   ....*....|....*
gi 1914779978  657 YSLMTKCWAYDPSRR 671
Cdd:cd14185    233 KDLISRLLVVDPEKR 247
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
466-680 2.30e-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: 88.99  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  466 SDSVREKFLQEALTMRQFDHPHIVK-----LIGviteNPVWIIMELCTLGELRSFLQVRKYSLDL--ASLIL-YAYQLST 537
Cdd:cd08530     39 SQKEREDSVNEIRLLASVNHPNIIRykeafLDG----NRLCIVMEYAPFGDLSKLISKRKKKRRLfpEDDIWrIFIQMLR 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  538 ALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLpikWMAPESINFRRFTSASDVWMFGVCM 617
Cdd:cd08530    115 GLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAKTQIGTPL---YAAPEVWKGRPYDYKSDIWSLGCLL 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  618 WEiLMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ 680
Cdd:cd08530    192 YE-MATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
428-630 2.72e-19

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: 89.08  E-value: 2.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKT--CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 504
Cdd:cd14105      8 DIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKrrSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTdVVLIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC----VKLGDFGLSRYMEDST 580
Cdd:cd14105     88 ELVAGGELFDFL-AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIEDGN 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQG 630
Cdd:cd14105    167 EFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 213
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
428-678 3.20e-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: 3.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPenpALAVAIKTCKNCTSDSV-REKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 505
Cdd:cd14074      6 DLEETLGRGHFAVVKLARHVFT---GEKVAVKVIDKTKLDDVsKAHLFQEVRCMKLVQHPNVVRLYEVIdTQTKLYLILE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-SNDCVKLGDFGLSRYMEDSTYYKA 584
Cdd:cd14074     83 LGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFeKQGLVKLTDFGFSNKFQPGEKLET 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKLpiKWMAPESINFRRFTS-ASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKC 663
Cdd:cd14074    163 SCGSL--AYSAPEILLGDEYDApAVDIWSLGVILY-MLVCGQPPFQEANDSETLTMIMDC-KYTVPAHVSPECKDLIRRM 238
                          250
                   ....*....|....*
gi 1914779978  664 WAYDPSRRPRFTELK 678
Cdd:cd14074    239 LIRDPKKRASLEEIE 253
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
467-671 4.51e-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: 88.08  E-value: 4.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  467 DSVReKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESK 545
Cdd:cd05578     42 DSVR-NVLNELEILQELEHPFLVNLWYSFQdEEDMYMVVDLLLGGDLRYHLQ-QKVKFSEETVKFYICEIVLALDYLHSK 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  546 RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGV 625
Cdd:cd05578    120 NIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYEMLR-GK 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1914779978  626 KPFQG--VKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05578    197 RPYEIhsRTSIEEIRAKFETASVLYPAGWSEEAIDLINKLLERDPQKR 244
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
470-686 4.58e-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: 4.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFV 548
Cdd:cd14156     32 QHKIVREISLLQKLSHPNIVRYLGIcVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIY 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLVSSNDCVK---LGDFGLSRYMEDSTYYKASKgKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd14156    112 HRDLNSKNCLIRVTPRGReavVTDFGLAREVGEMPANDPER-KLSLVgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  622 mhgvkpfqgvknndviGRI-ENGERLP--------------MPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14156    191 ----------------ARIpADPEVLPrtgdfgldvqafkeMVPGCPEPFLDLAASCCRMDAFKRPSFAELLDELEDIAE 254
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
433-677 4.79e-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: 87.82  E-value: 4.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiYMSPENpALAVAIKTCKN-CTSDSVREKFLQEALTMRQF-DHPHIVKLIGVITENP-VWIIMELCTL 509
Cdd:cd13997      8 IGSGSFSEVFK--VRSKVD-GCLYAVKKSKKpFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGhLYIQMELCEN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFL--QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd13997     85 GSLQDALeeLSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEGDS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 klpiKWMAPESIN-FRRFTSASDVWMFGVCMWEILMHGVKPfqgvKNNDVIGRIENGeRLPMPPNCPPT--LYSLMTKCW 664
Cdd:cd13997    165 ----RYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLP----RNGQQWQQLRQG-KLPLPPGLVLSqeLTRLLKVML 235
                          250
                   ....*....|...
gi 1914779978  665 AYDPSRRPRFTEL 677
Cdd:cd13997    236 DPDPTRRPTADQL 248
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
428-640 4.98e-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: 4.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDS-----VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVW 501
Cdd:cd14196      8 DIGEELGSGQFAIVKK---CREKSTGLEYAAKFIKKRQSRAsrrgvSREEIEREVSILRQVLHPNIITLHDVYeNRTDVV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC----VKLGDFGLSRYME 577
Cdd:cd14196     85 LILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  578 DSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 640
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); ...
433-671 5.74e-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: 5.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENP-ALAVAIKtcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLG 510
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTfALKCVKK--RHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKyLYMLMEYCLGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS--TY------- 581
Cdd:cd05572     79 ELWTILRDRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGrkTWtfcgtpe 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNND--VIGRIENG-ERLPMPPNCPPTLYS 658
Cdd:cd05572    158 Y-----------VAPEIILNKGYDFSVDYWSLGILLYE-LLTGRPPFGGDDEDPmkIYNIILKGiDKIEFPKYIDKNAKN 225
                          250
                   ....*....|...
gi 1914779978  659 LMTKCWAYDPSRR 671
Cdd:cd05572    226 LIKQLLRRNPEER 238
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
470-680 6.02e-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: 87.87  E-value: 6.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFLQVRKYSL-DLASLILYAYQLSTALAYLESKRF 547
Cdd:cd08220     43 RQAALNEVKVLSMLHHPNIIEYYeSFLEDKALMIVMEYAPGGTLFEYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQI 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSN-DCVKLGDFGLSRYMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvK 626
Cdd:cd08220    123 LHRDLKTQNILLNKKrTVVKIGDFGISKIL--SSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLK-R 199
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  627 PFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ 680
Cdd:cd08220    200 AFEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
427-647 6.65e-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: 87.74  E-value: 6.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIYmspENPALAVAIK-TCKNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14162      2 YIVGKTLGHGSYAVVKKAYS---TKHKCKVAIKiVSKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEAIeTTSRVYII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRKYSLDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymedsTYYK 583
Cdd:cd14162     79 MELAENGDLLDYIRKNGALPEPQARRWF-RQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR-----GVMK 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  584 ASKGKLPIK--------WMAPESINFRRFTS-ASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLP 647
Cdd:cd14162    153 TKDGKPKLSetycgsyaYASPEILRGIPYDPfLSDIWSMGVVLYT-MVYGRLPFDDSNLKVLLKQVQRRVVFP 224
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
430-677 7.95e-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: 87.49  E-value: 7.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIymspENPALAVAIKTCKNCTSDSVR-----EKFLQEALTMRQFDHPHIVKLIGV-ITENPVWII 503
Cdd:cd06631      6 GNVLGKGAYGTVYCGL----TSTGQLIAVKQVELDTSDKEKaekeyEKLQEEVDLLKTLKHVNIVGYLGTcLEDNVVSIF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-------YM 576
Cdd:cd06631     82 MEFVPGGSIASILA-RFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKrlcinlsSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLP--MPPNCPP 654
Cdd:cd06631    161 SQSQLLKSMRGT-PY-WMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRKPVprLPDKFSP 237
                          250       260
                   ....*....|....*....|...
gi 1914779978  655 TLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06631    238 EARDFVHACLTRDQDERPSAEQL 260
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
428-671 8.50e-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: 87.31  E-value: 8.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVItENP--VWIIME 505
Cdd:cd14081      4 RLGKTLGKGQTGLVKLAKH-CVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVY-ENKkyLYLVLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd14081     82 YVSGGELFDYL-VKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLETS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLpiKWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCW 664
Cdd:cd14081    161 CGSP--HYACPEVIKGEKYDgRKADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRG-VFHIPHFISPDAQDLLRRML 236

                   ....*..
gi 1914779978  665 AYDPSRR 671
Cdd:cd14081    237 EVNPEKR 243
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
425-649 1.19e-18

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: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREkflQEALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14184      1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIE---NEVSILRRVKHPNIIMLIEEMdTPAELYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMED 578
Cdd:cd14184     78 MELVKGGDLfDAITSSTKYTERDASAMVY--NLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEG 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  579 STYYKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKN--NDVIGRIENGE-RLPMP 649
Cdd:cd14184    156 PLYTVCGTP----TYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRSENNlqEDLFDQILLGKlEFPSP 224
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
423-677 1.32e-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: 86.73  E-value: 1.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  423 QRERIELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVW 501
Cdd:cd06648      5 PRSDLDNFVKIGEGSTGIVCIATDKSTGR---QVAVKK-MDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSsYLVGDELW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 580
Cdd:cd06648     81 VVMEFLEGGALTDIVtHTRMNEEQIATVCRAVLK---ALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGE--RLPMPPNCPPTLYS 658
Cdd:cd06648    158 PRRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIE-MVDGEPPYFNEPPLQAMKRIRDNEppKLKNLHKVSPRLRS 235
                          250
                   ....*....|....*....
gi 1914779978  659 LMTKCWAYDPSRRPRFTEL 677
Cdd:cd06648    236 FLDRMLVRDPAQRATAAEL 254
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
433-672 1.73e-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: 1.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDSVrekFLQEALTMRQFDHPHIVKLIGVITEnPVWIIMELCTLGEL 512
Cdd:cd14068      2 LGDGGFGSVYRAVYRGED-----VAVKIFNKHTSFRL---LRQELVVLSHLHHPSLVALLAAGTA-PRMLVMELAPKGSL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  513 RSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS--NDC---VKLGDFGLSRYMeDSTYYKASKG 587
Cdd:cd14068     73 DALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlyPNCaiiAKIADYGIAQYC-CRMGIKTSEG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KLPIKwmAPESINFR-RFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPP---NCP--PTLYSLMT 661
Cdd:cd14068    152 TPGFR--APEVARGNvIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPDPVkeyGCApwPGVEALIK 229
                          250
                   ....*....|.
gi 1914779978  662 KCWAYDPSRRP 672
Cdd:cd14068    230 DCLKENPQCRP 240
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
433-672 1.77e-18

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: 86.40  E-value: 1.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNC-TSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLG 510
Cdd:cd08218      8 IGEGSFG---KALLVKSKEDGKQYVIKEINISkMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENgNLYIVMDYCDGG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeDSTYYKASKGKL 589
Cdd:cd08218     85 DLYKRINAQRGVLFPEDQILdWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL-NSTVELARTCIG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PIKWMAPESINFRRFTSASDVWMFGVCMWEI--LMHgvkPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYD 667
Cdd:cd08218    164 TPYYLSPEICENKPYNNKSDIWALGCVLYEMctLKH---AFEAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRN 240

                   ....*
gi 1914779978  668 PSRRP 672
Cdd:cd08218    241 PRDRP 245
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
426-672 1.96e-18

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 87.58  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVIT------EN 498
Cdd:cd07834      1 RYELLKPIGSGAYGVVCSAYDKRTGRK---VAIKKISNVFDDLIDAKrILREIKILRHLKHENIIGLLDILRppspeeFN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELctlgelrsflqvrkYSLDLASLI------------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 566
Cdd:cd07834     78 DVYIVTEL--------------METDLHKVIkspqpltddhiqYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLK 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  567 LGDFGLSRYMEDS------TYYKASkgklpiKWM-APESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQG------- 630
Cdd:cd07834    144 ICDFGLARGVDPDedkgflTEYVVT------RWYrAPELLlSSKKYTKAIDIWSVGCIFAELLTR--KPlFPGrdyidql 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  631 --------VKNNDVIGRIENGE------RLP---------MPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd07834    216 nlivevlgTPSEEDLKFISSEKarnylkSLPkkpkkplseVFPGASPEAIDLLEKMLVFNPKKRI 280
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
429-672 2.03e-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: 2.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSPENPaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI--TENPVWIIMEL 506
Cdd:cd14164      4 LGTTIGEGSFSKVKLATSQKYCCK-VAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIevANGRLYIVMEA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGLSRYMED----STY 581
Cdd:cd14164     83 AATDLLQKIQEVHHIPKDLARDMFA--QMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDypelSTT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGklpikWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGvknnDVIGRIENGERlpmPPNCPPTLySLM 660
Cdd:cd14164    161 FCGSRA-----YTPPEVILGTPYDPKKyDVWSLGVVLY-VMVTGTMPFDE----TNVRRLRLQQR---GVLYPSGV-ALE 226
                          250
                   ....*....|....*....
gi 1914779978  661 TKCWA-------YDPSRRP 672
Cdd:cd14164    227 EPCRAlirtllqFNPSTRP 245
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
424-687 2.13e-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: 86.41  E-value: 2.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRC---IGEGQFGDVHQgiyMSPENPALAVAIKTCKnctsdsVREKFLQEALTMRQFDHPHIVKLIGVITENP- 499
Cdd:cd13991      2 REEVHWATHqlrIGRGSFGEVHR---MEDKQTGFQCAVKKVR------LEVFRAEELMACAGLTSPRVVPLYGAVREGPw 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVR-KYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSnDCVK--LGDFGLSRYM 576
Cdd:cd13991     73 VNIFMDLKEGGSLGQLIKEQgCLPEDRA--LHYLGQALEGLEYLHSRKILHGDVKADNVLLSS-DGSDafLCDFGHAECL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDS---------TYYKASKGKlpikwMAPESINFRRFTSASDVWMfGVCMWEILMHGVKPFQGVKNNDVIGRIENgERLP 647
Cdd:cd13991    150 DPDglgkslftgDYIPGTETH-----MAPEVVLGKPCDAKVDVWS-SCCMMLHMLNGCHPWTQYYSGPLCLKIAN-EPPP 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1914779978  648 M---PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEE 687
Cdd:cd13991    223 LreiPPSCAPLTAQAIQAGLRKEPVHRASAAELRRKTNRALQE 265
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
426-677 2.62e-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: 2.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFG------DVHQGIYmspenpalaVAIKTCKNCTSDSVREKFLQEALTMRQFD-------HPHIVKLI 492
Cdd:cd13993      1 RYQLISPIGEGAYGvvylavDLRTGRK---------YAIKCLYKSGPNSKDGNDFQKLPQLREIDlhrrvsrHPNIITLH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  493 GVI-TENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAY-QLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGD 569
Cdd:cd13993     72 DVFeTEVAIYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFlQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  570 FGLSryMEDSTYYKASKGKLpiKWMAPESI--NFRRF----TSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENG 643
Cdd:cd13993    152 FGLA--TTEKISMDFGVGSE--FYMAPECFdeVGRSLkgypCAAGDIWSLGIILLNLTF-GRNPWKIASESDPIFYDYYL 226
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  644 ER-------LPMPPNCpptlYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd13993    227 NSpnlfdviLPMSDDF----YNLLRQIFTVNPNNRILLPEL 263
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
433-681 2.78e-18

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: 86.01  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREkflQEALTmrQFDHPHIVKLIG-----------------VI 495
Cdd:cd14047     14 IGSGGFGQVFKAKHRIDGK---TYAIKRVKLNNEKAERE---VKALA--KLDHPNIVRYNGcwdgfdydpetsssnssRS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQVRKYS--LDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd14047     86 KTKCLFIQMEFCEKGTLESWIEKRNGEklDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDstYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVcMWEILMHGVKpfQGVKNNDVIGRIENGErlpMPPN-- 651
Cdd:cd14047    165 TSLKN--DGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGL-ILFELLHVCD--SAFEKSKFWTDLRNGI---LPDIfd 236
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  652 -CPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd14047    237 kRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
433-628 3.09e-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: 86.35  E-value: 3.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDV----HQGIymspenpALAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGV--------ITEN 498
Cdd:cd13989      1 LGSGGFGYVtlwkHQDT-------GEYVAIKKCRqeLSPSDKNRERWCLEVQIMKKLNHPNVVSARDVppeleklsPNDL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVwIIMELCTLGELRSFL-QVRKYS----LDLASLIlyaYQLSTALAYLESKRFVHRDIAARN-VLVSSNDCV--KLGDF 570
Cdd:cd13989     74 PL-LAMEYCSGGDLRKVLnQPENCCglkeSEVRTLL---SDISSAISYLHENRIIHRDLKPENiVLQQGGGRViyKLIDL 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  571 GLSRYMEDSTYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd13989    150 GYAKELDQGSLCTSFVGTL--QYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
431-677 3.25e-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: 85.58  E-value: 3.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHqgiYMSPENPALAVAIK----TCKNCT---SDSVRE-KFLqealtmRQFDHPHIVKLIGV-ITENPVW 501
Cdd:cd06607      7 REIGHGSFGAVY---YARNKRTSEVVAIKkmsySGKQSTekwQDIIKEvKFL------RQLRHPNTIEYKGCyLREHTAW 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCtLGELRSFLQVRKYSL---DLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd06607     78 LVMEYC-LGSASDIVEVHKKPLqevEIAAICHGALQ---GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 STYYKASkgklPIkWMAPESI---NFRRFTSASDVWMFGV-CmweilmhgvkpfqgvknndvigrIENGERLP------- 647
Cdd:cd06607    154 ANSFVGT----PY-WMAPEVIlamDEGQYDGKVDVWSLGItC-----------------------IELAERKPplfnmna 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  648 ------MPPNCPPTL---------YSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06607    206 msalyhIAQNDSPTLssgewsddfRNFVDSCLQKIPQDRPSAEDL 250
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
433-622 3.32e-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: 86.65  E-value: 3.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMspENPalaVAIKT----CKNCTsdsVREKFLQEALTMRqfdHPHIVKLIGV---ITENPVW---I 502
Cdd:cd14054      3 IGQGRYGTVWKGSLD--ERP---VAVKVfparHRQNF---QNEKDIYELPLME---HSNILRFIGAderPTADGRMeylL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKR---------FVHRDIAARNVLVSSN-DCVkLGDFGL 572
Cdd:cd14054     72 VLEYAPKGSLCSYL--RENTLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADgSCV-ICDFGL 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  573 SRYMEDSTYYK----ASKGKLP-----IKWMAPE----SINFRRFTSA---SDVWMFGVCMWEILM 622
Cdd:cd14054    149 AMVLRGSSLVRgrpgAAENASIsevgtLRYMAPEvlegAVNLRDCESAlkqVDVYALGLVLWEIAM 214
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
444-684 3.41e-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: 85.68  E-value: 3.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  444 GIYmspENPALAVAIKTCKNCT-SDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQVRKY 521
Cdd:cd14045     26 GIY---DGRTVAIKKIAKKSFTlSKRIR----KEVKQVRELDHPNLCKFIGGCIEVPnVAIITEYCPKGSLNDVLLNEDI 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  522 SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS--KGKLPIKWMAPE-- 597
Cdd:cd14045     99 PLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASgyQQRLMQVYLPPEnh 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  598 SINFRRFTSASDVWMFGVCMWEIlmhgvkpfqgVKNNDVIGR----IENGERLPMPP--------NCP-PTLY-SLMTKC 663
Cdd:cd14045    179 SNTDTEPTQATDVYSYAIILLEI----------ATRNDPVPEddysLDEAWCPPLPElisgktenSCPcPADYvELIRRC 248
                          250       260
                   ....*....|....*....|.
gi 1914779978  664 WAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14045    249 RKNNPAQRPTFEQIKKTLHKI 269
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
428-677 3.43e-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: 3.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRcigeGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDSVREKFLQEA-LTMRQFDHPHIVKLIGVI-TENPVWIIME 505
Cdd:cd06617      8 ELGR----GAYGVVDK---MRHVPTGTIMAVKRIRATVNSQEQKRLLMDLdISMRSVDCPYTVTFYGALfREGDVWICME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDLASLILYAYQLS--TALAYLESK-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 582
Cdd:cd06617     81 VMDTSLDKFYKKVYDKGLTIPEDILGKIAVSivKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVAK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLPikWMAPESIN----FRRFTSASDVWMFGVCMWEILMHGV------KPFQGVKNndVIGriENGERLPMPPnC 652
Cdd:cd06617    161 TIDAGCKP--YMAPERINpelnQKGYDVKSDVWSLGITMIELATGRFpydswkTPFQQLKQ--VVE--EPSPQLPAEK-F 233
                          250       260
                   ....*....|....*....|....*
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06617    234 SPEFQDFVNKCLKKNYKERPNYPEL 258
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
433-636 4.57e-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: 84.97  E-value: 4.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVAIKtcknCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd14103      1 LGRGKFGTVYRCVEKATGKELAAKFIK----CRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFeTPREMVLVMEYVAGGE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LrsFLQV--RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd14103     77 L--FERVvdDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGnqIKIIDFGLARKYDPDKKLKVLFG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  588 KlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGvkNNDV 636
Cdd:cd14103    155 T-P-EFVAPEVVNYEPISYATDMWSVGVICY-VLLSGLSPFMG--DNDA 198
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
433-676 7.52e-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: 7.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMspENPALAVAIK--TCKNCT-SDSVREKflqEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCT 508
Cdd:cd14120      1 IGHGAFAVVFKGRHR--KKPDLPVAIKciTKKNLSkSQNLLGK---EIKILKELSHENVVALLDCqETSSSVYLVMEYCN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-SNDC--------VKLGDFGLSRYMEDS 579
Cdd:cd14120     76 GGDLADYLQA-KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShNSGRkpspndirLKIADFGFARFLQDG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE-NGERLP-MPPNCPPTLY 657
Cdd:cd14120    155 MMAATLCGS-PM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEkNANLRPnIPSGTSPALK 231
                          250
                   ....*....|....*....
gi 1914779978  658 SLMTKCWAYDPSRRPRFTE 676
Cdd:cd14120    232 DLLLGLLKRNPKDRIDFED 250
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
471-680 9.00e-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: 85.02  E-value: 9.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  471 EKFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKYSLDLASLilYAYQLSTALAYLESKRF 547
Cdd:cd14199     70 ERVYQEIAILKKLDHPNVVKLVEVLddpSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARF--YFQDLIKGIEYLHYQKI 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESINFRR--FT-SASDVWMFGVCMWeILMHG 624
Cdd:cd14199    148 IHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTP-AFMAPETLSETRkiFSgKALDVWAMGVTLY-CFVFG 225
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  625 VKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ 680
Cdd:cd14199    226 QCPFMDERILSLHSKIKTQPlEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLH 282
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
430-629 1.01e-17

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: 84.21  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 508
Cdd:cd14189      6 GRLLGKGGFARCYEMTDLA-TNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDaENIYIFLELCS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd14189     85 RKSLAHIWKARHTLLE-PEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICG 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  589 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQ 629
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 ...
428-671 1.11e-17

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: 84.53  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVhqgiYMSPENP-----ALAVAIKTckNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VW 501
Cdd:cd14117      9 DIGRPLGKGKFGNV----YLAREKQskfivALKVLFKS--QIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKrIY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdSTY 581
Cdd:cd14117     83 LILEYAPRGELYKELQ-KHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAP-SLR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMT 661
Cdd:cd14117    161 RRTMCGTL--DYLPPEMIEGRTHDEKVDLWCIGVLCYELLV-GMPPFESASHTETYRRIVKVD-LKFPPFLSDGSRDLIS 236
                          250
                   ....*....|
gi 1914779978  662 KCWAYDPSRR 671
Cdd:cd14117    237 KLLRYHPSER 246
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
428-677 1.54e-17

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: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQgIYMSPENPALAVAIKTCKNCTSDSVREKF-LQEALTmrqfDHPHIVKLIG------VITENPV 500
Cdd:cd06638     21 EIIETIGKGTYGKVFK-VLNKKNGSKAAVKILDPIHDIDEEIEAEYnILKALS----DHPNVVKFYGmyykkdVKNGDQL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTAL---AYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd06638     96 WLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALmglQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNC 652
Cdd:cd06638    176 STRLRRNTSVGTPF-WMAPEVIACEQqldstYDARCDVWSLGITAIE-LGDGDPPLADLHPMRALFKI--------PRNP 245
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1914779978  653 PPTLYS----------LMTKCWAYDPSRRPRFTEL 677
Cdd:cd06638    246 PPTLHQpelwsnefndFIRKCLTKDYEKRPTVSDL 280
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
451-721 2.01e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 86.61  E-value: 2.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  451 NPALAVAIKTCKNCTSDSVREKFL------------QEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ 517
Cdd:PTZ00267    78 NPTTAAFVATRGSDPKEKVVAKFVmlnderqaayarSELHCLAACDHFGIVKHFDDFkSDDKLLLIMEYGSGGDLNKQIK 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  518 VR-KYSLDLAS--LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKW 593
Cdd:PTZ00267   158 QRlKEHLPFQEyeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDvASSFCGTPYY 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  594 MAPESINFRRFTSASDVWMFGVCMWEIL-MHgvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:PTZ00267   238 LAPELWERKRYSKKADMWSLGVILYELLtLH--RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRP 315
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  673 R-----FTELKAQLSTILEE-----EKAQQEERMRMESRRQatvswdsgGSDEAPPKPS 721
Cdd:PTZ00267   316 TtqqllHTEFLKYVANLFQDivrhsETISPHDREEILRQLQ--------ESGERAPPPS 366
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
420-630 2.04e-17

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: 84.15  E-value: 2.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRErielgrcIGEGQFGDVHQGIYMSPENPalaVAIKTCKNctsDSVREKF----LQEALTMRQFDHPHIVKLIGVI 495
Cdd:cd07840      1 YEKIAQ-------IGEGTYGQVYKARNKKTGEL---VALKKIRM---ENEKEGFpitaIREIKLLQKLDHPNVVRLKEIV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENP-------VWIIMELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLG 568
Cdd:cd07840     68 TSKGsakykgsIYMVFEYMD-HDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLA 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  569 DFGLSRYMEdstyyKASKGKLPIK----WMAPESINF--RRFTSASDVWMFGVCMWEILmHGVKPFQG 630
Cdd:cd07840    147 DFGLARPYT-----KENNADYTNRvitlWYRPPELLLgaTRYGPEVDMWSVGCILAELF-TGKPIFQG 208
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
433-630 2.31e-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: 83.05  E-value: 2.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd14190     12 LGGGKFGKVHT---CTEKRTGLKLAAKVINKQNSKD-KEMVLLEIQVMNQLNHRNLIQLYEAIeTPNEIVLFMEYVEGGE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSNDCVKLGDFGLSRYMEDSTYYKASKGKl 589
Cdd:cd14190     88 LFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPREKLKVNFGT- 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  590 PiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQG 630
Cdd:cd14190    167 P-EFLSPEVVNYDQVSFPTDMWSMGVITY-MLLSGLSPFLG 205
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
429-678 2.60e-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: 83.30  E-value: 2.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSPENPALA--VAIKTCKNCT-SDSVRE-KFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14076      5 LGRTLGEGEFGKVKLGWPLPKANHRSGvqVAIKLIRRDTqQENCQTsKIMREINILKGLTHPNIVRLLDVLkTKKYIGIV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST--Y 581
Cdd:cd14076     85 LEFVSGGELFDYILARRRLKDSVACRLFA-QLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNgdL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKlPIkWMAPESINFRRFTSAS--DVWMFGVCMWEILMhGVKPFQGVKNN---DVIGR----IENGErLPMPPNC 652
Cdd:cd14076    164 MSTSCGS-PC-YAAPELVVSDSMYAGRkaDIWSCGVILYAMLA-GYLPFDDDPHNpngDNVPRlyryICNTP-LIFPEYV 239
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  653 PPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14076    240 TPKARDLLRRILVPNPRKRIRLSAIM 265
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
430-677 4.32e-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: 82.37  E-value: 4.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCT 508
Cdd:cd14188      6 GKVLGKGGFAKCYEMTDLT-TNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKEnIYILLEYCS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd14188     85 RRSMAHILKARKVLTE-PEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd14188    164 TP-NYLSPEVLNKQGHGCESDIWALGCVMYTMLL-GRPPFETTNLKETYRCIREA-RYSLPSSLLAPAKHLIASMLSKNP 240

