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Conserved domains on  [gi|5031869|ref|NP_005560|]
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LIM domain kinase 2 isoform 2a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
337-608 0e+00

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: 596.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLR 496
Cdd:cd14222  81 LRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDKPTTKKRTLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  497 KNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAF 576
Cdd:cd14222 161 KNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVRLFWEKFVPKDCPPAF 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  577 FPLAAICCRLEPESRPAFSKLEDSFEALSLYL 608
Cdd:cd14222 241 FPLAAICCRLEPDSRPAFSKLEDSFEALSLYL 272
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
147-239 1.71e-46

PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the LIMK protein family, and related domains. The LIMK family is composed of LIMK1 and LIMK2, which are common downstream effectors of several signalization pathways and function as signaling nodes that control cytoskeleton dynamics through the phosphorylation of cofilin family proteins. They also control microtubule dynamics. The LIMK1 PDZ domain binds tubulin and nischarin. LIMK1 also binds a carboxy-terminal motif of membrane type 1-matrix metalloproteinase (MT1-MMP, also known as MMP14) having features of a PDZ domain-binding site; MT1-MMP is a major protease involved in dissemination of carcinoma cells during cancer progression. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LIMK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467236 [Multi-domain]  Cd Length: 92  Bit Score: 158.97  E-value: 1.71e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  147 PYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRnAIHPGDRILEINGTPVRTLRVEEVEDAISQ 226
Cdd:cd06754   1 PHSVTLVSIPPTPEGKRGFSVSVEKGCSEHSHTVRVSELDPMHLSPDLK-SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
                        90
                ....*....|...
gi 5031869  227 TSQTLQLLIEHDP 239
Cdd:cd06754  80 TSKTLQLTIEHDP 92
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
67-125 7.52e-39

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 136.99  E-value: 7.52e-39
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869   67 KFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCH 125
Cdd:cd09465   1 KFGELCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGDTYALVQHTTLYCGKCH 59
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
12-65 5.25e-33

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 120.36  E-value: 5.25e-33
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   12 CPGCGDHIAPSQiWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYW 65
Cdd:cd09463   1 CTGCGGRIQDSF-HYRVVQEAWHNSCFQCSVCQDLLTNWYYEKDGKLYCHKHYW 53
 
Name Accession Description Interval E-value
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
337-608 0e+00

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: 596.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLR 496
Cdd:cd14222  81 LRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDKPTTKKRTLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  497 KNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAF 576
Cdd:cd14222 161 KNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVRLFWEKFVPKDCPPAF 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  577 FPLAAICCRLEPESRPAFSKLEDSFEALSLYL 608
Cdd:cd14222 241 FPLAAICCRLEPDSRPAFSKLEDSFEALSLYL 272
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
334-601 2.65e-63

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 210.10  E-value: 2.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     334 GEVLGKGFFGqaiKVtHKATGKVMVMKELIRC---------DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:smart00221   4 GKKLGEGAFG---EV-YKGTLKGKGDGKEVEVavktlkedaSEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     405 TEYIEGGTLKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkr 482
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     483 apMEKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YadPDCLPRTLDFGLN 559
Cdd:smart00221 158 --YYKVKGGKLPIR---------------WMAPESLKEGKFTSKSDVWSFGVLLWEIFtlGEEpY--PGMSNAEVLEYLK 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 5031869     560 VKLFWEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:smart00221 219 KGYRLPK--PPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
334-597 8.65e-56

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 190.02  E-value: 8.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    334 GEVLGKGFFGQ---AIKVTHKATGKVMV----MKEliRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:pfam07714   4 GEKLGEGAFGEvykGTLKGEGENTKIKVavktLKE--GADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    407 YIEGGTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapM 485
Cdd:pfam07714  82 YMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDI--------Y 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    486 EKATTKKRTLRKndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YADPDC------------L 550
Cdd:pfam07714 154 DDDYYRKRGGGK----------LPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFtlGEQpYPGMSNeevlefledgyrL 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 5031869    551 PRtldfglnvklfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:pfam07714 224 PQ----------------PENCPDELYDLMKQCWAYDPEDRPTFSEL 254
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
147-239 1.71e-46

PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the LIMK protein family, and related domains. The LIMK family is composed of LIMK1 and LIMK2, which are common downstream effectors of several signalization pathways and function as signaling nodes that control cytoskeleton dynamics through the phosphorylation of cofilin family proteins. They also control microtubule dynamics. The LIMK1 PDZ domain binds tubulin and nischarin. LIMK1 also binds a carboxy-terminal motif of membrane type 1-matrix metalloproteinase (MT1-MMP, also known as MMP14) having features of a PDZ domain-binding site; MT1-MMP is a major protease involved in dissemination of carcinoma cells during cancer progression. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LIMK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467236 [Multi-domain]  Cd Length: 92  Bit Score: 158.97  E-value: 1.71e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  147 PYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRnAIHPGDRILEINGTPVRTLRVEEVEDAISQ 226
Cdd:cd06754   1 PHSVTLVSIPPTPEGKRGFSVSVEKGCSEHSHTVRVSELDPMHLSPDLK-SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
                        90
                ....*....|...
gi 5031869  227 TSQTLQLLIEHDP 239
Cdd:cd06754  80 TSKTLQLTIEHDP 92
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
335-593 4.81e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 153.24  E-value: 4.81e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEETQKTFLTEVKVMRSLDHPNVLKFI------GVLYkdkklnLLT 405
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGRPVALKVLrpeLAADPEARERFRREARALARLNHPNIVRVYdvgeedGRPY------LVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPM 485
Cdd:COG0515  87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  486 ekattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVKLFW 564
Cdd:COG0515 167 -------------------TVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLtGRPPFDGDSPAELLRAHLREPPPP 227
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  565 EKFVPTDCPPAffpLAAICCRL---EPESRPA 593
Cdd:COG0515 228 PSELRPDLPPA---LDAIVLRAlakDPEERYQ 256
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
67-125 7.52e-39

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 136.99  E-value: 7.52e-39
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869   67 KFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCH 125
Cdd:cd09465   1 KFGELCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGDTYALVQHTTLYCGKCH 59
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
12-65 5.25e-33

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 120.36  E-value: 5.25e-33
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   12 CPGCGDHIAPSQiWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYW 65
Cdd:cd09463   1 CTGCGGRIQDSF-HYRVVQEAWHNSCFQCSVCQDLLTNWYYEKDGKLYCHKHYW 53
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
330-540 5.08e-23

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 100.66  E-value: 5.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMK-----ELIRCDEetQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKclkkrEILKMKQ--VQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAP 484
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA-------KKVP 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869   485 mekattkKRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:PTZ00263 170 -------DRT---------FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFI 209
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
345-543 1.21e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 99.10  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   345 AIKVTHKatgkvmvmkELIRcDEETQKTFLTEVKVMRSLDHPNVlkfIGVlY---KDKKLN-LLTEYIEGGTLKDFLRSM 420
Cdd:NF033483  36 AVKVLRP---------DLAR-DPEFVARFRREAQSAASLSHPNI---VSV-YdvgEDGGIPyIVMEYVDGRTLKDYIREH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   421 DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekaTTKKRTlrkNdr 500
Cdd:NF033483 102 GPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSS----------TTMTQT---N-- 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 5031869   501 kkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV 543
Cdd:NF033483 167 ----SVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLtGRP 206
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
152-236 3.56e-17

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 76.55  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    152 LISMPATTEGRRGFSVSVESACSnyATTVQVKEVNRMhiSPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTL 231
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQG--DPGIFVSEVLPG--GAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKV 76

                  ....*
gi 5031869    232 QLLIE 236
Cdd:pfam00595  77 TLTIL 81
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
12-68 8.14e-15

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 68.90  E-value: 8.14e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869     12 CPGCGDHIAPSQIwYRTVNETWHGSCFRCSECQDSLTNW-YYEKDGKLYCPKDYWGKF 68
Cdd:pfam00412   1 CAGCNRPIYDREL-VRALGKVWHPECFRCAVCGKPLTTGdFYEKDGKLYCKHDYYKLF 57
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
11-63 4.26e-14