                   ....*....
gi 1914779978  669 SRRPRFTEL 677
Cdd:cd14188    241 EDRPSLDEI 249
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
433-640 4.55e-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: 4.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGE 511
Cdd:cd14191     10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIR----QEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEMVSGGE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSNDCVKLGDFGLSRYMEDSTYYKASKGKl 589
Cdd:cd14191     86 LFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAGSLKVLFGT- 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  590 PiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 640
Cdd:cd14191    165 P-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 213
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
430-678 4.85e-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: 4.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGIYMspeNPALAVAIKTCKNCTSDSVREKFLQ---------EALTMRQFDHPHIVKLIGV-ITENP 499
Cdd:cd06629      6 GELIGKGTYGRVYLAMNA---TTGEMLAVKQVELPKTSSDRADSRQktvvdalksEIDTLKDLDHPNIVQYLGFeETEDY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQ-VRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd06629     83 FSIFLEYVPGGSIGSCLRkYGKFEEDLVRFFTR--QILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 StyYKASKG---KLPIKWMAPESI-NFRRFTSAS-DVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERL-PMPP-- 650
Cdd:cd06629    161 I--YGNNGAtsmQGSVFWMAPEVIhSQGQGYSAKvDIWSLGCVVLEMLA-GRRPWSDDEAIAAMFKLGNKRSApPVPEdv 237
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  651 NCPPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd06629    238 NLSPEALDFLNACFAIDPRDRPTAAELL 265
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
408-677 5.14e-17

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 84.10  E-value: 5.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  408 PSKSYGIDEARDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPH 487
Cdd:PLN00034    57 SSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRL---YALKVIYGNHEDTVRRQICREIEILRDVNHPN 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  488 IVKLIGVITEN-PVWIIMELCTLGELRSflqvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 566
Cdd:PLN00034   134 VVKCHDMFDHNgEIQVLLEFMDGGSLEG-----THIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVK 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  567 LGDFGLSRYMeDSTYYKASKGKLPIKWMAPESINF-----RRFTSASDVWMFGVCMWEILMhGVKPFQGVKNND---VIG 638
Cdd:PLN00034   209 IADFGVSRIL-AQTMDPCNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYL-GRFPFGVGRQGDwasLMC 286
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  639 RIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:PLN00034   287 AICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQL 325
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
433-620 5.15e-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: 5.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCtLGE 511
Cdd:cd06633     29 IGHGSFGAVYFATN-SHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCyLKDHTAWLVMEYC-LGS 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKgklpi 591
Cdd:cd06633    107 ASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTP----- 181
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1914779978  592 KWMAPESI---NFRRFTSASDVWMFGVCMWEI 620
Cdd:cd06633    182 YWMAPEVIlamDEGQYDGKVDIWSLGITCIEL 213
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
433-706 5.67e-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: 82.86  E-value: 5.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd14086      9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARD--HQKLEREARICRLLKHPNIVRLHDSIsEEGFHYLVFDLVTGGE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRK-YSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd14086     87 LFEDIVAREfYSEADASHCI--QQILESVNHCHQNGIVHRDLKPENLLLASkskGAAVKLADFGLAIEVQGDQQAWFGFA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGeRLPMPPN----CPPTLYSLMTKC 663
Cdd:cd14086    165 GTP-GYLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDEDQHRLYAQIKAG-AYDYPSPewdtVTPEAKDLINQM 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1914779978  664 WAYDPSRRPRFTELkaqlstiLEEEKAQQEERMRMESRRQATV 706
Cdd:cd14086    242 LTVNPAKRITAAEA-------LKHPWICQRDRVASMVHRQETV 277
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
431-685 6.08e-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: 82.66  E-value: 6.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCT--SDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELC 507
Cdd:cd14026      3 RYLSRGAFGTVSRARHADWRVT---VAIKCLKLDSpvGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLgIVTEYM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRKYSLDLASLILYA--YQLSTALAYLE--SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 583
Cdd:cd14026     80 TNGSLNELLHEKDIYPDVAWPLRLRilYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSISQS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLP----IKWMAPESINFRRFTSAS---DVWMFGVCMWEILMHGVkPFQGVKNN-DVIGRIENGER-------LPM 648
Cdd:cd14026    160 RSSKSAPeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKI-PFEEVTNPlQIMYSVSQGHRpdtgedsLPV 238
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1914779978  649 PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd14026    239 DIPHRATLINLIESGWAQNPDERPSFLKCLIELEPVL 275
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
433-631 6.33e-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: 82.08  E-value: 6.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiYMSPENPALAVAIKTCKNCTSD-SVREKFLQEALTMRQFD---HPHIVKLIGVITENP-VWIIMELC 507
Cdd:cd14052      8 IGSGEFSQVYK--VSERVPTGKVYAVKKLKPNYAGaKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGhLYIQTELC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFL--QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG------LSRYME-- 577
Cdd:cd14052     86 ENGSLDVFLseLGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGmatvwpLIRGIEre 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  578 -DSTYykaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGV 631
Cdd:cd14052    166 gDREY------------IAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNGD 208
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
433-672 7.16e-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: 7.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDV-HQGIYMSPENPALAVAIKTCKNCTS-------------DSVRE--KFLQEALTMRQFDHPHIVKLIGvIT 496
Cdd:cd14067      1 LGQGGSGTViYRARYQGQPVAVKRFHIKKCKKRTDgsadtmlkhlraaDAMKNfsEFRQEASMLHSLQHPCIVYLIG-IS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGELRSFLQVRKYS---LDLASLILY--AYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-----VK 566
Cdd:cd14067     80 IHPLCFALELAPLGSLNTVLEENHKGssfMPLGHMLTFkiAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVqehinIK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  567 LGDFGLSR--YMEDSTYYKASKGklpikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGE 644
Cdd:cd14067    160 LSDYGISRqsFHEGALGVEGTPG-----YQAPEIRPRIVYDEKVDMFSYGMVLYE-LLSGQRPSLGHHQLQIAKKLSKGI 233
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1914779978  645 R--LPMPPNCP-PTLYSLMTKCWAYDPSRRP 672
Cdd:cd14067    234 RpvLGQPEEVQfFRLQALMMECWDTKPEKRP 264
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
456-676 7.83e-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: 82.99  E-value: 7.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKTC----KNCTsDS---VRE-KFLQEaLTmrqfDHPHIVKLIGVI-TEN--PVWIIMElctlgelrsFLQVrkyslD 524
Cdd:cd07852     35 VALKKIfdafRNAT-DAqrtFREiMFLQE-LN----DHPNIIKLLNVIrAENdkDIYLVFE---------YMET-----D 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  525 LASLI----------LY-AYQLSTALAYLESKRFVHRDIAARNVLVSSnDC-VKLGDFGLSRY---MEDS------TYYK 583
Cdd:cd07852     95 LHAVIraniledihkQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNS-DCrVKLADFGLARSlsqLEEDdenpvlTDYV 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASkgklpiKWM-APE----SinfRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGRIENG-------------- 643
Cdd:cd07852    174 AT------RWYrAPEillgS---TRYTKGVDMWSVGCILGEMLLG--KPlFPGTSTLNQLEKIIEVigrpsaediesiqs 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  644 -------ERLP---------MPPNCPPTLYSLMTKCWAYDPSRRPRFTE 676
Cdd:cd07852    243 pfaatmlESLPpsrpksldeLFPKASPDALDLLKKLLVFNPNKRLTAEE 291
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
433-677 7.99e-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: 7.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiyMSPENPALAVAIKTCkNCTSDsVREKFLQEALTMRQF-DHPHIVKLIGVITE------NPVWIIME 505
Cdd:cd06639     30 IGKGTYGKVYK---VTNKKDGSLAAVKIL-DPISD-VDEEIEAEYNILRSLpNHPNVVKFYGMFYKadqyvgGQLWLVLE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLG---ELRSFLQVRKYSLD--LASLILYAYQLstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 580
Cdd:cd06639    105 LCNGGsvtELVKGLLKCGQRLDeaMISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSAR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEIL--------MHGVKPFqgvknndvigriengerLP 647
Cdd:cd06639    183 LRRNTSVGTPF-WMAPEVIACEQqydysYDARCDVWSLGITAIELAdgdpplfdMHPVKAL-----------------FK 244
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1914779978  648 MPPNCPPTLYS----------LMTKCWAYDPSRRPRFTEL 677
Cdd:cd06639    245 IPRNPPPTLLNpekwcrgfshFISQCLIKDFEKRPSVTHL 284
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
143-248 8.88e-17

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). 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, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 76.52  E-value: 8.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  143 TLNFFYQQVKSDYMLEIAdQVDQEIALKLGCLEIRRSYwemrGNalekKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRK 222
Cdd:cd14473      1 TRYLLYLQVKRDILEGRL-PCSEETAALLAALALQAEY----GD----YDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEK 71
                           90       100
                   ....*....|....*....|....*.
gi 1914779978  223 LIQQTFRQFANLNREESILKFFEILS 248
Cdd:cd14473     72 RIVELHKKLRGLSPAEAKLKYLKIAR 97
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
433-677 9.25e-17

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: 81.51  E-value: 9.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCkNCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTLGE 511
Cdd:cd06647     15 IGQGASGTVYTAIDVATGQ---EVAIKQM-NLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06647     91 LTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-ENGE-RLPMPPNCPPTLYSLMTKCWAYDPS 669
Cdd:cd06647    169 -WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIaTNGTpELQNPEKLSAIFRDFLNRCLEMDVE 246

                   ....*...
gi 1914779978  670 RRPRFTEL 677
Cdd:cd06647    247 KRGSAKEL 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
425-676 1.02e-16

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: 82.20  E-value: 1.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVW 501
Cdd:cd14094      3 DVYELCEVIGKGPFSVVRRCIH-RETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYsSDGMLY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELrSFLQVRK------YSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC---VKLGDFGL 572
Cdd:cd14094     82 MVFEFMDGADL-CFEIVKRadagfvYSEAVASH--YMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKnNDVIGRIENGeRLPMPPNC 652
Cdd:cd14094    159 AIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK-ERLFEGIIKG-KYKMNPRQ 234
                          250       260
                   ....*....|....*....|....*...
gi 1914779978  653 PPTLYS----LMTKCWAYDPSRRPRFTE 676
Cdd:cd14094    235 WSHISEsakdLVRRMLMLDPAERITVYE 262
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
433-671 1.07e-16

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: 1.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVH------QGIYMspenpalavAIKTCKNCTSDS---VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 502
Cdd:cd05611      4 ISKGAFGSVYlakkrsTGDYF---------AIKVLKKSDMIAknqVTNVKAERAIMMIQGESPYVAKLYYSFqSKDYLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 582
Cdd:cd05611     75 VMEYLNGGDCASLIKTLGG-LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPN----CPPTLYS 658
Cdd:cd05611    154 KKFVGT-P-DYLAPETILGVGDDKMSDWWSLGCVIFEFLF-GYPPFHAETPDAVFDNILSR-RINWPEEvkefCSPEAVD 229
                          250
                   ....*....|...
gi 1914779978  659 LMTKCWAYDPSRR 671
Cdd:cd05611    230 LINRLLCMDPAKR 242
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
426-684 1.12e-16

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: 81.21  E-value: 1.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 504
Cdd:cd14153      1 QLEIGELIGKGRFGQVYHGRW----HGEVAIRLIDIERDNEEQLK-AFKREVMAYRQTRHENVVLFMGACMSPPhLAIIT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSNDCVKLGDFGL---SRYMEDSTy 581
Cdd:cd14153     76 SLCKGRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLftiSGVLQAGR- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 yKASKGKLPIKW---MAPESI---------NFRRFTSASDVWMFGVCMWEilMHGVK-PFQGVKNNDVIGRIENGerlpM 648
Cdd:cd14153    154 -REDKLRIQSGWlchLAPEIIrqlspeteeDKLPFSKHSDVFAFGTIWYE--LHAREwPFKTQPAEAIIWQVGSG----M 226
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  649 PPNCP-----PTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14153    227 KPNLSqigmgKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
480-681 1.35e-16

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: 81.49  E-value: 1.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  480 MRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQVRKYSLD---LASLIlyaYQLSTALAYLESKrfvhrDIAAR 555
Cdd:cd14042     56 MRDLQHDNLTRFIGACVDPPnICILTEYCPKGSLQDILENEDIKLDwmfRYSLI---HDIVKGMHYLHDS-----EIKSH 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  556 NVLVSSNdCV-------KLGDFGLSRYMEDSTY----YKASKGKLpikWMAPE--SINFR--RFTSASDVWMFGVCMWEI 620
Cdd:cd14042    128 GNLKSSN-CVvdsrfvlKITDFGLHSFRSGQEPpddsHAYYAKLL---WTAPEllRDPNPppPGTQKGDVYSFGIILQEI 203
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  621 lMHGVKPFqGVKNND------VIGRIENGERLPMPPN-----CPPTLYSLMTKCWAYDPSRRPRFTELKAQL 681
Cdd:cd14042    204 -ATRQGPF-YEEGPDlspkeiIKKKVRNGEKPPFRPSldeleCPDEVLSLMQRCWAEDPEERPDFSTLRNKL 273
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
433-642 1.86e-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: 1.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPALAVAIKTckncTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd14192     12 LGGGRFGQVHKCTELSTGLTLAAKIIKV----KGAKEREEVKNEINIMNQLNHVNLIQLYDAFeSKTNLTLIMEYVDGGE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSNDCVKLGDFGLSRYMEDSTYYKASKGKl 589
Cdd:cd14192     88 LFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLARRYKPREKLKVNFGT- 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  590 PiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIEN 642
Cdd:cd14192    167 P-EFLAPEVVNYDFVSFPTDMWSVGVITY-MLLSGLSPFLGETDAETMNNIVN 217
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
436-676 1.99e-16

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: 81.22  E-value: 1.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  436 GQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREkflQEALTMRQFDHPHIVKLIGV--ITENPV---WIIMELCTL 509
Cdd:cd14053      6 GRFGAVWKAQYLNRL-----VAVKIFPLQEKQSwLTE---REIYSLPGMKHENILQFIGAekHGESLEaeyWLITEFHER 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRkySLDLASLILYAYQLSTALAYLESKR----------FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd14053     78 GSLCDYLKGN--VISWNELCKIAESMARGLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACIADFGLALKFEPG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIK-WMAPE----SINFRR--FTsASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERlpmppnc 652
Cdd:cd14053    156 KSCGDTHGQVGTRrYMAPEvlegAINFTRdaFL-RIDMYAMGLVLWELLSRCSVHDGPVDEYQLPFEEEVGQH------- 227
                          250       260
                   ....*....|....*....|....
gi 1914779978  653 pPTLySLMTKCWAyDPSRRPRFTE 676
Cdd:cd14053    228 -PTL-EDMQECVV-HKKLRPQIRD 248
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
433-677 2.01e-16

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: 80.83  E-value: 2.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEAL----TMRQFDHPHIVKLIGV--ITENPVWIIMEL 506
Cdd:cd13990      8 LGKGGFSEVYKAFDLV-EQRYVACKIHQLNKDWSEEKKQNYIKHALreyeIHKSLDHPRIVKLYDVfeIDTDSFCTVLEY 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFL-QVRKYSLDLASLILYayQLSTALAYLESKR--FVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDST 580
Cdd:cd13990     87 CDGNDLDFYLkQHKSIPEREARSIIM--QVVSALKYLNEIKppIIHYDLKPGNILLHSGNvsgEIKITDFGLSKIMDDES 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYK-----ASKGKLPIKWMAPESI----NFRRFTSASDVWMFGVCMWEILmHGVKPF------QGVKNNDVIGRIENGEr 645
Cdd:cd13990    165 YNSdgmelTSQGAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQML-YGRKPFghnqsqEAILEENTILKATEVE- 242
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  646 LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd13990    243 FPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQL 274
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
428-640 2.15e-16

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: 80.43  E-value: 2.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 504
Cdd:cd14195      8 EMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRgvSREEIEREVNILREIQHPNIITLHDIFeNKTDVVLIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMEDST 580
Cdd:cd14195     88 ELVSGGELFDFL-AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKIEAGN 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 640
Cdd:cd14195    167 EFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGETKQETLTNI 223
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
429-677 2.19e-16

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: 80.21  E-value: 2.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVhQGIYMSPENPALAVAIKTCKNCTSDSVrEKFL-QEALTMRQFDHPHIVKL--IGVITENPVWIIME 505
Cdd:cd14165      5 LGINLGEGSYAKV-KSAYSERLKCNVAIKIIDKKKAPDDFV-EKFLpRELEILARLNHKSIIKTyeIFETSDGKVYIVME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdstyyKAS 585
Cdd:cd14165     83 LGVQGDLLEFIKLRG-ALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCL-----RDE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIK--------WMAPESINFRRFT-SASDVWMFGVCMWeILMHGVKPFQGvKNNDVIGRIENGERLPMPPNCPPT- 655
Cdd:cd14165    157 NGRIVLSktfcgsaaYAAPEVLQGIPYDpRIYDIWSLGVILY-IMVCGSMPYDD-SNVKKMLKIQKEHRVRFPRSKNLTs 234
                          250       260
                   ....*....|....*....|...
gi 1914779978  656 -LYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14165    235 eCKDLIYRLLQPDVSQRLCIDEV 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
431-677 2.28e-16

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: 80.17  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVhqGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTL 509
Cdd:cd08221      6 RVLGRGAFGEA--VLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNhFLDGESLFIEMEYCNG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeDSTYYKASKGK 588
Cdd:cd08221     84 GNLHDKIAQQKNQLfPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVL-DSESSMAESIV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd08221    163 GTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLK-RTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDP 241

                   ....*....
gi 1914779978  669 SRRPRFTEL 677
Cdd:cd08221    242 EDRPTAEEL 250
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
428-671 2.75e-16

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: 80.18  E-value: 2.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQG----------IYMSPENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVI- 495
Cdd:cd14077      4 EFVKTIGAGSMGKVKLAkhirtgekcaIKIIPRASNAGLKKEREKRLEKEISRDIrTIREAALSSLLNHPHICRLRDFLr 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 575
Cdd:cd14077     84 TPNHYYMLFEYVDGGQLLDYI-ISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEDSTYYKASKGKLpiKWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGeRLPMPPNCPP 654
Cdd:cd14077    163 YDPRRLLRTFCGSL--YFAAPELLQAQPYTGPEvDVWSFGVVLY-VLVCGKVPFDDENMPALHAKIKKG-KVEYPSYLSS 238
                          250
                   ....*....|....*..
gi 1914779978  655 TLYSLMTKCWAYDPSRR 671
Cdd:cd14077    239 ECKSLISRMLVVDPKKR 255
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
425-640 3.05e-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: 3.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVW 501
Cdd:cd14194      5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvSREDIEREVSILKEIQHPNVITLHEVYeNKTDVI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC----VKLGDFGLSRYME 577
Cdd:cd14194     85 LILELVAGGELFDFL-AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKID 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  578 DSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 640
Cdd:cd14194    164 FGNEFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANV 223
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
433-628 4.38e-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: 80.01  E-value: 4.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVhqgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVK-------LIGVITENPVWIIME 505
Cdd:cd14038      2 LGTGGFGNV---LRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPLLAME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDL--ASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDST 580
Cdd:cd14038     79 YCQGGDLRKYLNQFENCCGLreGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKELDQGS 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1914779978  581 YYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd14038    159 LCTSFVGTL--QYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
427-628 4.49e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 80.63  E-value: 4.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVH------QGIYMspenpalavAIKTCKNctSDSVREK----FLQEALTMRQFDHPHIVKLI-GVI 495
Cdd:PTZ00263    20 FEMGETLGTGSFGRVRiakhkgTGEYY---------AIKCLKK--REILKMKqvqhVAQEKSILMELSHPFIVNMMcSFQ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:PTZ00263    89 DENRVYFLLEFVVGGELFTHLRkAGRFPNDVAKF--YHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  575 YMEDSTYYKASKgklPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:PTZ00263   167 KVPDRTFTLCGT---P-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPF 215
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
424-684 6.32e-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: 79.47  E-value: 6.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVHQGiYMSPENPALAVAIKTCKNCTSDsVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-I 502
Cdd:cd14158     14 RPISVGGNKLGEGGFGVVFKG-YINDKNVAVKKLAAMVDISTED-LTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLcL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLQVRKYSLDLA--SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DS 579
Cdd:cd14158     92 VYTYMPNGSLLDRLACLNDTPPLSwhMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEkFS 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIKWMAPESINfRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN----DVIGRIENGERL--------- 646
Cdd:cd14158    172 QTIMTERIVGTTAYMAPEALR-GEITPKSDIFSFGVVLLEIIT-GLPPVDENRDPqlllDIKEEIEDEEKTiedyvdkkm 249
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1914779978  647 -PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14158    250 gDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
428-679 6.84e-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: 6.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGvITENP--VWIIME 505
Cdd:cd14098      3 QIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQREINILKSLEHPGIVRLID-WYEDDqhIYLVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND--CVKLGDFGLSRYMEDSTYYK 583
Cdd:cd14098     82 YVEGGDLMDFI-MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTGTFLV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLpiKWMAPESINFRR------FTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIENGeRLPMPP----NCP 653
Cdd:cd14098    161 TFCGTM--AYLAPEILMSKEqnlqggYSNLVDMWSVG-CLVYVMLTGALPFDGSSQLPVEKRIRKG-RYTQPPlvdfNIS 236
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  654 PTLYSLMTKCWAYDPSRRPrfTELKA 679
Cdd:cd14098    237 EEAIDFILRLLDVDPEKRM--TAAQA 260
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
425-628 8.28e-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: 8.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIY-MSPENpalaVAIKTC--KNCTSDSVREKFLQEAltMRQFDHPHIVKLIGVI-TENPV 500
Cdd:cd14078      3 KYYELHETIGSGGFAKVKLATHiLTGEK----VAIKIMdkKALGDDLPRVKTEIEA--LKNLSHQHICRLYHVIeTDNKI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 580
Cdd:cd14078     77 FMVLEYCPGGELFDYI-VAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGM 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  581 YYKASKGKLPIKWMAPESINFRRFT-SASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14078    156 DHHLETCCGSPAYAAPELIQGKPYIgSEADVWSMGVLLY-ALLCGFLPF 203
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
420-640 8.34e-16

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 78.80  E-value: 8.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIelgrcIGEGQFGDVHQGIYMSPenpALAVAIKTCKnCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TEN 498
Cdd:cd14193      4 YNVNKEEI-----LGGGRFGQVHKCEEKSS---GLKLAAKIIK-ARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFeSRN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYM 576
Cdd:cd14193     75 DIVLVMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGLARRY 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  577 EDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 640
Cdd:cd14193    155 KPREKLRVNFGT-P-EFLAPEVVNYEFVSFPTDMWSLGVIAY-MLLSGLSPFLGEDDNETLNNI 215
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
424-620 8.56e-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: 78.93  E-value: 8.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekflQEALTMRQFDHPHIVKLIG-VITENPVWI 502
Cdd:cd06645     10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQ----QEIIMMKDCKHSNIVAYFGsYLRRDKLWI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 582
Cdd:cd06645     86 CMEFCGGGSLQDIYHVTG-PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAK 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  583 KASKGKLPIkWMAPESINFRR---FTSASDVWMFGVCMWEI 620
Cdd:cd06645    165 RKSFIGTPY-WMAPEVAAVERkggYNQLCDIWAVGITAIEL 204
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
409-686 1.09e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 81.07  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  409 SKSYGIDEARDYEiQRERIELGRCIGEGQFGDVHQGIYMSPENPaLAVAIKTCKNCT-SDSVREKflQEALTMRQFDHPH 487
Cdd:PTZ00283    17 PDTFAKDEATAKE-QAKKYWISRVLGSGATGTVLCAKRVSDGEP-FAVKVVDMEGMSeADKNRAQ--AEVCCLLNCDFFS 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  488 IVK----LIGVITENPVWIIMELCTL-----GELRSFLQ-----VRKYSLDLASLILYayQLSTALAYLESKRFVHRDIA 553
Cdd:PTZ00283    93 IVKchedFAKKDPRNPENVLMIALVLdyanaGDLRQEIKsraktNRTFREHEAGLLFI--QVLLAVHHVHSKHMIHRDIK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  554 ARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG--KLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGV 631
Cdd:PTZ00283   171 SANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTfcGTPY-YVAPEIWRRKPYSKKADMFSLGVLLYELLTLK-RPFDGE 248
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  632 KNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL------KAQLSTILE 686
Cdd:PTZ00283   249 NMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLlnmpicKLFISGLLE 309
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
426-671 1.26e-15

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: 79.37  E-value: 1.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQF-DHPHIVKLIG--VITE---N 498
Cdd:cd07857      1 RYELIKELGQGAYGIVCSARNAE-TSEEETVAIKKITNVFSKKILAKrALRELKLLRHFrGHKNITCLYDmdIVFPgnfN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMEL--CTLGE-LRSFLQvrkysLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR- 574
Cdd:cd07857     80 ELYLYEELmeADLHQiIRSGQP-----LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARg 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDS-------TYYKASkgklpiKWM-APE-SINFRRFTSASDVWMFGVCMWEILmhGVKPF----------------Q 629
Cdd:cd07857    155 FSENPgenagfmTEYVAT------RWYrAPEiMLSFQSYTKAIDVWSVGCILAELL--GRKPVfkgkdyvdqlnqilqvL 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  630 GVKNNDVIGRI------ENGERLPMPPNCP-PTLY--------SLMTKCWAYDPSRR 671
Cdd:cd07857    227 GTPDEETLSRIgspkaqNYIRSLPNIPKKPfESIFpnanplalDLLEKLLAFDPTKR 283
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
474-671 1.33e-15

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: 79.20  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  474 LQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQVRK---YSLDLASLilYAYQLSTALAYLESKRFVH 549
Cdd:cd05574     49 LTEREILATLDHPFLPTLYASFqTSTHLCFVMDYCPGGELFRLLQKQPgkrLPEEVARF--YAAEVLLALEYLHLLGFVY 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  550 RDIAARNVLVSSNDCVKLGDFGLS------------RYMEDSTYYKASKGKLPIK----------------WMAPESINF 601
Cdd:cd05574    127 RDLKPENILLHESGHIMLTDFDLSkqssvtpppvrkSLRKGSRRSSVKSIEKETFvaepsarsnsfvgteeYIAPEVIKG 206
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  602 RRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05574    207 DGHGSAVDWWTLGILLYEML-YGTTPFKGSNRDETFSNILKKElTFPESPPVSSEAKDLIRKLLVKDPSKR 276
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
470-677 1.37e-15

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: 78.04  E-value: 1.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLIGV---ITENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR 546
Cdd:cd13983     44 RQRFKQEIEILKSLKHPNIIKFYDSwesKSKKEVIFITELMTSGTLKQYLK-RFKRLKLKVIKSWCRQILEGLNYLHTRD 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  547 --FVHRDIAARNVLVSSND-CVKLGDFGLSRYMedstyyKASKGKLPI---KWMAPEsINFRRFTSASDVWMFGVCMWEi 620
Cdd:cd13983    123 ppIIHRDLKCDNIFINGNTgEVKIGDLGLATLL------RQSFAKSVIgtpEFMAPE-MYEEHYDEKVDIYAFGMCLLE- 194
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  621 LMHGVKPFQGVKNN-DVIGRIENGErlpmPPNC-----PPTLYSLMTKCWAyDPSRRPRFTEL 677
Cdd:cd13983    195 MATGEYPYSECTNAaQIYKKVTSGI----KPESlskvkDPELKDFIEKCLK-PPDERPSAREL 252
PHA02988 PHA02988
hypothetical protein; Provisional
422-683 1.89e-15

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 77.86  E-value: 1.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  422 IQRERIELgrcIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVITENP 499
Cdd:PHA02988    20 IDKYTSVL---IKENDQNSIYKGIFNNKE-----VIIRTFKKFHKGHkvLIDITENEIKNLRRIDSNNILKIYGFIIDIV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 -----VWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESK-RFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:PHA02988    92 ddlprLSLILEYCTRGYLREVLDKEK-DLSFKTKLDMAIDCCKGLYNLYKYtNKPYKNLTSVSFLVTENYKLKIICHGLE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKaskgklpIKWMAPESIN-----FRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI--ENGErL 646
Cdd:PHA02988   171 KILSSPPFKN-------VNFMVYFSYKmlndiFSEYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIinKNNS-L 241
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1914779978  647 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 683
Cdd:PHA02988   242 KLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNLSL 278
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
431-620 2.01e-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: 78.53  E-value: 2.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCtL 509
Cdd:cd06634     21 REIGHGSFGAVYFARDVR-NNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCyLREHTAWLVMEYC-L 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKgkl 589
Cdd:cd06634     99 GSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPANSFVGTP--- 175
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1914779978  590 piKWMAPESI---NFRRFTSASDVWMFGVCMWEI 620
Cdd:cd06634    176 --YWMAPEVIlamDEGQYDGKVDVWSLGITCIEL 207
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
433-677 2.39e-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: 77.58  E-value: 2.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgIYMSPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGE 511
Cdd:cd06622      9 LGKGNYGSVYK-VLHRPTG--VTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFiEGAVYMCMEYMDAGS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFL--QVRKYSLDLASLILYAYQLSTALAYL-ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdstyykASKGK 588
Cdd:cd06622     86 LDKLYagGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV------ASLAK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPI---KWMAPESINFR------RFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGR---IENGERLPMPPNCPPTL 656
Cdd:cd06622    160 TNIgcqSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMAL-GRYPYPPETYANIFAQlsaIVDGDPPTLPSGYSDDA 238
                          250       260
                   ....*....|....*....|.
gi 1914779978  657 YSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06622    239 QDFVAKCLNKIPNRRPTYAQL 259
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
484-671 2.54e-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: 78.41  E-value: 2.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  484 DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSS 561
Cdd:cd05570     54 RHPFLTGLHACFqTEDRLYFVMEYVNGGDLMFHIQrARRFTEERA--RFYAAEICLALQFLHERGIIYRDLKLDNVLLDA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  562 NDCVKLGDFGLSRymEDSTYYKASK---GKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIG 638
Cdd:cd05570    132 EGHIKIADFGMCK--EGIWGGNTTStfcGTP--DYIAPEILREQDYGFSVDWWALGVLLYEMLA-GQSPFEGDDEDELFE 206
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1914779978  639 RIENGE-RLP--MPPNCPPTLYSLMTKcwayDPSRR 671
Cdd:cd05570    207 AILNDEvLYPrwLSREAVSILKGLLTK----DPARR 238
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-628 2.79e-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: 2.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKtCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGvITENP--V 500
Cdd:cd14083      2 RDKYEFKEVLGTGAFSEV---VLAEDKATGKLVAIK-CIDKKALKGKEDSLEnEIAVLRKIKHPNIVQLLD-IYESKshL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRyM 576
Cdd:cd14083     77 YLVMELVTGGELfDRIVEKGSYTEKDASHLIR--QVLEAVDYLHSLGIVHRDLKPENLLYYSPDedsKIMISDFGLSK-M 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  577 EDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14083    154 EDSGVMSTACGT-P-GYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPF 202
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
433-677 2.88e-15

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 76.58  E-value: 2.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiYMSPENPALaVAIKTCKNC-TSDSVREKFLQEALTMRQF-DHPHIVKLIGVITE-NPVWIIMELCTL 509
Cdd:cd14050      9 LGEGSFGEVFK--VRSREDGKL-YAVKRSRSRfRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEkGILYIQTELCDT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 gelrSFLQ--VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd14050     86 ----SLQQycEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KlpIKWMAPESINfRRFTSASDVWMFGVCMWEI-----LMHGVKPFQGVKNNDVIGRIENGerlpMPPNCPPTLYSLMTK 662
Cdd:cd14050    162 D--PRYMAPELLQ-GSFTKAADIFSLGITILELacnleLPSGGDGWHQLRQGYLPEEFTAG----LSPELRSIIKLMMDP 234
                          250
                   ....*....|....*
gi 1914779978  663 cwayDPSRRPRFTEL 677
Cdd:cd14050    235 ----DPERRPTAEDL 245
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
425-629 3.05e-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: 76.82  E-value: 3.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMspeNPALAVAIKTC--KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVW 501
Cdd:cd14186      1 EDFKVLNLLGKGSFACVYRARSL---HTGLEVAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDsNYVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRK--YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd14186     78 LVLEMCHNGEMSRYLKNRKkpFTEDEARHFMH--QIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMP 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQ 629
Cdd:cd14186    156 HEKHFTMCGTP-NYISPEIATRSAHGLESDVWSLG-CMFYTLLVGRPPFD 203
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
425-738 3.05e-15

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 80.22  E-value: 3.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHqgiymspenpaLA--------VAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGV 494
Cdd:NF033483     7 GRYEIGERIGRGGMAEVY-----------LAkdtrldrdVAVKVLRPdlARDPEFVARFRREAQSAASLSHPNIVSVYDV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITENPV-WIIMEL---CTLGEL---RSFLQVRKySLDLASLILyayqlsTALAYLESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:NF033483    76 GEDGGIpYIVMEYvdgRTLKDYireHGPLSPEE-AVEIMIQIL------SALEHAHRNGIVHRDIKPQNILITKDGRVKV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDST-----------YYkaskgklpikwMAPE-----SINFRrftsaSDVWMFGVCMWEILMhGVKPFQGv 631
Cdd:NF033483   149 TDFGIARALSSTTmtqtnsvlgtvHY-----------LSPEqarggTVDAR-----SDIYSLGIVLYEMLT-GRPPFDG- 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  632 knndvigriEN---------GERLPMP----PNCPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAqQEERMR 697
Cdd:NF033483   211 ---------DSpvsvaykhvQEDPPPPselnPGIPQSLDAVVLKATAKDPDDRYQsAAEMRADLETALSGQRL-NAPKFA 280
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  698 MESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSP 738
Cdd:NF033483   281 PDSDDDRTKVLPPIPPAPAPTAAEPPEDPDDDGEGGEPADD 321
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
433-677 3.68e-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: 77.45  E-value: 3.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPenpALAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTLGE 511
Cdd:cd06656     27 IGQGASGTVYTAIDIAT---GQEVAIKQ-MNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGS 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06656    103 LTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  592 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-ENGE-RLPMPPNCPPTLYSLMTKCWAYDPS 669
Cdd:cd06656    181 -WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIaTNGTpELQNPERLSAVFRDFLNRCLEMDVD 258

                   ....*...
gi 1914779978  670 RRPRFTEL 677
Cdd:cd06656    259 RRGSAKEL 266
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
455-672 5.08e-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: 76.54  E-value: 5.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  455 AVAIK-TCKNCTSDSVRE-KFLQEAltmrqFDHPHIVKLIGV-ITENPVWIIMELC--TLGEL----RSFLQVRKYSLDL 525
Cdd:cd13982     27 PVAVKrLLPEFFDFADREvQLLRES-----DEHPNVIRYFCTeKDRQFLYIALELCaaSLQDLvespRESKLFLRPGLEP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  526 ASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-----VKLGDFGLSRYMED--STYYKASKGKLPIKWMAPES 598
Cdd:cd13982    102 VRLL---RQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLDVgrSSFSRRSGVAGTSGWIAPEM 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  599 IN---FRRFTSASDVWMFGVCMWEILMHGVKPFQG--VKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd13982    179 LSgstKRRQTRAVDIFSLGCVFYYVLSGGSHPFGDklEREANILKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRP 257
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
438-684 5.51e-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: 76.29  E-value: 5.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  438 FGDVHQGIYMSPENPALAVA-------IKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELCTL 509
Cdd:cd14043      1 PSSPSSTSSVNATSSNTGVAyegdwvwLKKFPGGSHTELRPSTKNVFSKLRELRHENVNLFLGLFVDCGILaIVSEHCSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDL---ASLILyayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd14043     81 GSLEDLLRNDDMKLDWmfkSSLLL---DLIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEILEAQNLPLPEP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPIKWMAPESIN----FRRFTSASDVWMFGVCMWEILMHGvKPF--QGVKNNDVIGRIengeRLPmPPNC-------- 652
Cdd:cd14043    158 APEELLWTAPELLRdprlERRGTFPGDVFSFAIIMQEVIVRG-APYcmLGLSPEEIIEKV----RSP-PPLCrpsvsmdq 231
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1914779978  653 -PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14043    232 aPLECIQLMKQCWSEAPERRPTFDQIFDQFKSI 264
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
433-678 6.16e-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: 76.65  E-value: 6.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQG---IYMSPENPALAVAIKTCKNCTSDSvREKflqEALTMRQFDHPHIVKLI-----GVITENPVWIIM 504
Cdd:cd14055      3 VGKGRFAEVWKAklkQNASGQYETVAVKIFPYEEYASWK-NEK---DIFTDASLKHENILQFLtaeerGVGLDRQYWLIT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRF---------VHRDIAARNVLVSSN-DCVkLGDFGLSR 574
Cdd:cd14055     79 AYHENGSLQDYL--TRHILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDgTCV-LADFGLAL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDSTYYK--ASKGKL-PIKWMAPES----INFRRFTS--ASDVWMFGVCMWEI-----LMHGVKPFQ----------- 629
Cdd:cd14055    156 RLDPSLSVDelANSGQVgTARYMAPEAlesrVNLEDLESfkQIDVYSMALVLWEMasrceASGEVKPYElpfgskvrerp 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  630 ---GVKNNDVIGRiengERLPMPP--NCPPTLYSL---MTKCWAYDPSRR-------PRFTELK 678
Cdd:cd14055    236 cveSMKDLVLRDR----GRPEIPDswLTHQGMCVLcdtITECWDHDPEARltascvaERFNELK 295
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
419-673 6.49e-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: 76.52  E-value: 6.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHQGIYMSpENPALAVAI--KTCKNCtSDSVrekflqEALtMRQFDHPHIVKLIGV-I 495
Cdd:cd14091      1 EYEIKEE-------IGKGSYSVCKRCIHKA-TGKEYAVKIidKSKRDP-SEEI------EIL-LRYGQHPNIITLRDVyD 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRS-FLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLVSSN----DCVKLGDF 570
Cdd:cd14091     65 DGNSVYLVTELLRGGELLDrILRQKFFSEREASAVMKT--LTKTVEYLHSQGVVHRDLKPSNILYADEsgdpESLRICDF 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  571 GLSRYMedstyyKASKGKL--PI---KWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKN---NDVIGRIEN 642
Cdd:cd14091    143 GFAKQL------RAENGLLmtPCytaNFVAPEVLKKQGYDAACDIWSLGVLLY-TMLAGYTPFASGPNdtpEVILARIGS 215
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1914779978  643 GeRLPMP-PN---CPPTLYSLMTKCWAYDPSRRPR 673
Cdd:cd14091    216 G-KIDLSgGNwdhVSDSAKDLVRKMLHVDPSQRPT 249
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
433-673 7.50e-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: 75.81  E-value: 7.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHqgIYMS---PENPALAVAI--KTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVW-IIME 505
Cdd:cd13994      1 IGKGATSVVR--IVTKknpRSGVLYAVKEyrRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLcQDLHGKWcLVME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS---RYMEDST-- 580
Cdd:cd13994     79 YCPGGDLFTLI-EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAevfGMPAEKEsp 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKLPikWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLPMPPNCPPTLYS 658
Cdd:cd13994    158 MSAGLCGSEP--YMAPEVFTSGSYDgRAVDVWSCGIVLFALFT-GRFPWRSAKKSDSAYKAyEKSGDFTNGPYEPIENLL 234
                          250       260
                   ....*....|....*....|.
gi 1914779978  659 LMT-KCWAY-----DPSRRPR 673
Cdd:cd13994    235 PSEcRRLIYrmlhpDPEKRIT 255
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
471-678 8.17e-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: 76.14  E-value: 8.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  471 EKFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKYSLDLASLilYAYQLSTALAYLESKRF 547
Cdd:cd14200     68 ERVYQEIAILKKLDHVNIVKLIEVLddpAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARL--YFRDIVLGIEYLHYQKI 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESI--NFRRFT-SASDVWMFGVCMWeILMHG 624
Cdd:cd14200    146 VHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTP-AFMAPETLsdSGQSFSgKALDVWAMGVTLY-CFVYG 223
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  625 VKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14200    224 KCPFIDEFILALHNKIKNKPvEFPEEPEISEELKDLILKMLDKNPETRITVPEIK 278
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
426-705 1.12e-14

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: 76.74  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFG------DVHQGiymspenpaLAVAIKTCKNC---TSDSVRekFLQEALTMRQFDHPHIVKLIGVI- 495
Cdd:cd07859      1 RYKIQEVIGKGSYGvvcsaiDTHTG---------EKVAIKKINDVfehVSDATR--ILREIKLLRLLRHPDIVEIKHIMl 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 -----TENPVWIIMELctlgeLRSFL-QVRKYSLDLAS--LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 567
Cdd:cd07859     70 ppsrrEFKDIYVVFEL-----MESDLhQVIKANDDLTPehHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKI 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  568 GDFGLSRYMEDS-------TYYKASkgklpiKWM-APESIN--FRRFTSASDVWMFGvCMWEILMHGvKP---------- 627
Cdd:cd07859    145 CDFGLARVAFNDtptaifwTDYVAT------RWYrAPELCGsfFSKYTPAIDIWSIG-CIFAEVLTG-KPlfpgknvvhq 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  628 ------FQGVKNNDVIGRIENGE----------RLPMP-----PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ-----L 681
Cdd:cd07859    217 ldlitdLLGTPSPETISRVRNEKarrylssmrkKQPVPfsqkfPNADPLALRLLERLLAFDPKDRPTAEEALADpyfkgL 296
                          330       340
                   ....*....|....*....|....*
gi 1914779978  682 STILEEEKAQQEERMRME-SRRQAT 705
Cdd:cd07859    297 AKVEREPSAQPITKLEFEfERRRLT 321
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
433-651 1.42e-14

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: 74.76  E-value: 1.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLG 510
Cdd:cd14082     11 LGSGQFGIVYGGKH---RKTGRDVAIKVIDKLRFPTKQESQLRnEVAILQQLSHPGVVNLECMFeTPERVFVVMEKLHGD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC---VKLGDFGLSRYMEDSTYYKASKG 587
Cdd:cd14082     88 MLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARIIGEKSFRRSVVG 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  588 KlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQgvKNNDVIGRIENGERLpMPPN 651
Cdd:cd14082    168 T-P-AYLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPFN--EDEDINDQIQNAAFM-YPPN 225
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
468-630 1.52e-14

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: 75.08  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  468 SVREKFLQE-ALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESK 545
Cdd:cd14106     49 DCRNEILHEiAVLELCKDCPRVVNLHEVYeTRSELILILELAAGGELQTLL-DEEECLTEADVRRLMRQILEGVQYLHER 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  546 RFVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDSTYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWeILM 622
Cdd:cd14106    128 NIVHLDLKPQNILLTSefpLGDIKLCDFGISRVIGEGEEIREILGTP--DYVAPEILSYEPISLATDMWSIGVLTY-VLL 204

                   ....*...
gi 1914779978  623 HGVKPFQG 630
Cdd:cd14106    205 TGHSPFGG 212
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
431-684 1.55e-14

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: 75.21  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSpENPALAVAIKTCKnctSDSVREKFLQEALTMRqfdHPHIVKLIGV-ITENPVW----IIME 505
Cdd:cd14144      1 RSVGKGRYGEVWKGKWRG-EKVAVKIFFTTEE---ASWFRETEIYQTVLMR---HENILGFIAAdIKGTGSWtqlyLITD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRkySLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDFGLS-RYM 576
Cdd:cd14144     74 YHENGSLYDFLRGN--TLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLGLAvKFI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTYYKASKG-KLPIK-WMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK---------PFQGVKNND---- 635
Cdd:cd14144    152 SETNEVDLPPNtRVGTKrYMAPEvldeSLNRNHFDAykMADMYSFGLVLWEIARRCISggiveeyqlPYYDAVPSDpsye 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  636 VIGRIENGERL-PMPPN------CPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14144    232 DMRRVVCVERRrPSIPNrwssdeVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
433-628 1.72e-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: 75.53  E-value: 1.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPenpALAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTLGE 511
Cdd:cd06654     28 IGQGASGTVYTAMDVAT---GQEVAIRQ-MNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 591
Cdd:cd06654    104 LTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 181
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1914779978  592 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPF 628
Cdd:cd06654    182 -WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPY 216
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
470-643 2.00e-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: 2.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLIGVITENP--VWIIMELCTLGELRSFLQVRKYSLDLASLI-LYAYQLSTALAYLESKR 546
Cdd:cd14109     40 DPFLMREVDIHNSLDHPNIVQMHDAYDDEKlaVTVIDNLASTIELVRDNLLPGKDYYTERQVaVFVRQLLLALKHMHDLG 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  547 FVHRDIAARNVLVSsNDCVKLGDFGLSRYMEDSTYYKASKGkLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVK 626
Cdd:cd14109    120 IAHLDLRPEDILLQ-DDKLKLADFGQSRRLLRGKLTTLIYG-SP-EFVSPEIVNSYPVTLATDMWSVGVLTY-VLLGGIS 195
                          170
                   ....*....|....*..
gi 1914779978  627 PFQGVKNNDVIGRIENG 643
Cdd:cd14109    196 PFLGDNDRETLTNVRSG 212
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
425-685 2.05e-14

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: 75.17  E-value: 2.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSpENpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLIG--VITENP-- 499
Cdd:cd14142      5 RQITLVECIGKGRYGEVWRGQWQG-ES----VAVKIFSSRDEKSwFRETEIYNTVLLR---HENILGFIAsdMTSRNSct 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 -VWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDF 570
Cdd:cd14142     77 qLWLITHYHENGSLYDYLQ--RTTLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  571 GLsrymedSTYYKASKGKLPI---------KWMAP----ESINFRRFTS--ASDVWMFGVCMWEI----LMHGV-----K 626
Cdd:cd14142    155 GL------AVTHSQETNQLDVgnnprvgtkRYMAPevldETINTDCFESykRVDIYAFGLVLWEVarrcVSGGIveeykP 228
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  627 PFQGVKNND--------VIgrIENGERlPMPPN---CPPTLYS---LMTKCWAYDPSRRPRFTELKAQLSTIL 685
Cdd:cd14142    229 PFYDVVPSDpsfedmrkVV--CVDQQR-PNIPNrwsSDPTLTAmakLMKECWYQNPSARLTALRIKKTLLKIL 298
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
429-677 2.08e-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: 2.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQgIYMSPENPALAVA-IKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI---TENPVWII 503
Cdd:cd06653      6 LGKLLGRGAFGEVYL-CYDADTGRELAVKqVPFDPDSQETSKEVNALEcEIQLLKNLRHDRIVQYYGCLrdpEEKKLSIF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSflQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdsTYY 582
Cdd:cd06653     85 VEYMPGGSVKD--QLKAYgALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQ--TIC 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPM-PPNCPPTLY 657
Cdd:cd06653    161 MSGTGIKSVTgtpyWMSPEVISGEGYGRKADVWSVACTVVEMLTEK-PPWAEYEAMAAIFKIATQPTKPQlPDGVSDACR 239
                          250       260
                   ....*....|....*....|
gi 1914779978  658 SLMTKCWaYDPSRRPRFTEL 677
Cdd:cd06653    240 DFLRQIF-VEEKRRPTAEFL 258
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
433-640 2.28e-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: 2.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiymSPENPALAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlG 510
Cdd:cd07860      8 IGEGTYGVVYKA---RNKLTGEVVALKKIRlDTETEGVPSTAIREISLLKELNHPNIVKLLDVIhTENKLYLVFEFLH-Q 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY--MEDSTYykaSKG 587
Cdd:cd07860     84 DLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAfgVPVRTY---THE 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  588 KLPIKWMAPES-INFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRI 640
Cdd:cd07860    161 VVTLWYRAPEIlLGCKYYSTAVDIWSLG-CIFAEMVTRRALFPGDSEIDQLFRI 213
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
470-671 2.32e-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: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQF-----DHPHIVKL-IGVITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLE 543
Cdd:cd05583     38 KAKTAEHTMTERQVleavrQSPFLVTLhYAFQTDAKLHLILDYVNGGELFTHLYQREH-FTESEVRIYIGEIVLALEHLH 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  544 SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRR--FTSASDVWMFGVCMWEIL 621
Cdd:cd05583    117 KLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELL 196
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  622 MhGVKPF--QGVKNN--DVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
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; ...
433-642 2.33e-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: 2.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmsPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI---TENP-VWIIMELCT 508
Cdd:cd14664      1 IGRGGAGTVYKGVM--PNG--TLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCsnpTTNLlVYEYMPNGS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLE---SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd14664     77 LGELLHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMS 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQ---GVKNNDVIGRIEN 642
Cdd:cd14664    157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLE-LITGKRPFDeafLDDGVDIVDWVRG 215
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
433-653 2.44e-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: 74.68  E-value: 2.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMspENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQ---FDHPHIVKLIGVIT------ENPVWI 502
Cdd:cd07862      9 IGEGAYGKVFKARDL--KNGGRFVALKRVRVQTGEEgMPLSTIREVAVLRHletFEHPNVVRLFDVCTvsrtdrETKLTL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTlGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMedsTY 581
Cdd:cd07862     87 VFEHVD-QDLTTYLdKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIY---SF 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  582 YKASKGKLPIKWM-APESINFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRIENGERLPMPPNCP 653
Cdd:cd07862    163 QMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAE--MFRRKPlFRGSSDVDQLGKILDVIGLPGEEDWP 234
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
412-630 2.63e-14

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 75.04  E-value: 2.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  412 YGIDEARDYEIqrerieLGRcIGEGQFGDVHQGIYMSPENpalAVAIKtckNCTSDSVREKF----LQEALTMRQFDHPH 487
Cdd:cd07866      2 YGCSKLRDYEI------LGK-LGEGTFGEVYKARQIKTGR---VVALK---KILMHNEKDGFpitaLREIKILKKLKHPN 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  488 IVKLIGVITENPVwiimelCTLGELRSFLQVRKY-SLDLASLI-------------LYAYQLSTALAYLESKRFVHRDIA 553
Cdd:cd07866     69 VVPLIDMAVERPD------KSKRKRGSVYMVTPYmDHDLSGLLenpsvkltesqikCYMLQLLEGINYLHENHILHRDIK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  554 ARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIK--------WM-APESI-NFRRFTSASDVWMFGVCMWEilM 622
Cdd:cd07866    143 AANILIDNQGILKIADFGLARpYDGPPPNPKGGGGGGTRKytnlvvtrWYrPPELLlGERRYTTAVDIWGIGCVFAE--M 220

                   ....*....
gi 1914779978  623 HGVKP-FQG 630
Cdd:cd07866    221 FTRRPiLQG 229
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
471-678 2.89e-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: 2.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  471 EKFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKYSLDLASLilYAYQLSTALAYLESKRF 547
Cdd:cd14118     59 DRVYREIAILKKLDHPNVVKLVEVLddpNEDNLYMVFELVDKGAVMEVPTDNPLSEETARS--YFRDIVLGIEYLHYQKI 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESI-NFRRFTS--ASDVWMFGVCMWeILMHG 624
Cdd:cd14118    137 IHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTP-AFMAPEALsESRKKFSgkALDIWAMGVTLY-CFVFG 214
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  625 VKPFQgvkNNDVIG---RIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14118    215 RCPFE---DDHILGlheKIKTDPvVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIK 269
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
433-640 3.60e-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: 74.18  E-value: 3.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNctsDSVREKF----LQEALTMRQFDHPHIVKLIGVI---TENPVWIIME 505
Cdd:cd07843     13 IEEGTYGVVYRARDKKTGE---IVALKKLKM---EKEKEGFpitsLREINILLKLQHPNIVTVKEVVvgsNLDKIYMVME 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 lCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDstyykas 585
Cdd:cd07843     87 -YVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS------- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  586 kgklPIKWM----------APESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGRI 640
Cdd:cd07843    159 ----PLKPYtqlvvtlwyrAPELLlGAKEYSTAIDMWSVGCIFAELLTK--KPlFPGKSEIDQLNKI 219
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
484-686 3.86e-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: 3.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  484 DHPHIVKLIGVITEN--------PVWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAAR 555
Cdd:cd13975     56 KHERIVSLHGSVIDYsygggssiAVLLIMERLH----RDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLK 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  556 NVLVSSNDCVKLGDFGlsrYMEDSTYYKASKGKLPIKwMAPESINfRRFTSASDVWMFGVCMWEILMHGVK---PFQGVK 632
Cdd:cd13975    132 NVLLDKKNRAKITDLG---FCKPEAMMSGSIVGTPIH-MAPELFS-GKYDNSVDVYAFGILFWYLCAGHVKlpeAFEQCA 206
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  633 NNDVIGR-IENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd13975    207 SKDHLWNnVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMD 261
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
433-677 4.06e-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: 74.38  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVhqgiyMSPENPALA--VAIKTCkNCTSDSVREKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTL 509
Cdd:cd06655     27 IGQGASGTV-----FTAIDVATGqeVAIKQI-NLQKQPKKELIINEILVMKELKNPNIVNFLdSFLVGDELFVVMEYLAG 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 589
Cdd:cd06655    101 GSLTDV--VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  590 PIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-ENGE-RLPMPPNCPPTLYSLMTKCWAYD 667
Cdd:cd06655    179 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIaTNGTpELQNPEKLSPIFRDFLNRCLEMD 256
                          250
                   ....*....|
gi 1914779978  668 PSRRPRFTEL 677
Cdd:cd06655    257 VEKRGSAKEL 266
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
428-671 4.40e-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: 74.01  E-value: 4.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIY-MSPENPALAV-AIktcknctSDSVREKFLQ----EALTMRQFDHPHIVKLIGVI-TENPV 500
Cdd:cd05612      4 ERIKTIGTGTFGRVHLVRDrISEHYYALKVmAI-------PEVIRLKQEQhvhnEKRVLKEVSHPFIIRLFWTEhDQRFL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd05612     77 YMLMEYVPGGELFSYLRnSGRFSNSTG--LFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKgklPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSL 659
Cdd:cd05612    155 TWTLCGT---P-EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFDDNPFGIYEKILAG-KLEFPRHLDLYAKDL 228
                          250
                   ....*....|..
gi 1914779978  660 MTKCWAYDPSRR 671
Cdd:cd05612    229 IKKLLVVDRTRR 240
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
433-640 4.64e-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: 4.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSD------SVREKFLQEALtmRQFDHPHIVKLIGVIT------ENPV 500
Cdd:cd07863      8 IGVGAYGTVYKA--RDPHSGHF-VALKSVRVQTNEdglplsTVREVALLKRL--EAFDHPNIVRLMDVCAtsrtdrETKV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTlGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeds 579
Cdd:cd07863     83 TLVFEHVD-QDLRTYLdKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIY--- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  580 TYYKASKGKLPIKWM-APESINFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRI 640
Cdd:cd07863    159 SCQMALTPVVVTLWYrAPEVLLQSTYATPVDMWSVGCIFAE--MFRRKPlFCGNSEADQLGKI 219
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
478-677 5.20e-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: 73.48  E-value: 5.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  478 LTMRQFDHPHIVKLIGVItENPV------WIIMELCTLGELRSFLQVR---KYSLDLASLILYayQLSTALAYLESKRFV 548
Cdd:cd14089     46 LHWRASGCPHIVRIIDVY-ENTYqgrkclLVVMECMEGGELFSRIQERadsAFTEREAAEIMR--QIGSAVAHLHSMNIA 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLVSSN--DCV-KLGDFGLSRYMEDST---------YYkaskgklpikwMAPESINFRRFTSASDVWMFGVC 616
Cdd:cd14089    123 HRDLKPENLLYSSKgpNAIlKLTDFGFAKETTTKKslqtpcytpYY-----------VAPEVLGPEKYDKSCDMWSLGVI 191
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  617 MWeILMHGVKPF---------QGVKNndvigRIENGE-RLPMP--PNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14089    192 MY-ILLCGYPPFysnhglaisPGMKK-----RIRNGQyEFPNPewSNVSEEAKDLIRGLLKTDPSERLTIEEV 258
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
433-674 5.28e-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: 72.91  E-value: 5.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGVITE--NPVwIIMELCTLG 510
Cdd:cd14057      3 INETHSGELWKGRWQGND---IVAKILKVRDVTTRISRD-FNEEYPRLRIFSHPNVLPVLGACNSppNLV-VISQYMPYG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFL-QVRKYSLDLASLILYAYQLSTALAYLES-KRFVHR-DIAARNVLVSSNDCVKLGdfglsryMEDSTYYKASKG 587
Cdd:cd14057     78 SLYNVLhEGTGVVVDQSQAVKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARIN-------MADVKFSFQEPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KL-PIKWMAPES-------INFRrftsASDVWMFGVCMWEILMHGVkPFQGVKNNDVIGRIE-NGERLPMPPNCPPTLYS 658
Cdd:cd14057    151 KMyNPAWMAPEAlqkkpedINRR----SADMWSFAILLWELVTREV-PFADLSNMEIGMKIAlEGLRVTIPPGISPHMCK 225
                          250
                   ....*....|....*.
gi 1914779978  659 LMTKCWAYDPSRRPRF 674
Cdd:cd14057    226 LMKICMNEDPGKRPKF 241
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
433-671 5.42e-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: 5.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHqgIYMSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-----NPVWII-MEL 506
Cdd:cd14039      1 LGTGGFGNVC--LYQNQETGEK-IAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEmnflvNDVPLLaMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQVRKYSLDL--ASLILYAYQLSTALAYLESKRFVHRDIAARNVL---VSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd14039     78 CSGGDLRKLLNKPENCCGLkeSQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVlqeINGKIVHKIIDLGYAKDLDQGSL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEIL------MHGVKPFQ---GVKNND---------VIGRIENG 643
Cdd:cd14039    158 CTSFVGTL--QYLAPELFENKSYTVTVDYWSFGTMVFECIagfrpfLHNLQPFTwheKIKKKDpkhifaveeMNGEVRFS 235
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1914779978  644 ERLPMPPNCPPTLYSLMtKCW-----AYDPSRR 671
Cdd:cd14039    236 THLPQPNNLCSLIVEPM-EGWlqlmlNWDPVQR 267
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
431-620 5.56e-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: 74.32  E-value: 5.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNCTSDSVR--EKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELC 507
Cdd:cd06635     31 REIGHGSFGAVY---FARDVRTSEVVAIKKMSYSGKQSNEkwQDIIKEVKFLQRIKHPNSIEYKGCyLREHTAWLVMEYC 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 tLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKg 587
Cdd:cd06635    108 -LGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTP- 185
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1914779978  588 klpiKWMAPESI---NFRRFTSASDVWMFGVCMWEI 620
Cdd:cd06635    186 ----YWMAPEVIlamDEGQYDGKVDVWSLGITCIEL 217
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
425-677 5.63e-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: 73.40  E-value: 5.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIElgrCIGEGQFGDVHQgiYMSPENPALAVAiKTCKNCTSDSVREKFLQE-ALTMRQFDHPHIVKLIGV-ITENP--V 500
Cdd:cd14131      4 EILK---QLGKGGSSKVYK--VLNPKKKIYALK-RVDLEGADEQTLQSYKNEiELLKKLKGSDRIIQLYDYeVTDEDdyL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELctlGE--LRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARN-VLVSSNdcVKLGDFGLSRYM 576
Cdd:cd14131     78 YMVMEC---GEidLATILKKKRPKpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVKGR--LKLIDFGIAKAI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 -EDST-YYKASK-GKLpiKWMAPESINFRRFTS----------ASDVWMFGvCMWEILMHGVKPFQGVKN-NDVIGRIEN 642
Cdd:cd14131    153 qNDTTsIVRDSQvGTL--NYMSPEAIKDTSASGegkpkskigrPSDVWSLG-CILYQMVYGKTPFQHITNpIAKLQAIID 229
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  643 -GERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14131    230 pNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPEL 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
467-671 5.75e-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: 73.54  E-value: 5.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  467 DSVREKFLQEALTMRQFD-HPHIVKLIGVItENPVWI--IMELCTLGELRSFL-QVRKYSLDLASLILYayQLSTALAYL 542
Cdd:cd14093     49 EELREATRREIEILRQVSgHPNIIELHDVF-ESPTFIflVFELCRKGELFDYLtEVVTLSEKKTRRIMR--QLFEAVEFL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  543 ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRRFTSAS------DVWMFGVC 616
Cdd:cd14093    126 HSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRELCGT-P-GYLAPEVLKCSMYDNAPgygkevDMWACGVI 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  617 MWEILMhGVKPFQGVKNNDVIGRIENGE---RLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd14093    204 MYTLLA-GCPPFWHRKQMVMLRNIMEGKyefGSPEWDDISDTAKDLISKLLVVDPKKR 260
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
433-677 5.82e-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: 73.61  E-value: 5.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVITENPVWII----MELC 507
Cdd:cd07846      9 VGEGSYGMVMK---CRHKETGQIVAIKKFLESEDDKmVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLvfefVDHT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFlqvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM----EDSTYYK 583
Cdd:cd07846     86 VLDDLEKY----PNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEVYTDYV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASkgklpiKWM-APE-SINFRRFTSASDVWMFGVCMWEILM---------------HGVK-----------------PFQ 629
Cdd:cd07846    162 AT------RWYrAPElLVGDTKYGKAVDVWAVGCLVTEMLTgeplfpgdsdidqlyHIIKclgnliprhqelfqknpLFA 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1914779978  630 GVKNNDViGRIENGERLpmPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd07846    236 GVRLPEV-KEVEPLERR--YPKLSGVVIDLAKKCLHIDPDKRPSCSEL 280
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
418-628 7.60e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 74.25  E-value: 7.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  418 RDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAlaVAIKTCKNCTSdsVREKFLQEALTMRQF----DHPHIVKLIG 493
Cdd:PTZ00426    23 RKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDFPP--VAIKRFEKSKI--IKQKQVDHVFSERKIlnyiNHPFCVNLYG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 VIT-ENPVWIIMELCTLGELRSFLQVRK-YSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 571
Cdd:PTZ00426    99 SFKdESYLYLVLEFVIGGEFFTFLRRNKrFPNDVGCF--YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFG 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  572 LSRYMEDSTYYKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:PTZ00426   177 FAKVVDTRTYTLCGTP----EYIAPEILLNVGHGKAADWWTLGIFIYEILV-GCPPF 228
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
418-620 8.84e-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: 8.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  418 RDYE-IQRerielgrcIGEGQFGDVHQGIYMSPENPAlavAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIG-VI 495
Cdd:cd06646      9 HDYElIQR--------VGSGTYGDVYKARNLHTGELA---AVKIIKLEPGDDF-SLIQQEIFMVKECKHCNIVAYFGsYL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQVRK--YSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd06646     77 SREKLWICMEYCGGGSLQDIYHVTGplSELQIAYVCRETLQ---GLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVA 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKASKGKLPIkWMAPESINFRR---FTSASDVWMFGVCMWEI 620
Cdd:cd06646    154 AKITATIAKRKSFIGTPY-WMAPEVAAVEKnggYNQLCDIWAVGITAIEL 202
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
433-640 8.89e-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: 72.90  E-value: 8.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiyMSPENPALaVAIKTCK-----NCTSDSVREKFLqealtMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd07836      8 LGEGTYATVYKG--RNRTTGEI-VALKEIHldaeeGTPSTAIREISL-----MKELKHENIVRLHDVIhTENKLMLVFEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTlGELRSFLQVR--KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY--MEDSTYy 582
Cdd:cd07836     80 MD-KDLKKYMDTHgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAfgIPVNTF- 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  583 kaSKGKLPIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI 640
Cdd:cd07836    158 --SNEVVTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMIT-GRPLFPGTNNEDQLLKI 213
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
383-621 8.98e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.14  E-value: 8.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  383 STDEISGDETDDYAEIIDEEDTYTMPSKSYGIDEARDYEIqreriELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCK 462
Cdd:PHA03209    29 SDGDLEYSDDDSASESDDDDDDGLIPTKQKAREVVASLGY-----TVIKTLTPGSEGRV---FVATKPGQPDPVVLKIGQ 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  463 NCTSdsvrekfLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYL 542
Cdd:PHA03209   101 KGTT-------LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYL 173
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  543 ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEIL 621
Cdd:PHA03209   174 HAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGT--VETNAPEVLARDKYNSKADIWSAGIVLFEML 250
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
399-705 9.15e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 74.69  E-value: 9.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  399 IDEEDTYTMPSKSYGIDEAR--DYEIQR---ERIELGRCIGEGQFGDVHQGIYMspeNPALAVAIKtcknctsdsvreKF 473
Cdd:PTZ00036    35 LDEEERSHNNNAGEDEDEEKmiDNDINRspnKSYKLGNIIGNGSFGVVYEAICI---DTSEKVAIK------------KV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  474 LQ-------EALTMRQFDHPHIVKLIGVI-------TENPVW--IIMELC--TLGELRSFLQVRKYSLDLASLILYAYQL 535
Cdd:PTZ00036   100 LQdpqyknrELLIMKNLNHINIIFLKDYYytecfkkNEKNIFlnVVMEFIpqTVHKYMKHYARNNHALPLFLVKLYSYQL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  536 STALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGLSRYM---EDSTYYKASKgklpiKWMAPE-SINFRRFTSASDV 610
Cdd:PTZ00036   180 CRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFGSAKNLlagQRSVSYICSR-----FYRAPElMLGATNYTTHIDL 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  611 WMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLP-------MPPN---------------------CPPTLYSLMTK 662
Cdd:PTZ00036   255 WSLGCIIAEMIL-GYPIFSGQSSVDQLVRIIQVLGTPtedqlkeMNPNyadikfpdvkpkdlkkvfpkgTPDDAINFISQ 333
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  663 CWAYDPSRR---------PRFTELK----------AQLSTILEEEKAQQEErMRMESRRQAT 705
Cdd:PTZ00036   334 FLKYEPLKRlnpiealadPFFDDLRdpciklpkyiDKLPDLFNFCDAEIKE-MSDACRRKII 394
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
425-640 9.23e-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: 73.34  E-value: 9.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNctsdsVRE-KFLQEALTMRQF-DHPHIVKLIGVI----TEN 498
Cdd:cd14132     18 DDYEIIRKIGRGKYSEVFEGINIGNNEK---VVIKVLKP-----VKKkKIKREIKILQNLrGGPNIVKLLDVVkdpqSKT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVwIIMELCTLGELRSFLqvrkYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV-SSNDCVKLGDFGLSRY-- 575
Cdd:cd14132     90 PS-LIFEYVNNTDFKTLY----PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIdHEKRKLRLIDWGLAEFyh 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  576 -MED------STYYKaskgklpikwmAPES-INFRRFTSASDVWMFGvCMWEILMHGVKP-FQGVKNNDVIGRI 640
Cdd:cd14132    165 pGQEynvrvaSRYYK-----------GPELlVDYQYYDYSLDMWSLG-CMLASMIFRKEPfFHGHDNYDQLVKI 226
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
420-635 1.24e-13

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: 72.23  E-value: 1.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRErielgrcIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekflQEALTMRQFDHPHIVKLIGVITE-N 498
Cdd:cd14114      4 YDILEE-------LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVR----KEIQIMNQLHHPKLINLHDAFEDdN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS--SNDCVKLGDFGLSRYM 576
Cdd:cd14114     73 EMVLILEFLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHL 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  577 EDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGvKNND 635
Cdd:cd14114    153 DPKESVKVTTGT--AEFAAPEIVEREPVGFYTDMWAVGVLSY-VLLSGLSPFAG-ENDD 207
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
419-677 1.44e-13

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: 1.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  419 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEA-------LTMRQFDHPHIVKL 491
Cdd:cd14004      1 DYTILKE-------MGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKLGTVpleihilDTLNKRSHPNIVKL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  492 IGVItENPV--WIIMELCTLG-ELRSFLQvRKYSLD--LASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 566
Cdd:cd14004     74 LDFF-EDDEfyYLVMEKHGSGmDLFDFIE-RKPNMDekEAKYIFR--QVADAVKHLHDQGIVHRDIKDENVILDGNGTIK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  567 LGDFGLSRYMEDSTYYKASKgklPIKWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNndvigrIENGEr 645
Cdd:cd14004    150 LIDFGSAAYIKSGPFDTFVG---TIDYAAPEVLRGNPYGGKEqDIWALGVLLY-TLVFKENPFYNIEE------ILEAD- 218
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  646 LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14004    219 LRIPYAVSEDLIDLISRMLNRDVGDRPTIEEL 250
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
429-621 1.46e-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: 72.00  E-value: 1.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVH-------------QGIYMSPENPalavaiKTCKNCTSDSVREKFLQEALtmrqfdHPHIVKLIGVI 495
Cdd:cd06652      6 LGKLLGQGAFGRVYlcydadtgrelavKQVQFDPESP------ETSKEVNALECEIQLLKNLL------HERIVQYYGCL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENP---VWIIMELCTLGELRSflQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 571
Cdd:cd06652     74 RDPQertLSIFMEYMPGGSIKD--QLKSYgALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  572 LSRYME----DSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd06652    152 ASKRLQticlSGTGMKSVTGT-PY-WMSPEVISGEGYGRKADIWSVGCTVVEML 203
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
426-678 1.55e-13

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: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 504
Cdd:cd14665      1 RYELVKDIGSGNFGVAR---LMRDKQTKELVAVKYIER--GEKIDENVQREIINHRSLRHPNIVRFKEVIlTPTHLAIVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGEL-RSFLQVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTY 581
Cdd:cd14665     76 EYAAGGELfERICNAGRFSEDEARF--FFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKlPiKWMAPESINFRRFTSA-SDVWMFGVCMWEILMhGVKPFQGVKN----NDVIGRIENGE-RLPMPPNCPPT 655
Cdd:cd14665    154 PKSTVGT-P-AYIAPEVLLKKEYDGKiADVWSCGVTLYVMLV-GAYPFEDPEEprnfRKTIQRILSVQySIPDYVHISPE 230
                          250       260
                   ....*....|....*....|...
gi 1914779978  656 LYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14665    231 CRHLISRIFVADPATRITIPEIR 253
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
427-657 2.05e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 72.87  E-value: 2.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQGIymsPENPALAVAIKTCKNCTSDSVREKF-------------LQEALTMRQFDHPHIVKLIG 493
Cdd:PTZ00024    11 IQKGAHLGEGTYGKVEKAY---DTLTGKIVAIKKVKIIEISNDVTKDrqlvgmcgihfttLRELKIMNEIKHENIMGLVD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 VITE----NPVWIIMElctlGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 569
Cdd:PTZ00024    88 VYVEgdfiNLVMDIMA----SDLKKVVD-RKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIAD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  570 FGLSR------YMEDSTYYKASKGKLPIK------WM-APESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNN 634
Cdd:PTZ00024   163 FGLARrygyppYSDTLSKDETMQRREEMTskvvtlWYrAPELLmGAEKYHFAVDMWSVGCIFAELLTG--KPlFPGENEI 240
                          250       260
                   ....*....|....*....|...
gi 1914779978  635 DVIGRIENGERLPMPPNCPPTLY 657
Cdd:PTZ00024   241 DQLGRIFELLGTPNEDNWPQAKK 263
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
431-671 2.37e-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: 2.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVhqgIYMSPENPALAVAIKTCKN---CTSDSVREKfLQEALTMRQFDHPHIVKL-IGVITENPVWIIMEL 506
Cdd:cd05595      1 KLLGKGTFGKV---ILVREKATGRYYAMKILRKeviIAKDEVAHT-VTESRVLQNTRHPFLTALkYAFQTHDRLCFVMEY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKA 584
Cdd:cd05595     77 ANGGELFFHLsRERVFTEDRARF--YGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgITDGATMKT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd05595    155 FCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPFYNQDHERLFELILM-EEIRFPRTLSPEAKSLLAGLL 230

                   ....*..
gi 1914779978  665 AYDPSRR 671
Cdd:cd05595    231 KKDPKQR 237
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
428-665 2.55e-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: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPAlavAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENP------V 500
Cdd:cd06636     19 ELVEVVGNGTYGQVYKGRHVKTGQLA---AIKV-MDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAfIKKSPpghddqL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQVRKYSLDLASLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd06636     95 WLVMEFCGAGSVTDLVKNTKGNALKEDWIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPP 654
Cdd:cd06636    175 VGRRNTFIGTPY-WMAPEVIACDEnpdatYDYRSDIWSLGITAIE-MAEGAPPLCDMHPMRALFLI--------PRNPPP 244
                          250
                   ....*....|.
gi 1914779978  655 TLYSlmtKCWA 665
Cdd:cd06636    245 KLKS---KKWS 252
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
485-671 3.19e-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: 3.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  485 HPHIVKLIGVI-TENPVWIIMELCTLGELrsFLQVRKYSL---DLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVS 560
Cdd:cd05584     59 HPFIVDLHYAFqTGGKLYLILEYLSGGEL--FMHLEREGIfmeDTACF--YLAEITLALGHLHSLGIIYRDLKPENILLD 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  561 SNDCVKLGDFGLSR-YMEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGR 639
Cdd:cd05584    135 AQGHVKLTDFGLCKeSIHDGTVTHTFCGT--IEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKTIDK 211
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1914779978  640 IENGeRLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05584    212 ILKG-KLNLPPYLTNEARDLLKKLLKRNVSSR 242
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
431-677 4.03e-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: 70.83  E-value: 4.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGiymSPENPALAVAIKTCKNCTSDSVREkFLQEALTMRQF-DHPHIVKLIG--VITENP---VWIIM 504
Cdd:cd13985      6 KQLGEGGFSYVYLA---HDVNTGRRYALKRMYFNDEEQLRV-AIKEIEIMKRLcGHPNIVQYYDsaILSSEGrkeVLLLM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTlGELRSFLQVRKYS-LDLASLILYAYQLSTALAYL--ESKRFVHRDIAARNVLVSSNDCVKLGDFGlSRYMEDSTY 581
Cdd:cd13985     82 EYCP-GSLVDILEKSPPSpLSEEEVLRIFYQICQAVGHLhsQSPPIIHRDIKIENILFSNTGRFKLCDFG-SATTEHYPL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKLPIKWM---------APESIN-FRRF--TSASDVWMFGvCMWEILMHGVKPFQGvknnDVIGRIENGE-RLPM 648
Cdd:cd13985    160 ERAEEVNIIEEEIqknttpmyrAPEMIDlYSKKpiGEKADIWALG-CLLYKLCFFKLPFDE----SSKLAIVAGKySIPE 234
                          250       260
                   ....*....|....*....|....*....
gi 1914779978  649 PPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd13985    235 QPRYSPELHDLIRHMLTPDPAERPDIFQV 263
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
471-684 4.10e-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: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  471 EKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFV 548
Cdd:cd14209     46 EHTLNEKRILQAINFPFLVKLEYSFKDNSnLYMVMEYVPGGEMFSHLRrIGRFSEPHARF--YAAQIVLAFEYLHSLDLI 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKgklPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPF 628
Cdd:cd14209    124 YRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCGT---P-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  629 QGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCWAYDPSRrpRFTELKAQLSTI 684
Cdd:cd14209    199 FADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLTK--RFGNLKNGVNDI 251
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
428-628 4.78e-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: 70.90  E-value: 4.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPAlavAIKTcKNCTSDSvREKFLQEALTMRQFDH-PHIVKLIGV-ITENP------ 499
Cdd:cd06637      9 ELVELVGNGTYGQVYKGRHVKTGQLA---AIKV-MDVTGDE-EEEIKQEINMLKKYSHhRNIATYYGAfIKKNPpgmddq 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRSFLQVRKYSLDLASLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd06637     84 LWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYiCREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  579 STYYKASKGKLPIkWMAPESINFRRFTSA-----SDVWMFGVCMWEiLMHGVKPF 628
Cdd:cd06637    164 TVGRRNTFIGTPY-WMAPEVIACDENPDAtydfkSDLWSLGITAIE-MAEGAPPL 216
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
428-629 5.13e-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: 71.17  E-value: 5.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFgdVHQGIYmSPENPALAVAIKTCKNCTSDSVreKFLQ-EALTMRQFDHPHIVKLIGVITEN-PVWIIME 505
Cdd:cd08216      5 EIGKCFKGGGV--VHLAKH-KPTNTLVAVKKINLESDSKEDL--KFLQqEILTSRQLQHPNILPYVTSFVVDnDLYVVTP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQvRKYSLDLASLILyAYQLS---TALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFglsRYMedstYY 582
Cdd:cd08216     80 LMAYGSCRDLLK-THFPEGLPELAI-AFILRdvlNALEYIHSKGYIHRSVKASHILISGDGKVVLSGL---RYA----YS 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  583 KASKGK-------LPI------KWMAPESI--NFRRFTSASDVWMFGVCMWEiLMHGVKPFQ 629
Cdd:cd08216    151 MVKHGKrqrvvhdFPKsseknlPWLSPEVLqqNLLGYNEKSDIYSVGITACE-LANGVVPFS 211
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
456-621 5.37e-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: 5.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKtcKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKY-SLDLASLI---- 529
Cdd:cd07854     33 VAVK--KIVLTDPQSVKhALREIKIIRRLDHDNIVKVYEVLGPSGSDLTEDVGSLTELNSVYIVQEYmETDLANVLeqgp 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  530 -------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KLGDFGLSRYMeDSTYykASKGKLP----IKWM-AP 596
Cdd:cd07854    111 lseeharLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARIV-DPHY--SHKGYLSeglvTKWYrSP 187
                          170       180
                   ....*....|....*....|....*.
gi 1914779978  597 ESI-NFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd07854    188 RLLlSPNNYTKAIDMWAAGCIFAEML 213
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
433-620 5.54e-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: 5.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymspeNPALAVAIKTCKNCT---SDSVREKFLQEALTMRQFDHPHIVKLIG-----VITENPVWIIM 504
Cdd:cd14033      9 IGRGSFKTVYRGL-----DTETTVEVAWCELQTrklSKGERQRFSEEVEMLKGLQHPNIVRFYDswkstVRGHKCIILVT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS-NDCVKLGDFGLSrymedsTY 581
Cdd:cd14033     84 ELMTSGTLKTYLK-RFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLA------TL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  582 YKASKGKLPI---KWMAPESINfRRFTSASDVWMFGVCMWEI 620
Cdd:cd14033    157 KRASFAKSVIgtpEFMAPEMYE-EKYDEAVDVYAFGMCILEM 197
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
470-628 6.55e-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: 70.78  E-value: 6.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRF 547
Cdd:cd06659     62 RELLFNEVVIMRDYQHPNVVEMYkSYLVGEELWVLMEYLQGGALTDIVsQTRLNEEQIATVCEAVLQ---ALAYLHSQGV 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKP 627
Cdd:cd06659    139 IHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIE-MVDGEPP 216

                   .
gi 1914779978  628 F 628
Cdd:cd06659    217 Y 217
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
428-635 6.98e-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: 6.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRcigeGQFGDVHQGIYMSPENPALAVAIKT---CKNCTSDSVREKFLQEALTmrqfDHPHIVKLIGVI-TENPVWII 503
Cdd:cd14198     15 ELGR----GKFAVVRQCISKSTGQEYAAKFLKKrrrGQDCRAEILHEIAVLELAK----SNPRVVNLHEVYeTTSEIILI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSF----LQVRKYSLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSS----NDcVKLGDFGLSRY 575
Cdd:cd14198     87 LEYAAGGEIFNLcvpdLAEMVSENDIIRLI---RQILEGVYYLHQNNIVHLDLKPQNILLSSiyplGD-IKIVDFGMSRK 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNND 635
Cdd:cd14198    163 IGHACELREIMGT--PEYLAPEILNYDPITTATDMWNIGVIAY-MLLTHESPFVGEDNQE 219
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-628 7.21e-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: 7.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 502
Cdd:cd14167      2 RDIYDFREVLGTGAFSEV---VLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYeSGGHLYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGEL------RSFLQVRkyslDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLS 573
Cdd:cd14167     79 IMQLVSGGELfdriveKGFYTER----DASKLI---FQILDAVKYLHDMGIVHRDLKPENLLYYSLDedsKIMISDFGLS 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  574 RyMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14167    152 K-IEGSGSVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 203
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
428-671 7.24e-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: 7.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQ-FDH----PHIVKL-IGVITENPVW 501
Cdd:cd05614      3 ELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQ-KAKTVEHTRTERNvLEHvrqsPFLVTLhYAFQTDAKLH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM----E 577
Cdd:cd05614     82 LILDYVSGGELFTHLYQRDH-FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFlteeK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKgklpIKWMAPESINFRR-FTSASDVWMFGVCMWEILMhGVKPF--QGVKNN--DVIGRIENGERlPMPPNC 652
Cdd:cd05614    161 ERTYSFCGT----IEYMAPEIIRGKSgHGKAVDWWSLGILMFELLT-GASPFtlEGEKNTqsEVSRRILKCDP-PFPSFI 234
                          250
                   ....*....|....*....
gi 1914779978  653 PPTLYSLMTKCWAYDPSRR 671
Cdd:cd05614    235 GPVARDLLQKLLCKDPKKR 253
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
433-671 8.27e-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: 70.14  E-value: 8.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmspENPALAVAIKTCK------NCTSDSVREKFLqealtMRQFDHPHIVKLIGVI-TENPVWIIME 505
Cdd:cd07861      8 IGEGTYGVVYKGRN---KKTGQIVAMKKIRleseeeGVPSTAIREISL-----LKELQHPNIVCLEDVLmQENRLYLVFE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLgELRSFLQ---VRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMedstyy 582
Cdd:cd07861     80 FLSM-DLKKYLDslpKGKY-MDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF------ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 kaskgKLPIK----------WMAPESI-NFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRI---------- 640
Cdd:cd07861    152 -----GIPVRvythevvtlwYRAPEVLlGSPRYSTPVDIWSIGTIFAE--MATKKPlFHGDSEIDQLFRIfrilgtpted 224
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  641 --ENGERLP----------------MPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd07861    225 iwPGVTSLPdykntfpkwkkgslrtAVKNLDEDGLDLLEKMLIYDPAKR 273
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
431-671 9.81e-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: 9.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVhqgIYMSPENPALAVAIKTC-KNCTSDSVREKFL--QEALTMRQFDHPHIVKL-IGVITENPVWIIMEL 506
Cdd:cd05604      2 KVIGKGSFGKV---LLAKRKRDGKYYAVKVLqKKVILNRKEQKHImaERNVLLKNVKHPFLVGLhYSFQTTDKLYFVLDF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQVRKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd05604     79 VNGGELFFHLQRERSFPEPRAR-FYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQgvkNNDVIGRIEN--GERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd05604    158 CGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFY---CRDTAEMYENilHKPLVLRPGISLTAWSILEELL 232

                   ....*..
gi 1914779978  665 AYDPSRR 671
Cdd:cd05604    233 EKDRQLR 239
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
433-672 1.13e-12

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: 69.61  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDS------VREKFLQEALTmrQFDHPHIVKLIGVI------TENPV 500
Cdd:cd07838      7 IGEGAYGTVYKARDLQDGR---FVALKKVRVPLSEEgiplstIREIALLKQLE--SFEHPNVVRLLDVChgprtdRELKL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTlGELRSFLQ-VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMED 578
Cdd:cd07838     82 TLVFEHVD-QDLATYLDkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARiYSFE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 ST--------YYKaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRI--------- 640
Cdd:cd07838    161 MAltsvvvtlWYR-----------APEVLLQSSYATPVDMWSVGCIFAE--LFNRRPlFRGSSEADQLGKIfdviglpse 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  641 --------------ENGERLPM----PPNCPPTLySLMTKCWAYDPSRRP 672
Cdd:cd07838    228 eewprnsalprssfPSYTPRPFksfvPEIDEEGL-DLLKKMLTFNPHKRI 276
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
433-621 1.27e-12

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: 69.85  E-value: 1.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTS---DSVREKFLQEALTMRQFDHPHIVKLIGVITENP----VWIIME 505
Cdd:cd14159      1 IGEGGFGCVYQAVMRNTE-----YAVKRLKEDSEldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGnyclIYVYLP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLgELRSFLQVRKYSLDLASLILYAYQLSTALAYL--ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM------- 576
Cdd:cd14159     76 NGSL-EDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSrrpkqpg 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  577 EDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd14159    155 MSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELL 199
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
431-681 1.37e-12

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: 70.43  E-value: 1.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENpALAVAIKTCKNCTSDSVREKFLQEA-LTMRQFDHPHIVKL-IGVITENPVWIIMELCT 508
Cdd:cd05602     13 KVIGKGSFGKVLLARHKSDEK-FYAVKVLQKKAILKKKEEKHIMSERnVLLKNVKHPFLVGLhFSFQTTDKLYFVLDYIN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd05602     92 GGELFYHLQRERCFLEPRAR-FYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTSTFCG 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05602    171 TP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMYDNILN-KPLQLKPNITNSARHLLEGLLQKDR 247
                          250
                   ....*....|....*..
gi 1914779978  669 SRR----PRFTELKAQL 681
Cdd:cd05602    248 TKRlgakDDFTEIKNHI 264
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
431-671 1.43e-12

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: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGiYMSPENPALAV-AIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCT 508
Cdd:cd05620      1 KVLGKGSFGKVLLA-ELKGKGEYFAVkALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFqTKEHLFFVMEFLN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR---YMEDstyyKAS 585
Cdd:cd05620     80 GGDLMFHIQ-DKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKenvFGDN----RAS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErlpmpPNCPPTLY----SLMT 661
Cdd:cd05620    155 TFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLI-GQSPFHGDDEDELFESIRVDT-----PHYPRWITkeskDILE 228
                          250
                   ....*....|
gi 1914779978  662 KCWAYDPSRR 671
Cdd:cd05620    229 KLFERDPTRR 238
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
433-671 1.50e-12

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: 69.91  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQgiyMSPENPALAVAIKTCKNC--TSDSVREKFLQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTL 509
Cdd:cd05585      2 IGKGSFGKVMQ---VRKKDTSRIYALKTIRKAhiVSRSEVTHTLAERTVLAQVDCPFIVPLkFSFQSPEKLYLVLAFING 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKASKGK 588
Cdd:cd05585     79 GELFHHLQ-REGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLnMKDDDKTNTFCGT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 lPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05585    158 -P-EYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPFYDENTNEMYRKILQ-EPLRFPDGFDRDAKDLLIGLLNRDP 233

                   ...
gi 1914779978  669 SRR 671
Cdd:cd05585    234 TKR 236
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
432-630 1.51e-12

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: 70.01  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  432 CIGEGQFGDVHQGiYMSPENPALAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP---VWIIMEL 506
Cdd:cd07842      7 CIGRGTYGRVYKA-KRKNGKDGKEYAIKKFKgdKEQYTGISQSACREIALLRELKHENVVSLVEVFLEHAdksVYLLFDY 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CT--LGEL----RSFLQVRKYSLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYm 576
Cdd:cd07842     86 AEhdLWQIikfhRQAKRVSIPPSMVKSLL---WQILNGIHYLHSNWVLHRDLKPANILVMGEGpergVVKIGDLGLARL- 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  577 edstYYKASKGKL-------PIKWMAPESI-NFRRFTSASDVWMFGvCMWEILMHGVKPFQG 630
Cdd:cd07842    162 ----FNAPLKPLAdldpvvvTIWYRAPELLlGARHYTKAIDIWAIG-CIFAELLTLEPIFKG 218
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
433-633 1.53e-12

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: 1.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLgE 511
Cdd:cd07870      8 LGEGSYATVYKGI--SRINGQL-VALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIhTKETLTFVFEYMHT-D 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYKASKGKLp 590
Cdd:cd07870     84 LAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSiPSQTYSSEVVTL- 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  591 ikWMAPESI--NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKN 633
Cdd:cd07870    163 --WYRPPDVllGATDYSSALDIWGAG-CIFIEMLQGQPAFPGVSD 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
429-628 1.63e-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: 69.70  E-value: 1.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRcIGEGQFGDVHQGIYMSPENpalAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN---PVWIIM 504
Cdd:cd07845     12 LNR-IGEGTYGIVYRARDTTSGE---IVALKKVRmDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKhldSIFLVM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDStyYKA 584
Cdd:cd07845     88 EYCE-QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLP--AKP 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1914779978  585 SKGKLPIKWM-APESI-NFRRFTSASDVWMFGVCMWEILMHgvKPF 628
Cdd:cd07845    165 MTPKVVTLWYrAPELLlGCTTYTTAIDMWAVGCILAELLAH--KPL 208
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
428-671 1.78e-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: 1.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQ-FDH----PHIVKL-IGVITENPVW 501
Cdd:cd05613      3 ELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQ-KAKTAEHTRTERQvLEHirqsPFLVTLhYAFQTDTKLH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd05613     82 LILDYINGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKLPIKWMAPESINF--RRFTSASDVWMFGVCMWEILMhGVKPF--QGVKNN--DVIGRIENGERlPMPPNCPPT 655
Cdd:cd05613    161 ERAYSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELLT-GASPFtvDGEKNSqaEISRRILKSEP-PYPQEMSAL 238
                          250
                   ....*....|....*.
gi 1914779978  656 LYSLMTKCWAYDPSRR 671
Cdd:cd05613    239 AKDIIQRLLMKDPKKR 254
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
433-672 3.50e-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: 68.37  E-value: 3.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd06619      9 LGHGNGGTVYKAYHLLTRR---ILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFfVENRISICTEFMDGGS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLAslilyAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS---TYYKASkgk 588
Cdd:cd06619     86 LDVYRKIPEHVLGRI-----AVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSiakTYVGTN--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 lpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNdvigrieNGERLPM----------PPNCPPTLYS 658
Cdd:cd06619    158 ---AYMAPERISGEQYGIHSDVWSLGISFMELAL-GRFPYPQIQKN-------QGSLMPLqllqcivdedPPVLPVGQFS 226
                          250
                   ....*....|....*....
gi 1914779978  659 -----LMTKCWAYDPSRRP 672
Cdd:cd06619    227 ekfvhFITQCMRKQPKERP 245
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
425-671 4.04e-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: 68.09  E-value: 4.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCK------NCTSDSVRE-KFLQEaltMRqfdHPHIVKLIGVI-T 496
Cdd:cd07835      2 QKLEK---IGEGTYGVVYKARDKLTGE---IVALKKIRletedeGVPSTAIREiSLLKE---LN---HPNIVRLLDVVhS 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLgELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 575
Cdd:cd07835     70 ENKLYLVFEFLDL-DLKKYMdSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MedstyykaskgKLPIK---------WM-APES-INFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGRI--- 640
Cdd:cd07835    149 F-----------GVPVRtythevvtlWYrAPEIlLGSKHYSTPVDIWSVGCIFAEMVTR--RPlFPGDSEIDQLFRIfrt 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  641 ----------------------ENGERLPMP---PNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd07835    216 lgtpdedvwpgvtslpdykptfPKWARQDLSkvvPSLDEDGLDLLSQMLVYDPAKR 271
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
428-644 4.40e-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: 67.96  E-value: 4.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRcigeGQFGDVHQGIYMSPENPALAVAIKtCKncTSDSVREKflQEALTMRQFDHPHIVKLIGVItENPVWIIM--E 505
Cdd:cd14104      7 ELGR----GQFGIVHRCVETSSKKTYMAKFVK-VK--GADQVLVK--KEISILNIARHRNILRLHESF-ESHEELVMifE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL----VSSNdcVKLGDFGLSRYMEDSTY 581
Cdd:cd14104     77 FISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyctrRGSY--IKIIEFGQSRQLKPGDK 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  582 YKASKgkLPIKWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIENGE 644
Cdd:cd14104    155 FRLQY--TSAEFYAPEVHQHESVSTATDMWSLG-CLVYVLLSGINPFEAETNQQTIENIRNAE 214
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
429-671 4.90e-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: 4.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  429 LGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELC 507
Cdd:cd05619      9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFqTKENLFFVMEYL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymeDSTYYKASKG 587
Cdd:cd05619     89 NGGDLMFHIQ-SCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK---ENMLGDAKTS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErlPMPPN-CPPTLYSLMTKCW 664
Cdd:cd05619    165 TFcgTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLI-GQSPFHGQDEEELFQSIRMDN--PFYPRwLEKEAKDILVKLF 241

                   ....*..
gi 1914779978  665 AYDPSRR 671
Cdd:cd05619    242 VREPERR 248
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
470-628 5.17e-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: 5.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFV 548
Cdd:cd14113     47 RDQVTHELGVLQSLQHPQLVGLLDTFeTPTSYILVLEMADQGRLLDYV-VRWGNLTEEKIRFYLREILEALQYLHNCRIA 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLV---SSNDCVKLGDFGLSRYMeDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGV 625
Cdd:cd14113    126 HLDLKPENILVdqsLSKPTIKLADFGDAVQL-NTTYYIHQLLGSP-EFAAPEIILGNPVSLTSDLWSIGVLTY-VLLSGV 202

                   ...
gi 1914779978  626 KPF 628
Cdd:cd14113    203 SPF 205
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
143-248 5.29e-12

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 63.83  E-value: 5.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  143 TLNFFYQQVKSDYMLEIADqVDQEIALKLGCLEIRRSYwemrGNALEKKSNYEVLekdvGLKRFFPKSLLDSVKAKTLRK 222
Cdd:pfam00373   11 TRHLLYLQAKDDILEGRLP-CSEEEALLLAALQLQAEF----GDYQPSSHTSEYL----SLESFLPKQLLRKMKSKELEK 81
                           90       100
                   ....*....|....*....|....*.
gi 1914779978  223 LIQQTFRQFANLNREESILKFFEILS 248
Cdd:pfam00373   82 RVLEAHKNLRGLSAEEAKLKYLQIAQ 107
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
433-667 5.66e-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: 67.90  E-value: 5.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE----NPVwIIMELCT 508
Cdd:cd13988      1 LGQGATANVFRGRH---KKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEElttrHKV-LVMELCP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQ--VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CV-KLGDFGLSRYMEDSTYY 582
Cdd:cd13988     77 CGSLYTVLEepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEdgqSVyKLTDFGAARELEDDEQF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKLpiKWMAP---ESINFRR-----FTSASDVWMFGVCMWEILMhGVKPFQ----GVKNNDVIGRI---------- 640
Cdd:cd13988    157 VSLYGTE--EYLHPdmyERAVLRKdhqkkYGATVDLWSIGVTFYHAAT-GSLPFRpfegPRRNKEVMYKIitgkpsgais 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  641 -----ENGE---RLPMPPNCPPT--LYSLMT------------KCWAYD 667
Cdd:cd13988    234 gvqksENGPiewSGELPVSCSLSqgLQTLLTpvlanileadqeKCWGFD 282
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
431-671 5.77e-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: 5.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVhqgiymspenpaLAVAIKT------CKNCTSDSVREK-----FLQEALTMRQFDHPHIVKLI-GVITEN 498
Cdd:cd05630      6 RVLGKGGFGEV------------CACQVRAtgkmyaCKKLEKKRIKKRkgeamALNEKQILEKVNSRFVVSLAyAYETKD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05630     74 ALCLVLTLMNGGDLKFHIyHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNdvIGRiENGERL------PMPPN 651
Cdd:cd05630    154 EGQTIKGRVGT--VGYMAPEVVKNERYTFSPDWWALGCLLYE-MIAGQSPFQQRKKK--IKR-EEVERLvkevpeEYSEK 227
                          250       260
                   ....*....|....*....|
gi 1914779978  652 CPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05630    228 FSPQARSLCSMLLCKDPAER 247
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-644 5.90e-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: 5.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNctSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVW 501
Cdd:cd14166      2 RETFIFMEVLGSGAFSEVY---LVKQRSTGKLYALKCIKK--SPLSRDSSLEnEIAVLKRIKHENIVTLEDIYeSTTHYY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRyME 577
Cdd:cd14166     77 LVMQLVSGGELfDRILERGVYTEKDASRVIN--QVLSAVKYLHENGIVHRDLKPENLLYLTpdeNSKIMITDFGLSK-ME 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  578 DSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE 644
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 ...
418-649 6.73e-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: 6.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  418 RDYEIQRERIELGRCIGEGQFGDVHQgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKL-IGVIT 496
Cdd:cd05624     65 KEMQLHRDDFEIIKVIGRGAFGEVAV-VKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLhYAFQD 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  497 ENPVWIIMELCTLGELRSFLQVRKYSL--DLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd05624    144 ENYLYLVMDYYVGGDLLTLLSKFEDKLpeDMARF--YIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCL 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YMEDSTYYKASKGKLPIKWMAPESIN-----FRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENG-ERLPM 648
Cdd:cd05624    222 KMNDDGTVQSSVAVGTPDYISPEILQamedgMGKYGPECDWWSLGVCMYEML-YGETPFYAESLVETYGKIMNHeERFQF 300

                   .
gi 1914779978  649 P 649
Cdd:cd05624    301 P 301
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
433-628 7.25e-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: 67.37  E-value: 7.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVhqgIYMSPENPALAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGE 511
Cdd:cd06658     30 IGEGSTGIV---CIATEKHTGKQVAVKK-MDLRKQQRRELLFNEVVIMRDYHHENVVDMYnSYLVGDELWVVMEFLEGGA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLP 590
Cdd:cd06658    106 LTDIVtHTRMNEEQIATVCLSVLR---ALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTP 182
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1914779978  591 IkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPF 628
Cdd:cd06658    183 Y-WMAPEVISRLPYGTEVDIWSLGIMVIE-MIDGEPPY 218
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
533-672 7.70e-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: 67.35  E-value: 7.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  533 YQLSTALAYL-ESKRFVHRDIAARNVLVSSNDCVKLGDFGlsrYMEDST-------YYKASKGKLPI------KWMAPES 598
Cdd:cd14011    121 LQISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFD---FCISSEqatdqfpYFREYDPNLPPlaqpnlNYLAPEY 197
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  599 INFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKN---NDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd14011    198 ILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNllsYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRP 274
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
496-671 8.45e-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: 8.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd05616     72 TMDRLYFVMEYVNGGDLMYHIQqVGRFKEPHA--VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 Y-MEDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLP--MPP 650
Cdd:cd05616    150 EnIWDGVTTKTFCGT-P-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSImEHNVAYPksMSK 226
                          170       180
                   ....*....|....*....|.
gi 1914779978  651 NCPPTLYSLMTKcwayDPSRR 671
Cdd:cd05616    227 EAVAICKGLMTK----HPGKR 243
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
456-684 8.70e-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: 66.83  E-value: 8.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKTCKNcTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGELRSFLQvRKYS------LDLASL 528
Cdd:cd14044     34 VILKDLKN-NEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKlDTMIFGVIEYCERGSLRDVLN-DKISypdgtfMDWEFK 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  529 ILYAYQLSTALAYLE-SKRFVHRDIAARNVLVSSNDCVKLGDFGlsrymedstyykaSKGKLPIK---WMAPESINFRRF 604
Cdd:cd14044    112 ISVMYDIAKGMSYLHsSKTEVHGRLKSTNCVVDSRMVVKITDFG-------------CNSILPPSkdlWTAPEHLRQAGT 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  605 TSASDVWMFGVCMWEILMHGVKPF--QGVKNNDVIGRIENGERL-PMPPNC--------PPTLYSLMTKCWAYDPSRRPR 673
Cdd:cd14044    179 SQKGDVYSYGIIAQEIILRKETFYtaACSDRKEKIYRVQNPKGMkPFRPDLnlesagerEREVYGLVKNCWEEDPEKRPD 258
                          250
                   ....*....|.
gi 1914779978  674 FTELKAQLSTI 684
Cdd:cd14044    259 FKKIENTLAKI 269
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
433-679 9.20e-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: 67.98  E-value: 9.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiymSPENPALAVAIKTCKNctSDSVREKFLQEALTMRQF----DHPHIVKLI-GVITENPVWIIMELC 507
Cdd:cd05610     12 ISRGAFGKVYLG---RKKNNSKLYAVKVVKK--ADMINKNMVHQVQAERDAlalsKSPFIVHLYySLQSANNVYLVMEYL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-------MED-- 578
Cdd:cd05610     87 IGGDVKSLLHIYGY-FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVtlnrelnMMDil 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 ------------------------------STYYKASK----GKLPIK---------WMAPESINFRRFTSASDVWMFGV 615
Cdd:cd05610    166 ttpsmakpkndysrtpgqvlslisslgfntPTPYRTPKsvrrGAARVEgerilgtpdYLAPELLLGKPHGPAVDWWALGV 245
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  616 CMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPP-------NCPPTLYSLMTkcwaYDPSRRPRFTELKA 679
Cdd:cd05610    246 CLFEFLT-GIPPFNDETPQQVFQNILNRD-IPWPEgeeelsvNAQNAIEILLT----MDPTKRAGLKELKQ 310
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
470-677 1.15e-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: 66.97  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRF 547
Cdd:cd06657     61 RELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVMEFLEGGALTDIVtHTRMNEEQIAAVCLAVLK---ALSVLHAQGV 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKP 627
Cdd:cd06657    138 IHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPP 215
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  628 FQGVKNNDVIGRIENG--ERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd06657    216 YFNEPPLKAMKMIRDNlpPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAEL 267
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
470-643 1.20e-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: 66.09  E-value: 1.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  470 REKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFV 548
Cdd:cd14110     43 KQLVLREYQVLRRLSHPRIAQLHSAYlSPRHLVLIEELCSGPELLYNLAERN-SYSEAEVTDYLWQILSAVDYLHSRRIL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  549 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14110    122 HLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAF-IMLSADYPV 200
                          170
                   ....*....|....*
gi 1914779978  629 QGVKNNDVIGRIENG 643
Cdd:cd14110    201 SSDLNWERDRNIRKG 215
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
485-644 1.56e-11

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 66.55  E-value: 1.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  485 HPHIVKLIGVIT-ENPVWIIMELCTLGELrsFLQVRK---YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVS 560
Cdd:cd14092     58 HPNIVKLHEVFQdELHTYLVMELLRGGEL--LERIRKkkrFTESEASRIMR--QLVSAVSFMHSKGVVHRDLKPENLLFT 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  561 SND---CVKLGDFGLSRYMEDSTYYKASKGKLPikWMAPE----SINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKN 633
Cdd:cd14092    134 DEDddaEIKIVDFGFARLKPENQPLKTPCFTLP--YAAPEvlkqALSTQGYDESCDLWSLGVILYTML-SGQVPFQSPSR 210
                          170
                   ....*....|....*
gi 1914779978  634 N----DVIGRIENGE 644
Cdd:cd14092    211 NesaaEIMKRIKSGD 225
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
432-671 1.58e-11

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 67.01  E-value: 1.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  432 CIGEGQFGdvhqgIYMSPENPAL--AVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITE------NPVWI 502
Cdd:cd07858     12 PIGRGAYG-----IVCSAKNSETneKVAIKKIANAFDNRIDAKrTLREIKLLRHLDHENVIAIKDIMPPphreafNDVYI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELctlgelrsflqvrkYSLDLASLI------------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDF 570
Cdd:cd07858     87 VYEL--------------MDTDLHQIIrssqtlsddhcqYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDF 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  571 GLSRYMEDS----TYYKASKgklpiKWMAPESI-NFRRFTSASDVWMFGVCMWEILmhGVKP-FQ--------------- 629
Cdd:cd07858    153 GLARTTSEKgdfmTEYVVTR-----WYRAPELLlNCSEYTTAIDVWSVGCIFAELL--GRKPlFPgkdyvhqlklitell 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  630 GVKNNDVIGRIENG------ERLP---------MPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd07858    226 GSPSEEDLGFIRNEkarryiRSLPytprqsfarLFPHANPLAIDLLEKMLVFDPSKR 282
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
433-640 1.60e-11

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: 66.30  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiymSPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlG 510
Cdd:cd07839      8 IGEGTYGTVFKA---KNRETHEIVALKRVRLDDDDEgVPSSALREICLLKELKHKNIVRLYDVLhSDKKLTLVFEYCD-Q 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKL 589
Cdd:cd07839     84 DLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARaFGIPVRCYSAEVVTL 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  590 pikWMAPESINF--RRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI 640
Cdd:cd07839    164 ---WYRPPDVLFgaKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRI 213
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
437-644 1.72e-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: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  437 QFGDVhqgiYMSPENPALAvAIKTCKNCT-------------SDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWI 502
Cdd:cd14177      1 QFTDV----YELKEDIGVG-SYSVCKRCIhratnmefavkiiDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRyVYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMe 577
Cdd:cd14177     76 VTELMKGGELlDRILRQKFFSEREASAVLYT--ITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQL- 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  578 dstyyKASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN---DVIGRIENGE 644
Cdd:cd14177    153 -----RGENGLLltpcyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFANGPNDtpeEILLRIGSGK 221
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
425-679 1.77e-11

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 66.92  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCtsDSVREK----FLQEALTMRQFDHPHIVKLigVIT---E 497
Cdd:cd05573      1 DDFEVIKVIGRGAFGEVWLVRDKDTGQV---YAMKILRKS--DMLKREqiahVRAERDILADADSPWIVRL--HYAfqdE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05573     74 DHLYLVMEYMPGGDLMNLL-IKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMN 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DS--TYYKASKGKLPIK--------------------------WMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQ 629
Cdd:cd05573    153 KSgdRESYLNDSVNTLFqdnvlarrrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEML-YGFPPFY 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  630 GVKNNDVIGRIENGE---RLPMPPNCPPTLYSLMTKCWAyDPSRR-PRFTELKA 679
Cdd:cd05573    232 SDSLVETYSKIMNWKeslVFPDDPDVSPEAIDLIRRLLC-DPEDRlGSAEEIKA 284
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
433-629 2.22e-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: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCKncTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 511
Cdd:cd14087      9 IGRGSFSRVVRVEHRVTRQP---YAIKMIE--TKCRGREVCESELNVLRRVRHTNIIQLIEVFeTKERVYMVMELATGGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVR-KYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLV--SSNDC-VKLGDFGLS--RYMEDSTYYKAS 585
Cdd:cd14087     84 LFDRIIAKgSFTERDATRVL--QMVLDGVKYLHGLGITHRDLKPENLLYyhPGPDSkIMITDFGLAstRKKGPNCLMKTT 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1914779978  586 KGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQ 629
Cdd:cd14087    162 CGT-P-EYIAPEILLRKPYTQSVDMWAVGVIAY-ILLSGTMPFD 202
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
433-653 2.27e-11

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 65.98  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymsPENPALAVAIKTCKnctSDSVREKF----LQEALTMRQFDHPHIVKLIGVITENpvwiIMELCT 508
Cdd:cd07864     15 IGEGTYGQVYKAK---DKDTGELVALKKVR---LDNEKEGFpitaIREIKILRQLNHRSVVNLKEIVTDK----QDALDF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKY-SLDLASLI-------------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd07864     85 KKDKGAFYLVFEYmDHDLMGLLesglvhfsedhikSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLAR 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 YM--EDSTYYkasKGKLPIKWMAPESINF--RRFTSASDVWMFGVCMWEILMHgvKP-FQGvknNDVIGRIENGERL--- 646
Cdd:cd07864    165 LYnsEESRPY---TNKVITLWYRPPELLLgeERYGPAIDVWSCGCILGELFTK--KPiFQA---NQELAQLELISRLcgs 236

                   ....*..
gi 1914779978  647 PMPPNCP 653
Cdd:cd07864    237 PCPAVWP 243
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
433-680 3.45e-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: 65.24  E-value: 3.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHqGIYMSPENPALAvaiktCKNCTSDSVREK-----FLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd05577      1 LGRGGFGEVC-ACQVKATGKMYA-----CKKLDKKRIKKKkgetmALNEKIILEKVSSPFIVSLAYAFeTKDKLCLVLTL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 585
Cdd:cd05577     75 MNGGDLKYHIyNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKlpIKWMAPESI-NFRRFTSASDVWMFGVCMWEiLMHGVKPFQ----GVKNNDVIGRIENGErLPMPPNCPPTLYSLM 660
Cdd:cd05577    155 VGT--HGYMAPEVLqKEVAYDFSVDWFALGCMLYE-MIAGRSPFRqrkeKVDKEELKRRTLEMA-VEYPDSFSPEARSLC 230
                          250       260
                   ....*....|....*....|
gi 1914779978  661 TKCWAYDPSRRPRFTELKAQ 680
Cdd:cd05577    231 EGLLQKDPERRLGCRGGSAD 250
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
407-635 4.64e-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: 65.82  E-value: 4.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  407 MPSKSYGIDEARDYEIQRERIELGRCIGEGQfgdvhQGIYMSPENPALAVAI---KTCKNCTSDSVREKFLQEALTMRQF 483
Cdd:cd07876      3 EDSQFYSVQVADSTFTVLKRYQQLKPIGSGA-----QGIVCAAFDTVLGINVavkKLSRPFQNQTHAKRAYRELVLLKCV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  484 DHPHIVKLIGVITENP-------VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARN 556
Cdd:cd07876     78 NHKNIISLLNVFTPQKsleefqdVYLVMELMD----ANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  557 VLVSSNDCVKLGDFGLSRYMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNND 635
Cdd:cd07876    154 IVVKSDCTLKILDFGLARTA--CTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGE-LVKGSVIFQGTDHID 229
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
461-629 4.90e-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: 4.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  461 CKNCTSDSVREKFL-------QEALTMRQF-------DHPHIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-YSLD 524
Cdd:cd14179     23 CRKCLHKKTNQEYAvkivskrMEANTQREIaalklceGHPNIVKLHEVYHDQlHTFLVMELLKGGELLERIKKKQhFSET 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  525 LASLILYayQLSTALAYLESKRFVHRDIAARNVLV---SSNDCVKLGDFGLSRYME-DSTYYKASKgkLPIKWMAPESIN 600
Cdd:cd14179    103 EASHIMR--KLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPpDNQPLKTPC--FTLHYAAPELLN 178
                          170       180
                   ....*....|....*....|....*....
gi 1914779978  601 FRRFTSASDVWMFGVCMWEILmHGVKPFQ 629
Cdd:cd14179    179 YNGYDESCDLWSLGVILYTML-SGQVPFQ 206
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
425-688 4.99e-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: 4.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-----GVITEN 498
Cdd:cd14219      5 KQIQMVKQIGKGRYGEVWMGKWRGEK-----VAVKVFFTTEEASwFRETEIYQTVLMR---HENILGFIaadikGTGSWT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDF 570
Cdd:cd14219     77 QLYLITDYHENGSLYDYL--KSTTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNILVKKNGTCCIADL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  571 GLS-RYMEDStyykaSKGKLPI-------KWMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK---------P 627
Cdd:cd14219    155 GLAvKFISDT-----NEVDIPPntrvgtkRYMPPEvldeSLNRNHFQSyiMADMYSFGLILWEVARRCVSggiveeyqlP 229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  628 FQGVKNND----------VIGRIEngerlPMPPN------CPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEE 688
Cdd:cd14219    230 YHDLVPSDpsyedmreivCIKRLR-----PSFPNrwssdeCLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQ 301
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
433-673 5.08e-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: 64.21  E-value: 5.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTS---DSVRE-KFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELc 507
Cdd:cd14133      7 LGKGTFGQVVKCYDLLTGE---EVALKIIKNNKDyldQSLDEiRLLELLNKKDKADKYHIVRLKDVFYfKNHLCIVFEL- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 tLGE-LRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND-C-VKLGDFGLSRYMED----- 578
Cdd:cd14133     83 -LSQnLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrCqIKIIDFGSSCFLTQrlysy 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  579 --STYYKaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE------NGERLPMPP 650
Cdd:cd14133    162 iqSRYYR-----------APEVILGLPYDEKIDMWSLGCILAELYT-GEPLFPGASEVDQLARIIgtigipPAHMLDQGK 229
                          250       260
                   ....*....|....*....|...
gi 1914779978  651 NCPPTLYSLMTKCWAYDPSRRPR 673
Cdd:cd14133    230 ADDELFVDFLKKLLEIDPKERPT 252
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
430-621 5.19e-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: 64.72  E-value: 5.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVH-------------QGIYMSPENPALAVAIKTCKnCtsdsvrekflqEALTMRQFDHPHIVKLIGVI- 495
Cdd:cd06651     12 GKLLGQGAFGRVYlcydvdtgrelaaKQVQFDPESPETSKEVSALE-C-----------EIQLLKNLQHERIVQYYGCLr 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 --TENPVWIIMELCTLGELRSflQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd06651     80 drAEKTLTIFMEYMPGGSVKD--QLKAYGALTESVTRkYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  573 SRYMEdsTYYKASKGKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd06651    158 SKRLQ--TICMSGTGIRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEML 208
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
428-628 5.24e-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: 5.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVhqgIYMSPENPALAVAIKtCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGvITENP--VWIIM 504
Cdd:cd14169      6 ELKEKLGEGAFSEV---VLAQERGSQRLVALK-CIPKKALRGKEAMVEnEIAVLRRINHENIVSLED-IYESPthLYLAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRKY--SLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRyMEDS 579
Cdd:cd14169     81 ELVTGGELFDRIIERGSytEKDASQLI---GQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK-IEAQ 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  580 TYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14169    157 GMLSTACGT-P-GYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPF 202
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
416-649 5.52e-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: 65.81  E-value: 5.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  416 EARDYEIQRERIELGRCIGEGQFGDVHQgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKL-IGV 494
Cdd:cd05623     63 KVKQMRLHKEDFEILKVIGRGAFGEVAV-VKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLhYAF 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  495 ITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS- 573
Cdd:cd05623    142 QDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCl 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  574 RYMEDSTYYKASKGKLPiKWMAPESINFR-----RFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIEN-GERLP 647
Cdd:cd05623    222 KLMEDGTVQSSVAVGTP-DYISPEILQAMedgkgKYGPECDWWSLGVCMYEML-YGETPFYAESLVETYGKIMNhKERFQ 299

                   ..
gi 1914779978  648 MP 649
Cdd:cd05623    300 FP 301
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
433-620 6.50e-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: 6.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlGE 511
Cdd:cd07873     10 LGEGTYATVYKGRSKLTDN---LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIhTEKSLTLVFEYLD-KD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyyKASKGKLPI 591
Cdd:cd07873     86 LKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPT--KTYSNEVVT 163
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1914779978  592 KWMAPESI--NFRRFTSASDVWMFGVCMWEI 620
Cdd:cd07873    164 LWYRPPDIllGSTDYSTQIDMWGVGCIFYEM 194
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
459-620 6.75e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 65.40  E-value: 6.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  459 KTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLST 537
Cdd:PHA03212   115 KTCEHVVIKAgQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKR-NIAICDILAIERSVLR 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  538 ALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCM 617
Cdd:PHA03212   194 AIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVL 273

                   ...
gi 1914779978  618 WEI 620
Cdd:PHA03212   274 FEM 276
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
433-661 7.02e-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: 7.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymsPENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITE-------NPVWIIM 504
Cdd:cd07877     25 VGSGAYGSVCAAF---DTKTGLRVAVKKLSRPFQSIIHAKrTYRELRLLKHMKHENVIGLLDVFTParsleefNDVYLVT 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTlGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyyka 584
Cdd:cd07877    102 HLMG-ADLNNIVKCQKLTDDHVQFLIY--QILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEM---- 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  585 sKGKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEILMhGVKPFQGvknNDVIGRIENGERLPMPPncPPTLYSLMT 661
Cdd:cd07877    175 -TGYVATRWYrAPEiMLNWMHYNQTVDIWSVGCIMAELLT-GRTLFPG---TDHIDQLKLILRLVGTP--GAELLKKIS 246
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
428-686 7.18e-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: 63.79  E-value: 7.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMspeNPALAVAIK-TCKNCTSDSVR----EKFLQE-ALTMR--QFDHPHIVKLIG--VITE 497
Cdd:cd14005      3 EVGDLLGKGGFGTVYSGVRI---RDGLPVAVKfVPKSRVTEWAMingpVPVPLEiALLLKasKPGVPGVIRLLDwyERPD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVwIIME---LCTlgELRSFLQVR-KYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGL 572
Cdd:cd14005     80 GFL-LIMErpePCQ--DLFDFITERgALSENLARIIFR--QVVEAVRHCHQRGVLHRDIKDENLLINLRTgEVKLIDFGC 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLpikWMAPESINFRRF--TSASdVWMFGVCMWEiLMHGVKPFqgvkNNDvIGRIENgeRLPMPP 650
Cdd:cd14005    155 GALLKDSVYTDFDGTRV---YSPPEWIRHGRYhgRPAT-VWSLGILLYD-MLCGDIPF----END-EQILRG--NVLFRP 222
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  651 NCPPTLYSLMTKCWAYDPSRRPrftelkaQLSTILE 686
Cdd:cd14005    223 RLSKECCDLISRCLQFDPSKRP-------SLEQILS 251
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
431-671 7.22e-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: 65.10  E-value: 7.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVhqgIYMSPENPALAVAIKTCKN---CTSDSVREKfLQEALTMRQFDHPHIVKL-IGVITENPVWIIMEL 506
Cdd:cd05593     21 KLLGKGTFGKV---ILVREKASGKYYAMKILKKeviIAKDEVAHT-LTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKA 584
Cdd:cd05593     97 VNGGELFFHLsRERVFSEDRTRF--YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGvKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 664
Cdd:cd05593    175 FCGT--PEYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPFYN-QDHEKLFELILMEDIKFPRTLSADAKSLLSGLL 250

                   ....*..
gi 1914779978  665 AYDPSRR 671
Cdd:cd05593    251 IKDPNKR 257
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
425-671 7.27e-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: 64.70  E-value: 7.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEAL----TMRQFDHPHIVKLIGVIT--EN 498
Cdd:cd14041      6 DRYLLLHLLGRGGFSEVYKAFDLT-EQRYVAVKIHQLNKNWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSldTD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKY--SLDLASLILyayQLSTALAYLESKR--FVHRDIAARNVL-VSSNDC--VKLGDFG 571
Cdd:cd14041     85 SFCTVLEYCEGNDLDFYLKQHKLmsEKEARSIIM---QIVNALKYLNEIKppIIHYDLKPGNILlVNGTACgeIKITDFG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  572 LSRYMEDSTYYK------ASKGKLPIKWMAPESINF----RRFTSASDVWMFGVCMWEILmHGVKPFQG-------VKNN 634
Cdd:cd14041    162 LSKIMDDDSYNSvdgmelTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFYQCL-YGRKPFGHnqsqqdiLQEN 240
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1914779978  635 DVIGRIEngERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd14041    241 TILKATE--VQFPPKPVVTPEAKAFIRRCLAYRKEDR 275
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
425-628 8.40e-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: 8.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDvhqgIYMSPENPALAvaIKTCKNCTSD---SVREKFLQEALTMRQFDHPHIVKLIGV-ITENPV 500
Cdd:cd14088      1 DRYDLGQVIKTEEFCE----IFRAKDKTTGK--LYTCKKFLKRdgrKVRKAAKNEINILKMVKHPNILQLVDVfETRKEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  501 WIIMELCTLGELRSFLQVRKY--SLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRY 575
Cdd:cd14088     75 FIFLELATGREVFDWILDQGYysERDTSNVI---RQVLEAVAYLHSLKIVHRNLKLENLVYYNrlkNSKIVISDFHLAKL 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  576 meDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14088    152 --ENGLIKEPCGT-P-EYLAPEVVGRQRYGRPVDCWAIGVIMY-ILLSGNPPF 199
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
407-648 9.61e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 66.30  E-value: 9.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  407 MPSKsYGIDEAR--DYEIQRErielgrcIGEGQFGDVHQGIYMSPENPAL--AVAIKTCKNctsdsvREK--FLQEALTM 480
Cdd:PTZ00266     1 MPGK-YDDGESRlnEYEVIKK-------IGNGRFGEVFLVKHKRTQEFFCwkAISYRGLKE------REKsqLVIEVNVM 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  481 RQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQvRKYSL----DLASLILYAYQLSTALAYLES-------KR 546
Cdd:PTZ00266    67 RELKHKNIVRYIDRFlnkANQKLYILMEFCDAGDLSRNIQ-KCYKMfgkiEEHAIVDITRQLLHALAYCHNlkdgpngER 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  547 FVHRDIAARNVLVSSN-----------------DCVKLGDFGLSRYMEDSTYYKASKGKlPIKWmAPESI--NFRRFTSA 607
Cdd:PTZ00266   146 VLHRDLKPQNIFLSTGirhigkitaqannlngrPIAKIGDFGLSKNIGIESMAHSCVGT-PYYW-SPELLlhETKSYDDK 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1914779978  608 SDVWMFGVCMWEiLMHGVKPFQGVKN-NDVIGRIENGERLPM 648
Cdd:PTZ00266   224 SDMWALGCIIYE-LCSGKTPFHKANNfSQLISELKRGPDLPI 264
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
433-624 1.13e-10

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: 63.93  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKnctSDSVREKF----LQEALTMRQFDHPHIVKLIGVITENP--------- 499
Cdd:cd07865     20 IGQGTFGEVFKARHRKTGQ---IVALKKVL---MENEKEGFpitaLREIKILQLLKHENVVNLIEICRTKAtpynrykgs 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 579
Cdd:cd07865     94 IYLVFEFCE-HDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSLA 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  580 TYYKASK--GKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEI-----LMHG 624
Cdd:cd07865    173 KNSQPNRytNRVVTLWYrPPElLLGERDYGPPIDMWGAGCIMAEMwtrspIMQG 226
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
468-679 1.24e-10

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: 63.99  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  468 SVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLILYAyqLSTALAYLESK 545
Cdd:cd06615     41 AIRNQIIRELKVLHECNSPYIVGFYGAFySDGEISICMEHMDGGSLDQVLKkAGRIPENILGKISIA--VLRGLTYLREK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  546 R-FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyykASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL--- 621
Cdd:cd06615    119 HkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM---ANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAigr 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  622 -------------MHGVKPFQGVKNNDVIGRIENG--ERLPM-------------PPNCPPTLYS-----LMTKCWAYDP 668
Cdd:cd06615    196 ypipppdakeleaMFGRPVSEGEAKESHRPVSGHPpdSPRPMaifelldyivnepPPKLPSGAFSdefqdFVDKCLKKNP 275
                          250
                   ....*....|.
gi 1914779978  669 SRRPRFTELKA 679
Cdd:cd06615    276 KERADLKELTK 286
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
426-580 1.27e-10

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: 63.25  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKT-CKNCTSDSVRekflQEALTMRQF-DHPHIVKLIGVITENPV-WI 502
Cdd:cd14016      1 RYKLVKKIGSGSFGEVYLGIDLKTGEE---VAIKIeKKDSKHPQLE----YEAKVYKLLqGGPGIPRLYWFGQEGDYnVM 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMEL--CTLGELRSFLQvRKYSLDLASLIlyAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK---LGDFGLS-RYM 576
Cdd:cd14016     74 VMDLlgPSLEDLFNKCG-RKFSLKTVLML--ADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAkKYR 150

                   ....
gi 1914779978  577 EDST 580
Cdd:cd14016    151 DPRT 154
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
478-644 1.45e-10

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 63.49  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  478 LTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAAR 555
Cdd:cd14178     49 ILLRYGQHPNIITLKDVYDDGKfVYLVMELMRGGELlDRILRQKCFSEREASAVLCT--ITKTVEYLHSQGVVHRDLKPS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  556 NVL----VSSNDCVKLGDFGLSRYMedstyyKASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVK 626
Cdd:cd14178    127 NILymdeSGNPESIRICDFGFAKQL------RAENGLLmtpcyTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFT 199
                          170       180
                   ....*....|....*....|.
gi 1914779978  627 PFQGVKNN---DVIGRIENGE 644
Cdd:cd14178    200 PFANGPDDtpeEILARIGSGK 220
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
433-620 1.51e-10

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: 63.23  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-------GVITEnpVWIIM 504
Cdd:cd14143      3 IGKGRFGEVWRGRWRGED-----VAVKIFSSREERSwFREAEIYQTVMLR---HENILGFIaadnkdnGTWTQ--LWLVS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESK--------RFVHRDIAARNVLVSSNDCVKLGDFGLS-RY 575
Cdd:cd14143     73 DYHEHGSLFDYLN--RYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGLAvRH 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  576 -MEDSTYYKASKGKLPIK-WMAPE----SINFRRFTS--ASDVWMFGVCMWEI 620
Cdd:cd14143    151 dSATDTIDIAPNHRVGTKrYMAPEvlddTINMKHFESfkRADIYALGLVFWEI 203
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
425-621 1.92e-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: 63.54  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIymsPENPALAVAIKTCKNcTSDSVR--EKFLQEALTMRQFDHPHIVKLIGVITEN---- 498
Cdd:cd07855      5 DRYEPIETIGSGAYGVVCSAI---DTKSGQKVAIKKIPN-AFDVVTtaKRTLRELKILRHFKHDNIIAIRDILRPKvpya 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 ---PVWIIMELctlgeLRSFLQVRKYS---LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd07855     81 dfkDVYVVLDL-----MESDLHHIIHSdqpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGM 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  573 SRYM----EDSTYYKASkgKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd07855    156 ARGLctspEEHKYFMTE--YVATRWYrAPElMLSLPEYTQAIDMWSVGCIFAEML 208
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
433-677 1.98e-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: 62.72  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHqgiymspenpaLAVAIKTCKNCTSDSVR-EKFLQEALTMRQ-FDHPHIVKLIG-VITENPVWIIMEL--- 506
Cdd:cd13995     12 IPRGAFGKVY-----------LAQDTKTKKRMACKLIPvEQFKPSDVEIQAcFRHENIAELYGaLLWEETVHLFMEAgeg 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 -CTLGELRSFLQVRKYSLdlaslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVkLGDFGLSRYMEDSTYYKAS 585
Cdd:cd13995     81 gSVLEKLESCGPMREFEI-----IWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  586 KGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFqgVKNNDVIG-----RIENGERLPM---PPNCPPTLY 657
Cdd:cd13995    155 LRGTEI-YMSPEVILCRGHNTKADIYSLGATIIH-MQTGSPPW--VRRYPRSAypsylYIIHKQAPPLediAQDCSPAMR 230
                          250       260
                   ....*....|....*....|
gi 1914779978  658 SLMTKCWAYDPSRRPRFTEL 677
Cdd:cd13995    231 ELLEAALERNPNHRSSAAEL 250
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
433-640 2.49e-10

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 62.79  E-value: 2.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLgE 511
Cdd:cd07869     13 LGEGSYATVYKG--KSKVNGKL-VALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIhTKETLTLVFEYVHT-D 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKASKGKLPI 591
Cdd:cd07869     89 LCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR--AKSVPSHTYSNEVVT 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  592 KWMAPESI--NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKN-NDVIGRI 640
Cdd:cd07869    167 LWYRPPDVllGSTEYSTCLDMWGVG-CIFVEMIQGVAAFPGMKDiQDQLERI 217
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
431-684 2.53e-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: 2.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-----GVITENPVWIIM 504
Cdd:cd14220      1 RQIGKGRYGEVWMGKWRGEK-----VAVKVFFTTEEASwFRETEIYQTVLMR---HENILGFIaadikGTGSWTQLYLIT 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQVRkySLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDFGLSRYM 576
Cdd:cd14220     73 DYHENGSLYDFLKCT--TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVKF 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  577 EDSTyykaSKGKLPI-------KWMAP----ESINFRRFTS--ASDVWMFGVCMWEILMHGVK---------PFQGVKNN 634
Cdd:cd14220    151 NSDT----NEVDVPLntrvgtkRYMAPevldESLNKNHFQAyiMADIYSFGLIIWEMARRCVTggiveeyqlPYYDMVPS 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  635 DV----IGRIENGERL-PMPPN------CPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 684
Cdd:cd14220    227 DPsyedMREVVCVKRLrPTVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
503-628 2.73e-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: 63.10  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLqVRK--YSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS---RYME 577
Cdd:cd05598     79 VMDYIPGGDLMSLL-IKKgiFEEDLARF--YIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTH 155
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  578 DSTYYKA-SKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd05598    156 DSKYYLAhSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEMLV-GQPPF 205
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
424-672 2.95e-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: 62.53  E-value: 2.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRcIGEGQFGDVHQ------GIYMspenpalavAIK--TCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVI 495
Cdd:cd14049      6 NEFEEIAR-LGKGGYGKVYKvrnkldGQYY---------AIKkiLIKKVTKRDCM-KVLREVKVLAGLQHPNIVGYHTAW 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TEN---PVWIIMELCTLgELRSFLQVRK---------------YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNV 557
Cdd:cd14049     75 MEHvqlMLYIQMQLCEL-SLWDWIVERNkrpceeefksapytpVDVDVTTKILQ--QLLEGVTYIHSMGIVHRDLKPRNI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  558 LVSSNDC-VKLGDFGL-----------SRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILmhgv 625
Cdd:cd14049    152 FLHGSDIhVRIGDFGLacpdilqdgndSTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---- 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  626 KPFQG-VKNNDVIGRIENGErlpMPPN---CPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd14049    228 QPFGTeMERAEVLTQLRNGQ---IPKSlckRWPVQAKYIKLLTSTEPSERP 275
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
485-671 2.95e-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: 2.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  485 HPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 562
Cdd:cd05592     55 HPFLTHLFCTFqTESHLFFVMEYLNGGDLMFHIQqSGRFDEDRARF--YGAEIICGLQFLHSRGIIYRDLKLDNVLLDRE 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  563 DCVKLGDFGLS-----RYMEDSTYYKASKgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI 637
Cdd:cd05592    133 GHIKIADFGMCkeniyGENKASTFCGTPD------YIAPEILKGQKYNQSVDWWSFGVLLYEMLI-GQSPFHGEDEDELF 205
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1914779978  638 GRIENgERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05592    206 WSICN-DTPHYPRWLTKEAASCLSLLLERNPEKR 238
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
486-628 3.00e-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: 62.74  E-value: 3.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  486 PHIVKLIGVI-----TENPVWIIMELCTLGELRSFLQVR---KYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNV 557
Cdd:cd14170     55 PHIVRIVDVYenlyaGRKCLLIVMECLDGGELFSRIQDRgdqAFTEREASEIMKS--IGEAIQYLHSINIAHRDVKPENL 132
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  558 LVSS---NDCVKLGDFGLSRymEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14170    133 LYTSkrpNAILKLTDFGFAK--ETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPF 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
431-632 3.22e-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: 3.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVhqgiymspenpaLAVAIKT------CKNCTSDSVREK-----FLQEALTMRQFDHPHIVKLIGVI-TEN 498
Cdd:cd05607      8 RVLGKGGFGEV------------CAVQVKNtgqmyaCKKLDKKRLKKKsgekmALLEKEILEKVNSPFIVSLAYAFeTKT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELR-SFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05607     76 HLCLVMSLMNGGDLKyHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  578 DS---TYYKASKGklpikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVK 632
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 ...
431-671 3.51e-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: 3.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSPENpalAVAIKTCKN---CTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 506
Cdd:cd05590      1 RVLGKGSFGKVMLARLKESGR---LYAVKVLKKdviLQDDDVECTMTEKRILSLARNHPFLTQLYCCFqTPDRLFFVMEF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 586
Cdd:cd05590     78 VNGGDLMFHIQ-KSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  587 GKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLP---MPPNCPPTLYSLMTKc 663
Cdd:cd05590    157 CGTP-DYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFEAILNDEVVYptwLSQDAVDILKAFMTK- 233

                   ....*...
gi 1914779978  664 wayDPSRR 671
Cdd:cd05590    234 ---NPTMR 238
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
433-620 3.57e-10

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: 62.38  E-value: 3.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymspeNPALAVAIKTCK---NCTSDSVREKFLQEALTMRQFDHPHIVKLIG-----VITENPVWIIM 504
Cdd:cd14030     33 IGRGSFKTVYKGL-----DTETTVEVAWCElqdRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDswestVKGKKCIVLVT 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS-NDCVKLGDFGLSRyMEDSTY 581
Cdd:cd14030    108 ELMTSGTLKTYLK-RFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT-LKRASF 185
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1914779978  582 YKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWEI 620
Cdd:cd14030    186 AKSVIGT--PEFMAPEMYE-EKYDESVDVYAFGMCMLEM 221
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
427-621 4.10e-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: 4.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRCIGEGQFGDVHQgiYMSPENpALAVAIKTCKNCTSDSVREKFLQEALTMR-QFDHPHIVKLIGVITENPVWIIME 505
Cdd:cd07853      2 VEPDRPIGYGAFGVVWS--VTDPRD-GKRVALKKMPNVFQNLVSCKRVFRELKMLcFFKHDNVLSALDILQPPHIDPFEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGEL-RSFLQ---VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 581
Cdd:cd07853     79 IYVVTELmQSDLHkiiVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDES 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  582 YKASKGKLPIKWMAPESI-NFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd07853    159 KHMTQEVVTQYYRAPEILmGSRHYTSAVDIWSVGCIFAELL 199
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
425-640 4.28e-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: 4.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGiYMSPENPALAVAiKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE------- 497
Cdd:cd07878     15 ERYQNLTPVGSGAYGSVCSA-YDTRLRQKVAVK-KLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPatsienf 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTlGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSnDC-VKLGDFGLSRYM 576
Cdd:cd07878     93 NEVYLVTNLMG-ADLNNIVKCQKLSDEHVQFLIY--QLLRGLKYIHSAGIIHRDLKPSNVAVNE-DCeLRILDFGLARQA 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  577 EDSTyykasKGKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI 640
Cdd:cd07878    169 DDEM-----TGYVATRWYrAPEiMLNWMHYNQTVDIWSVGCIMAE-LLKGKALFPGNDYIDQLKRI 228
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
474-672 4.33e-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: 61.38  E-value: 4.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  474 LQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTLGELRSFLQVR-KYSLDlaSLILYAYQLSTALAYLESKRFVHRD 551
Cdd:cd14111     47 LQEYEILKSLHHERIMALhEAYITPRYLVLIAEFCSGKELLHSLIDRfRYSED--DVVGYLVQILQGLEYLHGRRVLHLD 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  552 IAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGV 631
Cdd:cd14111    125 IKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTY-IMLSGRSPFEDQ 203
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1914779978  632 KNNDVIGRIENGERLP--MPPNCPPTLYSLMTKCWAYDPSRRP 672
Cdd:cd14111    204 DPQETEAKILVAKFDAfkLYPNVSQSASLFLKKVLSSYPWSRP 246
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
475-628 4.57e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 63.37  E-value: 4.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  475 QEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAA 554
Cdd:PHA03211   209 HEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRSDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKT 288
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  555 RNVLVSSNDCVKLGDFG---LSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPF 628
Cdd:PHA03211   289 ENVLVNGPEDICLGDFGaacFARGSWSTPFHYGIAGT--VDTNAPEVLAGDPYTPSVDIWSAGLVIFEAAVHTASLF 363
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
475-625 5.54e-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: 5.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  475 QEALTMRQFDHPHIVKLIGVITENP-------VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRF 547
Cdd:cd07850     48 RELVLMKLVNHKNIIGLLNVFTPQKsleefqdVYLVMELMD----ANLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGI 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSnDCV-KLGDFGLSRYMEDST---------YYKaskgklpikwmAPESINFRRFTSASDVWMFGVCM 617
Cdd:cd07850    124 IHRDLKPSNIVVKS-DCTlKILDFGLARTAGTSFmmtpyvvtrYYR-----------APEVILGMGYKENVDIWSVGCIM 191

                   ....*...
gi 1914779978  618 WEILMHGV 625
Cdd:cd07850    192 GEMIRGTV 199
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
457-628 5.60e-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: 61.76  E-value: 5.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  457 AIKTCKNcTSDsvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQVRKY--SLDLASLIlyaY 533
Cdd:cd14085     32 AVKKLKK-TVD--KKIVRTEIGVLLRLSHPNIIKLKEIFeTPTEISLVLELVTGGELFDRIVEKGYysERDAADAV---K 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  534 QLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRRFTSASDV 610
Cdd:cd14085    106 QILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKIVDQQVTMKTVCGT-P-GYCAPEILRGCAYGPEVDM 183
                          170
                   ....*....|....*...
gi 1914779978  611 WMFGVCMWeILMHGVKPF 628
Cdd:cd14085    184 WSVGVITY-ILLCGFEPF 200
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
433-644 5.88e-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: 5.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGD----VHQGIYMSpenpalaVAIKTCKNCTSDSVREKflqeALTMRQFDHPHIVKLIGVITE-NPVWIIMELC 507
Cdd:cd14175      9 IGVGSYSVckrcVHKATNME-------YAVKVIDKSKRDPSEEI----EILLRYGQHPNIITLKDVYDDgKHVYLVTELM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  508 TLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLV---SSN-DCVKLGDFGLSRYMedstyy 582
Cdd:cd14175     78 RGGELlDKILRQKFFSEREASSVLHT--ICKTVEYLHSQGVVHRDLKPSNILYvdeSGNpESLRICDFGFAKQL------ 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  583 KASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF-QGVKNN--DVIGRIENGE 644
Cdd:cd14175    150 RAENGLLmtpcyTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFaNGPSDTpeEILTRIGSGK 218
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
433-640 5.93e-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: 5.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKN---CTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCT 508
Cdd:cd05615     18 LGKGSFGKVMLAERKGSDE---LYAIKILKKdvvIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFqTVDRLYFVMEYVN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASK 586
Cdd:cd05615     95 GGDLMYHIQqVGKFKEPQA--VFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKeHMVEGVTTRTFC 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  587 GKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI 640
Cdd:cd05615    173 GT-P-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSI 223
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
474-671 6.29e-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: 6.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  474 LQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTLGELrsFLQV---RKYSLDLASLilYAYQLSTALAYLESKRFVH 549
Cdd:cd05571     43 LTENRVLQNTRHPFLTSLkYSFQTNDRLCFVMEYVNGGEL--FFHLsreRVFSEDRTRF--YGAEIVLALGYLHSQGIVY 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  550 RDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKASK---GKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVK 626
Cdd:cd05571    119 RDLKLENLLLDKDGHIKITDFGLCK--EEISYGATTKtfcGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRL 193
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  627 PFQGvKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd05571    194 PFYN-RDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
425-671 6.56e-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: 61.61  E-value: 6.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIYMSPENPAlAVAIKTCKNCTSDSVREKFLQEAL----TMRQFDHPHIVKLIGVIT--EN 498
Cdd:cd14040      6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYA-AVKIHQLNKSWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSldTD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKY--SLDLASLILyayQLSTALAYLESKR--FVHRDIAARNVL-VSSNDC--VKLGDFG 571
Cdd:cd14040     85 TFCTVLEYCEGNDLDFYLKQHKLmsEKEARSIVM---QIVNALRYLNEIKppIIHYDLKPGNILlVDGTACgeIKITDFG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  572 LSRYMEDSTYYK-----ASKGKLPIKWMAPESINF----RRFTSASDVWMFGVCMWEILmHGVKPFQG-------VKNND 635
Cdd:cd14040    162 LSKIMDDDSYGVdgmdlTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFGHnqsqqdiLQENT 240
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1914779978  636 VIGRIEngERLPMPPNCPPTLYSLMTKCWAYDPSRR 671
Cdd:cd14040    241 ILKATE--VQFPVKPVVSNEAKAFIRRCLAYRKEDR 274
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
468-662 6.66e-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: 61.99  E-value: 6.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  468 SVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRsflQVRKYSLDLASLILYAYQLST--ALAYLES 544
Cdd:cd06650     45 AIRNQIIRELQVLHECNSPYIVGFYGAFySDGEISICMEHMDGGSLD---QVLKKAGRIPEQILGKVSIAVikGLTYLRE 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  545 K-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyykASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMH 623
Cdd:cd06650    122 KhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM---ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVG 198
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1914779978  624 -------GVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTK 662
Cdd:cd06650    199 rypipppDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR 244
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
427-620 8.48e-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: 8.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRcIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 505
Cdd:cd07871      8 VKLDK-LGEGTYATVFKGRSKLTEN---LVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIhTERCLTLVFE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKAS 585
Cdd:cd07871     84 YLD-SDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLAR--AKSVPTKTY 160
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1914779978  586 KGKLPIKWMAPESI--NFRRFTSASDVWMFGVCMWEI 620
Cdd:cd07871    161 SNEVVTLWYRPPDVllGSTEYSTPIDMWGVGCILYEM 197
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
486-628 9.51e-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: 60.77  E-value: 9.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  486 PHIVKLIGVItENP------VWIIMELCTLGELRSFLQVR---KYSLDLASLILYayQLSTALAYLESKRFVHRDIAARN 556
Cdd:cd14172     57 PHIVHILDVY-ENMhhgkrcLLIIMECMEGGELFSRIQERgdqAFTEREASEIMR--DIGTAIQYLHSMNIAHRDVKPEN 133
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  557 VLVSS---NDCVKLGDFGLSRymEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14172    134 LLYTSkekDAVLKLTDFGFAK--ETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPF 205
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
427-620 9.75e-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: 60.89  E-value: 9.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRcigeGQFGDVHQGIymspeNPALAVAIKTCK---NCTSDSVREKFLQEALTMRQFDHPHIVKLIG-----VITEN 498
Cdd:cd14031     16 IELGR----GAFKTVYKGL-----DTETWVEVAWCElqdRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDswesvLKGKK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS-NDCVKLGDFGLSRY 575
Cdd:cd14031     87 CIVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  576 MEDStYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWEI 620
Cdd:cd14031    166 MRTS-FAKSVIGT--PEFMAPEMYE-EHYDESVDVYAFGMCMLEM 206
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
529-644 1.06e-09

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: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  529 ILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSAS 608
Cdd:cd05631    105 IFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGT--VGYMAPEVINNEKYTFSP 182
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1914779978  609 DVWMFGVCMWEiLMHGVKPF----QGVKNNDVIGRIENGE 644
Cdd:cd05631    183 DWWGLGCLIYE-MIQGQSPFrkrkERVKREEVDRRVKEDQ 221
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
431-628 1.06e-09

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: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQE-ALTMRQFDHPHIVKL-IGVITENPVWIIMELCT 508
Cdd:cd05603      1 KVIGKGSFGKVLLAKRKC-DGKFYAVKVLQKKTILKKKEQNHIMAErNVLLKNLKHPFLVGLhYSFQTSEKLYFVLDYVN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 588
Cdd:cd05603     80 GGELFFHLQ-RERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1914779978  589 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPF 628
Cdd:cd05603    159 TP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPF 196
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
425-677 1.14e-09

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: 60.85  E-value: 1.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIE-LGRcIGEGQFGDVHQgiYMSPENPALaVAIKTCKNCTSDSVREKF-LQEALTMRQFDHPHIVKLIGVITEN-PVW 501
Cdd:cd07847      1 EKYEkLSK-IGEGSYGVVFK--CRNRETGQI-VAIKKFVESEDDPVIKKIaLREIRMLKQLKHPNLVNLIEVFRRKrKLH 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELCTLGELRSfLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM----E 577
Cdd:cd07847     77 LVFEYCDHTVLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILtgpgD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  578 DSTYYKASkgklpiKWM-APESI-NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIE-------------- 641
Cdd:cd07847    156 DYTDYVAT------RWYrAPELLvGDTQYGPPVDVWAIG-CVFAELLTGQPLWPGKSDVDQLYLIRktlgdliprhqqif 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  642 ------NGERLPMP----------PNCPPTLYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd07847    229 stnqffKGLSIPEPetrepleskfPNISSPALSFLKGCLQMDPTERLSCEEL 280
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
420-573 1.19e-09

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: 60.46  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRERIELgrcIGEGQFGDVHQ------GIYMspenpalavAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG 493
Cdd:cd14046      4 YLTDFEELQV---LGKGAFGQVVKvrnkldGRYY---------AIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQ 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 V-ITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd14046     72 AwIERANLYIQMEYCEKSTLRDLIDSGLF-QDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL 150

                   .
gi 1914779978  573 S 573
Cdd:cd14046    151 A 151
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
425-621 1.20e-09

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: 61.17  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGIymspENPA-LAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI------TE 497
Cdd:cd07849      5 PRYQNLSYIGEGAYGMVCSAV----HKPTgQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQrpptfeSF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NPVWIIMELCTLgELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd07849     81 KDVYIVQELMET-DLYKLIKTQHLSNDHIQYFLY--QILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIAD 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  578 DS-------TYYKASkgklpiKWM-APE-SINFRRFTSASDVWMFGVCMWEIL 621
Cdd:cd07849    158 PEhdhtgflTEYVAT------RWYrAPEiMLNSKGYTKAIDIWSVGCILAEML 204
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
426-621 1.27e-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: 61.03  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYmspENPALAVAIKTCKnCTSDSVREKFLQE--ALTMRQFDHPHIVK------------- 490
Cdd:cd13977      1 KYSLIREVGRGSYGVVYEAVV---RRTGARVAVKKIR-CNAPENVELALREfwALSSIQRQHPNVIQleecvlqrdglaq 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  491 -------------------LIGVITENP-----VWIIMELCTLGELRSFLQVRKYSLDL-ASLILyayQLSTALAYLESK 545
Cdd:cd13977     77 rmshgssksdlylllvetsLKGERCFDPrsacyLWFVMEFCDGGDMNEYLLSRRPDRQTnTSFML---QLSSALAFLHRN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  546 RFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDStyykASKGKLPIK--------------WMAPEsINFRRFTSAS 608
Cdd:cd13977    154 QIVHRDLKPDNILISHKRgepILKVADFGLSKVCSGS----GLNPEEPANvnkhflssacgsdfYMAPE-VWEGHYTAKA 228
                          250
                   ....*....|...
gi 1914779978  609 DVWMFGVCMWEIL 621
Cdd:cd13977    229 DIFALGIIIWAMV 241
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
476-678 1.35e-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: 60.66  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  476 EALTMRQF-------DHPHIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-YSLDLASLILYAyqLSTALAYLESKR 546
Cdd:cd14180     44 EANTQREVaalrlcqSHPNIVALHEVLHDQyHTYLVMELLRGGELLDRIKKKArFSESEASQLMRS--LVSAVSFMHEAG 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  547 FVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDStyykASKGKLP---IKWMAPESINFRRFTSASDVWMFGVCMWEI 620
Cdd:cd14180    122 VVHRDLKPENILYADesdGAVLKVIDFGFARLRPQG----SRPLQTPcftLQYAAPELFSNQGYDESCDLWSLGVILYTM 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  621 LmHGVKPFQGVKNN-------DVIGRIENGErlpmppncpptlYSLMTKCW---------------AYDPSRRPRFTELK 678
Cdd:cd14180    198 L-SGQVPFQSKRGKmfhnhaaDIMHKIKEGD------------FSLEGEAWkgvseeakdlvrgllTVDPAKRLKLSELR 264
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
433-571 1.46e-09

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: 57.45  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMsPENPALAVAIKTCKNctsDSVREKFLQEALTMRQFD--HPHIVKLIGV-ITENPVWIIMELCTL 509
Cdd:cd13968      1 MGEGASAKVFWAEGE-CTTIGVAVKIGDDVN---NEEGEDLESEMDILRRLKglELNIPKVLVTeDVDGPNILLMELVKG 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  510 GELRSFLQVRkySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 571
Cdd:cd13968     77 GTLIAYTQEE--ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
428-671 1.61e-09

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: 60.81  E-value: 1.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCKN---CTSDSVREKfLQEALTMRQFDHPHIVKL-IGVITENPVWII 503
Cdd:cd05594     28 EYLKLLGKGTFGKV---ILVKEKATGRYYAMKILKKeviVAKDEVAHT-LTENRVLQNSRHPFLTALkYSFQTHDRLCFV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKR-FVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDST 580
Cdd:cd05594    104 MEYANGGELFFHLsRERVFSEDRARF--YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  581 YYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGvKNNDVIGRIENGERLPMPPNCPPTLYSLM 660
Cdd:cd05594    182 TMKTFCGT--PEYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPFYN-QDHEKLFELILMEEIRFPRTLSPEAKSLL 257
                          250
                   ....*....|.
gi 1914779978  661 TKCWAYDPSRR 671
Cdd:cd05594    258 SGLLKKDPKQR 268
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
428-644 1.83e-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: 60.80  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREKflqeALTMRQFDHPHIVKLIGVITENP-VWIIMEL 506
Cdd:cd14176     22 EVKEDIGVGSYSVCKRCIHKATN---MEFAVKIIDKSKRDPTEEI----EILLRYGQHPNIITLKDVYDDGKyVYVVTEL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  507 CTLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLV---SSN-DCVKLGDFGLSRYMedsty 581
Cdd:cd14176     95 MKGGELlDKILRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYvdeSGNpESIRICDFGFAKQL----- 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  582 yKASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN---DVIGRIENGE 644
Cdd:cd14176    168 -RAENGLLmtpcyTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDtpeEILARIGSGK 236
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
484-644 1.86e-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: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  484 DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSS 561
Cdd:cd05609     58 ENPFVVSMYCSFeTKRHLCMVMEYVEGGDCATLLKnIGPLPVDMARM--YFAETVLALEYLHSYGIVHRDLKPDNLLITS 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  562 NDCVKLGDFGLSR-------------YMEDSTYYKASKGKL--PiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVK 626
Cdd:cd05609    136 MGHIKLTDFGLSKiglmslttnlyegHIEKDTREFLDKQVCgtP-EYIAPEVILRQGYGKPVDWWAMGIILYEFL-VGCV 213
                          170
                   ....*....|....*...
gi 1914779978  627 PFQGVKNNDVIGRIENGE 644
Cdd:cd05609    214 PFFGDTPEELFGQVISDE 231
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
439-677 2.09e-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: 60.49  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  439 GDVHQGIYMSPENPAL--AVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITENP-------VWIIMELCT 508
Cdd:cd07874     26 GSGAQGIVCAAYDAVLdrNVAIKKLSRPFQNQTHAKrAYRELVLMKCVNHKNIISLLNVFTPQKsleefqdVYLVMELMD 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 lgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMedSTYYKASKGK 588
Cdd:cd07874    106 ----ANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA--GTSFMMTPYV 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKpFQGVKNNDVIGRIEngERLPMPpnCPPTLYSLMTKCWAYdP 668
Cdd:cd07874    180 VTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKIL-FPGRDYIDQWNKVI--EQLGTP--CPEFMKKLQPTVRNY-V 253

                   ....*....
gi 1914779978  669 SRRPRFTEL 677
Cdd:cd07874    254 ENRPKYAGL 262
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
426-658 2.19e-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: 2.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCT-SDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWII 503
Cdd:cd07848      2 KFEVLGVVGEGAYGVVLKCRHKETKE---IVAIKKFKDSEeNEEVKETTLRELKMLRTLKQENIVELKEAFRRrGKLYLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRsFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 583
Cdd:cd07848     79 FEYVEKNMLE-LLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNAN 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914779978  584 ASKgKLPIKWM-APESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIEN--GerlPMPPNCPPTLYS 658
Cdd:cd07848    158 YTE-YVATRWYrSPELLLGAPYGKAVDMWSVG-CILGELSDGQPLFPGESEIDQLFTIQKvlG---PLPAEQMKLFYS 230
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
428-642 2.35e-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: 60.02  E-value: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVH-------QGIYmspenpalavAIKTCKNCTSDSVREK--FLQEALTMRQFDHPHIVKLIGVITEN 498
Cdd:cd05601      4 EVKNVIGRGHFGEVQvvkekatGDIY----------AMKVLKKSETLAQEEVsfFEEERDIMAKANSPWITKLQYAFQDS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 P-VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 577
Cdd:cd05601     74 EnLYLVMEYHPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLS 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  578 DStyyKASKGKLPI---KWMAPE---SINfRRFTSASDV----WMFGVCMWEiLMHGVKPFQGVKNNDVIGRIEN 642
Cdd:cd05601    154 SD---KTVTSKMPVgtpDYIAPEvltSMN-GGSKGTYGVecdwWSLGIVAYE-MLYGKTPFTEDTVIKTYSNIMN 223
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
433-671 2.38e-09

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: 59.16  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDV------HQGIYMSPENPAlaVAIKtCKNCTSDSVRekFLQE-ALTMRQFDHPHIVKLIGVI-TENPVWIIM 504
Cdd:cd14019      9 IGEGTFSSVykaedkLHDLYDRNKGRL--VALK-HIYPTSSPSR--ILNElECLERLGGSNNVSGLITAFrNEDQVVAVL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGELRSFLqvrkYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSndcvKLG-----DFGLSRYMEDS 579
Cdd:cd14019     84 PYIEHDDFRDFY----RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNR----ETGkgvlvDFGLAQREEDR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  580 TYYKASKGKLPiKWMAPESInFRRF--TSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIEN--GERLpmppncppt 655
Cdd:cd14019    156 PEQRAPRAGTR-GFRAPEVL-FKCPhqTTAIDIWSAGVILLSILSGRFPFFFSSDDIDALAEIATifGSDE--------- 224
                          250
                   ....*....|....*.
gi 1914779978  656 LYSLMTKCWAYDPSRR 671
Cdd:cd14019    225 AYDLLDKLLELDPSKR 240
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
475-674 2.58e-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: 2.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  475 QEALTMRQFDHPHIVKLIGVITENP-------VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRF 547
Cdd:cd07875     72 RELVLMKCVNHKNIIGLLNVFTPQKsleefqdVYIVMELMD----ANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGI 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  548 VHRDIAARNVLVSSNDCVKLGDFGLSRYMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKp 627
Cdd:cd07875    148 IHRDLKPSNIVVKSDCTLKILDFGLARTA--GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVL- 224
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1914779978  628 FQGVKNNDVIGRIEngERLPMPpnCPPTLYSLMTKCWAYdPSRRPRF 674
Cdd:cd07875    225 FPGTDHIDQWNKVI--EQLGTP--CPEFMKKLQPTVRTY-VENRPKY 266
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
464-677 2.81e-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: 59.62  E-value: 2.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  464 CTSDSVREKFLQEALTMRQFDHPHIVKLI--GVITENP----VWIIMELCTLGELRSFLQVRK-----YSLDLASLILYa 532
Cdd:cd13986     35 CHSKEDVKEAMREIENYRLFNHPNILRLLdsQIVKEAGgkkeVYLLLPYYKRGSLQDEIERRLvkgtfFPEDRILHIFL- 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  533 yQLSTALAYL---ESKRFVHRDIAARNVLVSSNDCVKLGDFG-------------LSRYMEDSTyykASKGKLPikWMAP 596
Cdd:cd13986    114 -GICRGLKAMhepELVPYAHRDIKPGNVLLSEDDEPILMDLGsmnparieiegrrEALALQDWA---AEHCTMP--YRAP 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  597 ESINFRR---FTSASDVWMFGvCMWEILMHGVKPFQGV--KNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSR 670
Cdd:cd13986    188 ELFDVKShctIDEKTDIWSLG-CTLYALMYGESPFERIfqKGDSLALAVLSGNySFPDNSRYSEELHQLVKSMLVVNPAE 266

                   ....*..
gi 1914779978  671 RPRFTEL 677
Cdd:cd13986    267 RPSIDDL 273
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
510-671 3.01e-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: 3.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQVRKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKASKGK 588
Cdd:cd05575     81 GELFFHLQRERHFPEPRAR-FYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEgIEPSDTTSTFCGT 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  589 lPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDP 668
Cdd:cd05575    160 -P-EYLAPEVLRKQPYDRTVDWWCLGAVLYE-MLYGLPPFYSRDTAEMYDNILH-KPLRLRTNVSPSARDLLEGLLQKDR 235

                   ...
gi 1914779978  669 SRR 671
Cdd:cd05575    236 TKR 238
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
420-644 3.21e-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: 58.75  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  420 YEIQRErielgrcIGEGQFGDV----HQGIYMSPENPALAVAIKTcknctsdsvREKFLQEALTMRQFDHPHIVKLIGVI 495
Cdd:cd14107      4 YEVKEE-------IGRGTFGFVkrvtHKGNGECCAAKFIPLRSST---------RARAFQERDILARLSHRRLTCLLDQF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 -TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS--NDCVKLGDFGL 572
Cdd:cd14107     68 eTRKTLILILELCSSEELLDRL-FLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSptREDIKICDFGF 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  573 SRYMeDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGE 644
Cdd:cd14107    147 AQEI-TPSEHQFSKYGSP-EFVAPEIVHQEPVSAATDIWALGVIAYLSLTCH-SPFAGENDRATLLNVAEGV 215
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
426-630 3.74e-09

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: 59.48  E-value: 3.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDV-----HQgiymSPENpalaVAIKTCKNctsdsvREKFLQEALT-------MRQFD---HPHIVK 490
Cdd:cd14210     14 RYEVLSVLGKGSFGQVvkcldHK----TGQL----VAIKIIRN------KKRFHQQALVevkilkhLNDNDpddKHNIVR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  491 LIGVIT-ENPVWIIMELctLG-ELRSFLQVRKY---SLDLASLIlyAYQLSTALAYLESKRFVHRDIAARNVLVSSND-- 563
Cdd:cd14210     80 YKDSFIfRGHLCIVFEL--LSiNLYELLKSNNFqglSLSLIRKF--AKQILQALQFLHKLNIIHCDLKPENILLKQPSks 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  564 CVKLGDFGLS--------RYMEdSTYYKaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQG 630
Cdd:cd14210    156 SIKVIDFGSScfegekvyTYIQ-SRFYR-----------APEVILGLPYDTAIDMWSLGCILAE-LYTGYPLFPG 217
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
427-620 4.79e-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: 58.55  E-value: 4.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  427 IELGRcigeGQFGDVHQGIymspeNPALAVAIKTCK---NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP---- 499
Cdd:cd14032      7 IELGR----GSFKTVYKGL-----DTETWVEVAWCElqdRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAkgkr 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 -VWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS-NDCVKLGDFGLSRy 575
Cdd:cd14032     78 cIVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT- 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1914779978  576 MEDSTYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWEI 620
Cdd:cd14032    156 LKRASFAKSVIGT--PEFMAPEMYE-EHYDESVDVYAFGMCMLEM 197
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
430-630 4.91e-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: 4.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  430 GRCIGEGQFGDVHQGI--YMSPEnpalaVAIKTCKNCTSDSvREKFLQEALTMRQFD-HPHIVKLIGVITENPV-WIIME 505
Cdd:cd14090      7 GELLGEGAYASVQTCInlYTGKE-----YAVKIIEKHPGHS-RSRVFREVETLHQCQgHPNILQLIEYFEDDERfYLVFE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 LCTLGELRSFLQVRK-YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDC---VKLGDFGLSRYMEDSTY 581
Cdd:cd14090     81 KMRGGPLLSHIEKRVhFTEQEASLVVR--DIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIKLSST 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914779978  582 YkASKGKLP--------IKWMAPESINFRRFTSAS-----DVWMFGVCMWeILMHGVKPFQG 630
Cdd:cd14090    159 S-MTPVTTPelltpvgsAEYMAPEVVDAFVGEALSydkrcDLWSLGVILY-IMLCGYPPFYG 218
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
431-647 6.83e-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: 6.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  431 RCI---GEGQFGDVHQGIYMSPENpalAVAIKTCKNC---TSDSVR----EKFLQEALT-MRqfdHPHIVKLIGVI-TEN 498
Cdd:cd05589      2 RCIavlGRGHFGKVLLAEYKPTGE---LFAIKALKKGdiiARDEVEslmcEKRIFETVNsAR---HPFLVNLFACFqTPE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  499 PVWIIMELCTLGELRSFLQVRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymED 578
Cdd:cd05589     76 HVCFVMEYAAGGDLMMHIHEDVFSEPRA--VFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EG 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  579 -------STYYKASKgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGE-RLP 647
Cdd:cd05589    152 mgfgdrtSTFCGTPE------FLAPEVLTDTSYTRAVDWWGLGVLIYEMLV-GESPFPGDDEEEVFDSIVNDEvRYP 221
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
421-620 6.92e-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: 58.91  E-value: 6.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  421 EIQRERIELGRCIGEGQFGDVHQgIYMSPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENP 499
Cdd:cd06649      1 ELKDDDFERISELGAGNGGVVTK-VQHKPSG--LIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFySDGE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIMELCTLGELRsflQVRKYSLDLASLILYAYQLST--ALAYLESK-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 576
Cdd:cd06649     78 ISICMEHMDGGSLD---QVLKEAKRIPEEILGKVSIAVlrGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1914779978  577 EDSTyykASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEI 620
Cdd:cd06649    155 IDSM---ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEL 195
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
529-640 8.13e-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: 58.14  E-value: 8.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  529 ILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSAS 608
Cdd:cd05605    105 VFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGRVGT--VGYMAPEVVKNERYTFSP 182
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1914779978  609 DVWMFGVCMWEILMhGVKPFQG----VKNNDVIGRI 640
Cdd:cd05605    183 DWWGLGCLIYEMIE-GQAPFRArkekVKREEVDRRV 217
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
474-642 1.05e-08

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: 57.22  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  474 LQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDI 552
Cdd:cd14108     46 RRELALLAELDHKSIVRFHDAFEKrRVVIIVTELCHEELLERIT--KRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDL 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  553 AARNVLV--SSNDCVKLGDFGLSRYME-DSTYYkaSKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQ 629
Cdd:cd14108    124 KPENLLMadQKTDQVRICDFGNAQELTpNEPQY--CKYGTP-EFVAPEIVNQSPVSKVTDIWPVGVIAY-LCLTGISPFV 199
                          170
                   ....*....|...
gi 1914779978  630 GVKNNDVIGRIEN 642
Cdd:cd14108    200 GENDRTTLMNIRN 212
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
496-734 1.24e-08

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: 57.79  E-value: 1.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 574
Cdd:cd05587     68 TMDRLYFVMEYVNGGDLMYHIQqVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  575 --YMEDSTyYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLP--MP 649
Cdd:cd05587    146 egIFGGKT-TRTFCGT-P-DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSImEHNVSYPksLS 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  650 PNCPPTLYSLMTKcwayDPSRRPRFTelkaqlstileeEKAQQEERMRMESRRqatVSWDSGGSDEAPPkPSRPGYPSPR 729
Cdd:cd05587    222 KEAVSICKGLLTK----HPAKRLGCG------------PTGERDIKEHPFFRR---IDWEKLERREIQP-PFKPKIKSPR 281

                   ....*
gi 1914779978  730 SSEGF 734
Cdd:cd05587    282 DAENF 286
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
529-644 1.33e-08

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: 57.67  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  529 ILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSAS 608
Cdd:cd05632    107 LFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGT--VGYMAPEVLNNQRYTLSP 184
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1914779978  609 DVWMFGVCMWEiLMHGVKPFQG----VKNNDVIGRIENGE 644
Cdd:cd05632    185 DYWGLGCLIYE-MIEGQSPFRGrkekVKREEVDRRVLETE 223
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
480-640 1.49e-08

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: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  480 MRQFDHPHIVKLIGVITENP-------VWIIMELctLG-ELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRD 551
Cdd:cd07851     68 LKHMKHENVIGLLDVFTPASsledfqdVYLVTHL--MGaDLNNIVKCQKLSDDHIQFLVY--QILRGLKYIHSAGIIHRD 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  552 IAARNVLVSSNDCVKLGDFGLSRYMEDS-TYYKASkgklpiKW-MAPESI-NFRRFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd07851    144 LKPSNLAVNEDCELKILDFGLARHTDDEmTGYVAT------RWyRAPEIMlNWMHYNQTVDIWSVGCIMAELLT-GKTLF 216
                          170
                   ....*....|..
gi 1914779978  629 QGVKNNDVIGRI 640
Cdd:cd07851    217 PGSDHIDQLKRI 228
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
380-634 1.57e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 57.93  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  380 DPPSTDEISGDETDDYAEIIDEEDTYTMPSKSYGIDEARDY-EIQRERIELGRCIGEGQFGDVHQGIyMSPENPALAVAI 458
Cdd:PHA03207    30 DTSDSKDTTGDKFDDCDELGDSDDVTHATDYDADEESLSPQtDVCQEPCETTSSSDPASVVRMQYNI-LSSLTPGSEGEV 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  459 KTCKNcTSDSVREKFLQEALT-----------MRQFDHPHIVKLIGVITENP-VWIIMELCTLgELRSFLQvRKYSLDLA 526
Cdd:PHA03207   109 FVCTK-HGDEQRKKVIVKAVTggktpgreidiLKTISHRAIINLIHAYRWKStVCMVMPKYKC-DLFTYVD-RSGPLPLE 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  527 SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY----YKASkGKLPIKwmAPESINFR 602
Cdd:PHA03207   186 QAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDtpqcYGWS-GTLETN--SPELLALD 262
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1914779978  603 RFTSASDVWMFGVCMWEILMHGVkPFQGVKNN 634
Cdd:PHA03207   263 PYCAKTDIWSAGLVLFEMSVKNV-TLFGKQVK 293
pknD PRK13184
serine/threonine-protein kinase PknD;
425-686 1.61e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 59.01  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  425 ERIELGRCIGEGQFGDVHQGiymspENPALA--VAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVITE-NP 499
Cdd:PRK13184     2 QRYDIIRLIGKGGMGEVYLA-----YDPVCSrrVALKKIREDLSENplLKKRFLREAKIAADLIHPGIVPVYSICSDgDP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 VWIIM---ELCTLGE-LRSFLQVRKYSLDLA------SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 569
Cdd:PRK13184    77 VYYTMpyiEGYTLKSlLKSVWQKESLSKELAektsvgAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  570 FGLSRY--------------MEDSTYYKASK-GKL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVkPFQGVK 632
Cdd:PRK13184   157 WGAAIFkkleeedlldidvdERNICYSSMTIpGKIvgTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSF-PYRRKK 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  633 NNdvigRIENGERLPMPP------NCPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILE 686
Cdd:PRK13184   236 GR----KISYRDVILSPIevapyrEIPPFLSQIAMKALAVDPAERYSsVQELKQDLEPHLQ 292
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
534-630 1.62e-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: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  534 QLSTALAYLESKRFVHRDIAARNVLVSSnDC----VKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRRFTSASD 609
Cdd:cd14197    119 QILEGVSFLHNNNVVHLDLKPQNILLTS-ESplgdIKIVDFGLSRILKNSEELREIMGT-P-EYVAPEILSYEPISTATD 195
                           90       100
                   ....*....|....*....|.
gi 1914779978  610 VWMFGVCMWeILMHGVKPFQG 630
Cdd:cd14197    196 MWSIGVLAY-VMLTGISPFLG 215
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
457-621 1.84e-08

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: 57.02  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  457 AIKT----CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN--PVWIIMELC--TLGELrsfLQVRKYSLD---L 525
Cdd:cd14001     32 AVKKinskCDKGQRSLYQERLKEEAKILKSLNHPNIVGFRAFTKSEdgSLCLAMEYGgkSLNDL---IEERYEAGLgpfP 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  526 ASLIL-YAYQLSTALAYLES-KRFVHRDIAARNVLVSSN-DCVKLGDFGLS-RYMEDSTYYKASK----GKLPikWMAPE 597
Cdd:cd14001    109 AATILkVALSIARALEYLHNeKKILHGDIKSGNVLIKGDfESVKLCDFGVSlPLTENLEVDSDPKaqyvGTEP--WKAKE 186
                          170       180
                   ....*....|....*....|....*
gi 1914779978  598 SINFRR-FTSASDVWMFGVCMWEIL 621
Cdd:cd14001    187 ALEEGGvITDKADIFAYGLVLWEMM 211
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
467-628 2.01e-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: 2.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  467 DSVREKFLQEALTMRQF-DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLES 544
Cdd:cd14181     56 EEVRSSTLKEIHILRQVsGHPSIITLIDSYeSSTFIFLVFDLMRRGELFDYL-TEKVTLSEKETRSIMRSLLEAVSYLHA 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  545 KRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRR------FTSASDVWMFGVCMW 618
Cdd:cd14181    135 NNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCGT-P-GYLAPEILKCSMdethpgYGKEVDLWACGVILF 212
                          170
                   ....*....|
gi 1914779978  619 EILMhGVKPF 628
Cdd:cd14181    213 TLLA-GSPPF 221
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
480-635 2.80e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 56.02  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  480 MRqfDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL 558
Cdd:PHA03390    65 MK--DNPNFIKLYYSVtTLKGHVLIMDYIKDGDLFDLLK-KEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVL 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  559 VS-SNDCVKLGDFGLSRY-----MEDST--YYkaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQg 630
Cdd:PHA03390   142 YDrAKDRIYLCDYGLCKIigtpsCYDGTldYF------------SPEKIKGHNYDVSFDWWAVGVLTYELLT-GKHPFK- 207

                   ....*
gi 1914779978  631 vKNND 635
Cdd:PHA03390   208 -EDED 211
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
456-676 3.58e-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: 3.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  456 VAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKL--IGVITENPVWIIMELctLG-ELRSFLQVRKYSLDLASLILY 531
Cdd:cd07856     38 VAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLsdIFISPLEDIYFVTEL--LGtDLHRLLTSRPLEKQFIQYFLY 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  532 ayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-TYYKASKgklpiKWMAPE-SINFRRFTSASD 609
Cdd:cd07856    116 --QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQmTGYVSTR-----YYRAPEiMLTWQKYDVEVD 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  610 VWMFGvCMWEILMHGVKPFQGvKNN----------------DVIGRI--ENG----------ERLPMP---PNCPPTLYS 658
Cdd:cd07856    189 IWSAG-CIFAEMLEGKPLFPG-KDHvnqfsiitellgtppdDVINTIcsENTlrfvqslpkrERVPFSekfKNADPDAID 266
                          250
                   ....*....|....*...
gi 1914779978  659 LMTKCWAYDPSRRPRFTE 676
Cdd:cd07856    267 LLEKMLVFDPKKRISAAE 284
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
424-630 4.04e-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: 4.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE----- 497
Cdd:cd07880     14 PDRYRDLKQVGSGAYGTV---CSALDRRTGAKVAIKKLyRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPdlsld 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 --NPVWIIMEL--CTLGELrsfLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 573
Cdd:cd07880     91 rfHDFYLVMPFmgTDLGKL---MKHEKLSEDRIQFLVY--QMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914779978  574 RYMEDSTyykasKGKLPIKWM-APESI-NFRRFTSASDVWMFGVCMWEILMhGVKPFQG 630
Cdd:cd07880    166 RQTDSEM-----TGYVVTRWYrAPEVIlNWMHYTQTVDIWSVGCIMAEMLT-GKPLFKG 218
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
426-686 4.62e-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: 4.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGiymSPENPALAVAIKTCKNcTSDSVREKFLQEALTMRQFD-HPHIVKLIGVITENP----- 499
Cdd:cd14036      1 KLRIKRVIAEGGFAFVYEA---QDVGTGKEYALKRLLS-NEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGKeesdq 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  500 ----VWIIMELCTLGELRSFLQVR-KYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd14036     77 gqaeYLLLTELCKGQLVDFVKKVEaPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGK------------LPIkWMAPESINFRR---FTSASDVWMFGvCMWEILMHGVKPFQ-GVKNndv 636
Cdd:cd14036    157 ATTEAHYPDYSWSAQKrslvedeitrntTPM-YRTPEMIDLYSnypIGEKQDIWALG-CILYLLCFRKHPFEdGAKL--- 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  637 igRIENGeRLPMPPNcpPTLYS----LMTKCWAYDPSRRPRFTELKAQLSTILE 686
Cdd:cd14036    232 --RIINA-KYTIPPN--DTQYTvfhdLIRSTLKVNPEERLSITEIVEQLQELAA 280
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
433-620 5.06e-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: 55.77  E-value: 5.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlGE 511
Cdd:cd07872     14 LGEGTYATVFKGRSKLTEN---LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVhTDKSLTLVFEYLD-KD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  512 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKASKGKLPI 591
Cdd:cd07872     90 LKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR--AKSVPTKTYSNEVVT 167
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1914779978  592 KWMAPESI--NFRRFTSASDVWMFGVCMWEI 620
Cdd:cd07872    168 LWYRPPDVllGSSEYSTQIDMWGVGCIFFEM 198
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
434-651 5.08e-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: 56.10  E-value: 5.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  434 GEGQFGDVHQGIymSPENPALaVAIKTCKNctsdsvREKFLQEA------LTM--RQFD---HPHIVKLIG-VITENPVW 501
Cdd:cd14212      8 GQGTFGQVVKCQ--DLKTNKL-VAVKVLKN------KPAYFRQAmleiaiLTLlnTKYDpedKHHIVRLLDhFMHHGHLC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 IIMELctLG-ELRSFLQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGlSRYME 577
Cdd:cd14212     79 IVFEL--LGvNLYELLKQNQFrGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSpeIKLIDFG-SACFE 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914779978  578 DSTYYKASKGKLpikWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIEngERLPMPPN 651
Cdd:cd14212    156 NYTLYTYIQSRF---YRSPEVLLGLPYSTAIDMWSLG-CIAAELFLGLPLFPGNSEYNQLSRII--EMLGMPPD 223
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
433-630 6.89e-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: 55.68  E-value: 6.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIymsPENPALAVAIKT-CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIME--LCTL 509
Cdd:cd07879     23 VGSGAYGSVCSAI---DKRTGEKVAIKKlSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQdfYLVM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLQ-VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyykasKGK 588
Cdd:cd07879    100 PYMQTDLQkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEM-----TGY 174
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1914779978  589 LPIKWM-APESI-NFRRFTSASDVWMFGVCMWEILmHGVKPFQG 630
Cdd:cd07879    175 VVTRWYrAPEVIlNWMHYNQTVDIWSVGCIMAEML-TGKTLFKG 217
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
428-677 6.98e-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: 6.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTC-KNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVI--TENPVWII 503
Cdd:cd14163      3 QLGKTIGEGTYSKVKEAFSKKHQR---KVAIKIIdKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLesADGKIYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  504 MELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDcVKLGDFGLSRYMEDSTYYK 583
Cdd:cd14163     80 MELAEDGDVFDCVLHGGPLPEHRAKALFR-QLVEAIRYCHGCGVAHRDLKCENALLQGFT-LKLTDFGFAKQLPKGGREL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  584 ASKGKLPIKWMAPESIN-FRRFTSASDVWMFGVCMWEILMHGVkPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTK 662
Cdd:cd14163    158 SQTFCGSTAYAAPEVLQgVPHDSRKGDIWSMGVVLYVMLCAQL-PFDDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKR 236
                          250
                   ....*....|....*
gi 1914779978  663 CWAYDPSRRPRFTEL 677
Cdd:cd14163    237 LLEPDMVLRPSIEEV 251
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
534-677 7.15e-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: 54.86  E-value: 7.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  534 QLSTALAYLESKRFVHRDIAARNVLVSS-NDCVKLGDFGLSRYMEDSTYYKASKGKLpikWMAPESINFRRFTS-ASDVW 611
Cdd:cd14101    116 QVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFGSGATLKDSMYTDFDGTRV---YSPPEWILYHQYHAlPATVW 192
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914779978  612 MFGVCMWEILMhGVKPFQgvKNNDVIgRIENGERLPMPPNCpptlYSLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14101    193 SLGILLYDMVC-GDIPFE--RDTDIL-KAKPSFNKRVSNDC----RSLIRSCLAYNPSDRPSLEQI 250
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
433-637 8.76e-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: 55.31  E-value: 8.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpaLAVAIKTCKNctSDSVREKFLQEALTMRQF------DHPHIVKLIGVIT-ENPVWIIME 505
Cdd:cd14135      8 LGKGVFSNVVRARDLARGN--QEVAIKIIRN--NELMHKAGLKELEILKKLndadpdDKKHCIRLLRHFEhKNHLCLVFE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  506 lCTLGELRSFLQV--RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KLGDFGLSRYMEDS--T 580
Cdd:cd14135     84 -SLSMNLREVLKKygKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFGSASDIGENeiT 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  581 YYKASKgklpiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVI 637
Cdd:cd14135    163 PYLVSR-----FYRAPEIILGLPYDYPIDMWSVGCTLYE-LYTGKILFPGKTNNHML 213
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-628 9.63e-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: 55.05  E-value: 9.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  424 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 502
Cdd:cd14168      9 KKIFEFKEVLGTGAFSEV---VLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYeSPNHLYL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  503 IMELCTLGELRSFLQVRKY--SLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRyME 577
Cdd:cd14168     86 VMQLVSGGELFDRIVEKGFytEKDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYFSQDeesKIMISDFGLSK-ME 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1914779978  578 DSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14168    162 GKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 210
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
414-628 1.34e-07

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 55.01  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  414 IDEARDYEIQRERIELGRCIGEGQFGDVhQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG 493
Cdd:cd05622     62 INKIRDLRMKAEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFY 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 VITENP-VWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd05622    141 AFQDDRyLYMVMEYMPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 218
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLPIKWMAPESINFR----RFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd05622    219 CMKMNKEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLV-GDTPF 277
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
426-678 1.54e-07

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: 54.00  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 504
Cdd:cd14662      1 RYELVKDIGSGNFGVAR---LMRNKETKELVAVKYIER--GLKIDENVQREIINHRSLRHPNIIRFKEVVlTPTHLAIVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  505 ELCTLGEL-RSFLQVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTY 581
Cdd:cd14662     76 EYAAGGELfERICNAGRFSEDEARY--FFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  582 YKASKGKlPiKWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPFQGVKN----NDVIGRIENGE-RLPMPPNCPPT 655
Cdd:cd14662    154 PKSTVGT-P-AYIAPEVLSRKEYDgKVADVWSCGVTLYVMLV-GAYPFEDPDDpknfRKTIQRIMSVQyKIPDYVRVSQD 230
                          250       260
                   ....*....|....*....|...
gi 1914779978  656 LYSLMTKCWAYDPSRRPRFTELK 678
Cdd:cd14662    231 CRHLLSRIFVANPAKRITIPEIK 253
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
485-620 1.62e-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: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  485 HPHIVKLIGV-----ITENPVWIIMELCTLGELRSFLQVRKYSLDlaSLILYAYQLSTALAYLESK----------RFVH 549
Cdd:cd14141     48 HENILQFIGAekrgtNLDVDLWLITAFHEKGSLTDYLKANVVSWN--ELCHIAQTMARGLAYLHEDipglkdghkpAIAH 125
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914779978  550 RDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI-KWMAPE----SINFRRFTSAS-DVWMFGVCMWEI 620
Cdd:cd14141    126 RDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTrRYMAPEvlegAINFQRDAFLRiDMYAMGLVLWEL 202
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
433-628 1.76e-07

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: 53.43  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVItENPV--WIIMELCTLG 510
Cdd:cd14115      1 IGRGRFSIVKKCLHKATRKD---VAVKFVSKKMKK--KEQAAHEAALLQHLQHPQYITLHDTY-ESPTsyILVLELMDDG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  511 ELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---SNDCVKLGDFGLSryMEDSTYYKASKG 587
Cdd:cd14115     75 RLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDA--VQISGHRHVHHL 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1914779978  588 KLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 628
Cdd:cd14115    152 LGNPEFAAPEVIQGTPVSLATDIWSIGVLTY-VMLSGVSPF 191
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
423-574 1.83e-07

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 54.05  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  423 QRERIELgrcIGEGQFGDVHQGiymSPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPV 500
Cdd:PLN00009     3 QYEKVEK---IGEGTYGVVYKA---RDRVTNETIALKKIRLEQEDEgVPSTAIREISLLKEMQHGNIVRLQDVVhSEKRL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914779978  501 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-SNDCVKLGDFGLSR 574
Cdd:PLN00009    77 YLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLAR 151
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
484-635 1.90e-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: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  484 DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 562
Cdd:cd05618     79 NHPFLVGLHSCFqTESRLFFVIEYVNGGDLMFHMQ-RQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE 157
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914779978  563 DCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNND 635
Cdd:cd05618    158 GHIKLTDYGMCKEGLRPGDTTSTFCGTP-NYIAPEILRGEDYGFSVDWWALGVLMFE-MMAGRSPFDIVGSSD 228
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
433-661 2.10e-07

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: 53.42  E-value: 2.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  433 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREkflQEALTMRQFD-HPHIVKLIGVITENPV-WIIMELC--T 508
Cdd:cd14017      8 IGGGGFGEIYKVRDVVDGE---EVAMKVESKSQPKQVLK---MEVAVLKKLQgKPHFCRLIGCGRTERYnYIVMTLLgpN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  509 LGELRSFLQVRKYSLdlASLILYAYQLSTALAYLESKRFVHRDIAARNVL--VSSNDC--VKLGDFGLSRymedstYYKA 584
Cdd:cd14017     82 LAELRRSQPRGKFSV--STTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAigRGPSDErtVYILDFGLAR------QYTN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  585 SKGKlpIKWMAPESINFR---RFTSAS-----------DVWMFGVCMWEiLMHGVKPFQGVKNNDVIG----RIENGERL 646
Cdd:cd14017    154 KDGE--VERPPRNAAGFRgtvRYASVNahrnkeqgrrdDLWSWFYMLIE-FVTGQLPWRKLKDKEEVGkmkeKIDHEELL 230
                          250
                   ....*....|....*
gi 1914779978  647 pmpPNCPPTLYSLMT 661
Cdd:cd14017    231 ---KGLPKEFFQILK 242
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
428-677 2.30e-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: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  428 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKtckNCTSDSVRE--------KFLQEALTMRQFDHPH--IVKLIGVItE 497
Cdd:cd14100      3 QVGPLLGSGGFGSVYSGIRVADGAP---VAIK---HVEKDRVSEwgelpngtRVPMEIVLLKKVGSGFrgVIRLLDWF-E 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  498 NP---VWIIMELCTLGELRSFLQVR-KYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-VKLGDFGL 572
Cdd:cd14100     76 RPdsfVLVLERPEPVQDLFDFITERgALPEELARS--FFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGeLKLIDFGS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLpikWMAPESINFRRFTSAS-DVWMFGVCMWEILMhGVKPFQgvkNNDVIGRIENGERLPMPPN 651
Cdd:cd14100    154 GALLKDTVYTDFDGTRV---YSPPEWIRFHRYHGRSaAVWSLGILLYDMVC-GDIPFE---HDEEIIRGQVFFRQRVSSE 226
                          250       260
                   ....*....|....*....|....*.
gi 1914779978  652 CPptlySLMTKCWAYDPSRRPRFTEL 677
Cdd:cd14100    227 CQ----HLIKWCLALRPSDRPSFEDI 248
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
414-628 2.53e-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: 54.24  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  414 IDEARDYEIQRERIELGRCIGEGQFGDVhQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG 493
Cdd:cd05621     41 VNKIRELQMKAEDYDVVKVIGRGAFGEV-QLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFC 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  494 VIT-ENPVWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 572
Cdd:cd05621    120 AFQdDKYLYMVMEYMPGGDLVNLMS--NYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGT 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  573 SRYMEDSTYYKASKGKLPIKWMAPESINFR----RFTSASDVWMFGVCMWEILMhGVKPF 628
Cdd:cd05621    198 CMKMDETGMVHCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLV-GDTPF 256
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
496-679 2.58e-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: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  496 TENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 575
Cdd:cd05617     87 TTSRLFLVIEYVNGGDLMFHMQ-RQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKE 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  576 MEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIgriengerlpmppNCPPT 655
Cdd:cd05617    166 GLGPGDTTSTFCGTP-NYIAPEILRGEEYGFSVDWWALGVLMFE-MMAGRSPFDIITDNPDM-------------NTEDY 230
                          170       180
                   ....*....|....*....|....
gi 1914779978  656 LYSLMTKcwayDPSRRPRFTELKA 679
Cdd:cd05617    231 LFQVILE----KPIRIPRFLSVKA 250
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
485-717 3.46e-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: 53.26  E-value: 3.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  485 HPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYslDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 562
Cdd:cd05591     55 HPFLTALHSCFqTKDRLFFVMEYVNGGDLMFQIQrARKF--DEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  563 DCVKLGDFGLSR--YMEDSTyyKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI 640
Cdd:cd05591    133 GHCKLADFGMCKegILNGKT--TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYE-MMAGQPPFEADNEDDLFESI 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  641 ENGERL-P--MPPNCPPTLYSLMTKcwayDPSRR----------------PRFTELKAQLstiLEEEKAQQEERMRMESR 701
Cdd:cd05591    209 LHDDVLyPvwLSKEAVSILKAFMTK----NPAKRlgcvasqggedairqhPFFREIDWEA---LEQRKVKPPFKPKIKTK 281
                          250
                   ....*....|....*.
gi 1914779978  702 RQATvSWDSGGSDEAP 717
Cdd:cd05591    282 RDAN-NFDQDFTKEEP 296
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
436-621 3.73e-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: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  436 GQFGDVHQGIYMspeNPALAVAIKTCKNCTS-DSVREKFLQEALTmrqfdHPHIVKLI-----GVITENPVWIIMELCTL 509
Cdd:cd14140      6 GRFGCVWKAQLM---NEYVAVKIFPIQDKQSwQSEREIFSTPGMK-----HENLLQFIaaekrGSNLEMELWLITAFHDK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  510 GELRSFLqvRKYSLDLASLILYAYQLSTALAYLESK-----------RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 578
Cdd:cd14140     78 GSLTDYL--KGNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEP 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1914779978  579 STYYKASKGKLPI-KWMAPE----SINFRRFTSAS-DVWMFGVCMWEIL 621
Cdd:cd14140    156 GKPPGDTHGQVGTrRYMAPEvlegAINFQRDSFLRiDMYAMGLVLWELV 204
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
531-653 4.03e-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: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  531 YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS-RYMEDSTYYKASKGKLPiKWMAPESINFR-----RF 604
Cdd:cd05597    107 YLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClKLREDGTVQSSVAVGTP-DYISPEILQAMedgkgRY 185
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1914779978  605 TSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIEN-GERLPMPPNCP 653
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; ...
426-586 4.23e-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: 4.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  426 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTcknctsDSVREKFLQEALTMRqfdhphIVKLI--GVITENPVW-- 501
Cdd:cd14125      1 KYRLGRKIGSGSFGDIYLGTNIQTGEE---VAIKL------ESVKTKHPQLLYESK------LYKILqgGVGIPNVRWyg 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  502 -------IIMELC--TLGELRSFLQvRKYSLDlaSLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---SNDCVKLGD 569
Cdd:cd14125     66 vegdynvMVMDLLgpSLEDLFNFCS-RKFSLK--TVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGlgkKGNLVYIID 142
                          170       180
                   ....*....|....*....|..
gi 1914779978  570 FGLS-RYMEDSTY----YKASK 586
Cdd:cd14125    143 FGLAkKYRDPRTHqhipYRENK 164
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
447-671 4.95e-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: 4.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  447 MSPENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQFD-HPHIVKLIGVITENPVWIIMELCTLGELrsfLQVRKYSLD 524
Cdd:cd14020     23 RGADQPTSALKEFQLDHQGSQESGDYgFAKERAALEQLQgHRNIVTLYGVFTNHYSANVPSRCLLLEL---LDVSVSELL 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  525 LAS--------LILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGLS--RYMEDSTY-----YKASKG 587
Cdd:cd14020    100 LRSsnqgcsmwMIQHcARDVLEALAFLHHEGYVHADLKPRNILWSAEDeCFKLIDFGLSfkEGNQDVKYiqtdgYRAPEA 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914779978  588 KLPIKWMAPESINFRRFTSASDVWMFGVCMWEI-----LMHGVKPfQGVKNND--VIGRIENGERLPMPPNCPPTLYSLM 660
Cdd:cd14020    180 ELQNCLAQAGLQSETECTSAVDLWSLGIVLLEMfsgmkLKHTVRS-QEWKDNSsaIIDHIFASNAVVNPAIPAYHLRDLI 258
                          250
                   ....*....|.
gi 1914779978  661 TKCWAYDPSRR 671
Cdd:cd14020    259 KSMLHNDPGKR 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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