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 67.02  E-value: 4.26e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 5031869      11 RCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTN-WYYEKDGKLYCPKD 63
Cdd:smart00132   1 KCAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLSGdTFFEKDGKLYCKDC 54
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
159-239 1.60e-09

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 55.08  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     159 TEGRRGFSVSVESACSNYattVQVKEVnrMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHD 238
Cdd:smart00228  10 GGGGLGFSLVGGKDEGGG---VVVSSV--VPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRG 84

                   .
gi 5031869     239 P 239
Cdd:smart00228  85 G 85
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
72-125 2.31e-07

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 47.71  E-value: 2.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869     72 CHGCSLLMTGPFMV-AGEFKYHPECFACMSCKVIIEDGDAYalVQHATLYCGKCH 125
Cdd:pfam00412   1 CAGCNRPIYDRELVrALGKVWHPECFRCAVCGKPLTTGDFY--EKDGKLYCKHDY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
72-124 2.33e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 45.07  E-value: 2.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869      72 CHGCSLLMTG--PFMVAGEFKYHPECFACMSCKVIIEDGDAYalVQHATLYCGKC 124
Cdd:smart00132   2 CAGCGKPIYGteRVLRALGKVWHPECFKCATCGKPLSGDTFF--EKDGKLYCKDC 54
 
Name Accession Description Interval E-value
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
337-608 0e+00

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: 596.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLR 496
Cdd:cd14222  81 LRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDKPTTKKRTLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  497 KNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAF 576
Cdd:cd14222 161 KNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVRLFWEKFVPKDCPPAF 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  577 FPLAAICCRLEPESRPAFSKLEDSFEALSLYL 608
Cdd:cd14222 241 FPLAAICCRLEPDSRPAFSKLEDSFEALSLYL 272
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
337-608 0e+00

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: 560.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSM-DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTL 495
Cdd:cd14154  81 LKDMaRPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLPSGNMSPSETLRHL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  496 RKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPtDCPPA 575
Cdd:cd14154 161 KSPDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPRTKDFGLNVDSFREKFCA-GCPPP 239
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031869  576 FFPLAAICCRLEPESRPAFSKLEDSFEALSLYL 608
Cdd:cd14154 240 FFKLAFLCCDLDPEKRPPFETLEEWLEALYLHL 272
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
337-608 1.08e-157

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: 453.64  E-value: 1.08e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPmekattKKRTL 495
Cdd:cd14221  81 IKSMDShYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPE------GLRSL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  496 RKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPA 575
Cdd:cd14221 155 KKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPS 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031869  576 FFPLAAICCRLEPESRPAFSKLEDSFEALSLYL 608
Cdd:cd14221 235 FFPIAVLCCDLDPEKRPSFSKLEHWLETLRMHL 267
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
337-599 9.55e-127

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: 374.14  E-value: 9.55e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEetQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDE--QRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL---DKTVVVADFGLSRLIVEERKRAPmekattkk 492
Cdd:cd14065  79 LKSMDeQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGRNAVVADFGLAREMPDEKTKKP-------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrknDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPtDC 572
Cdd:cd14065 151 ------DRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFGLDVRAFRTLYVP-DC 223
                       250       260
                ....*....|....*....|....*..
gi 5031869  573 PPAFFPLAAICCRLEPESRPAFSKLED 599
Cdd:cd14065 224 PPSFLPLAIRCCQLDPEKRPSFVELEH 250
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
337-604 9.29e-87

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: 271.27  E-value: 9.29e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKelIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALK--MNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK---TVVVADFGLSRLIveerkraPMEKattkkr 493
Cdd:cd14155  79 LDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKI-------PDYS------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 tlrknDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFwEKFVPtDCP 573
Cdd:cd14155 146 -----DGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLDYDAF-QHMVG-DCP 218
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031869  574 PAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14155 219 PDFLQLAFNCCNMDPKSRPSFHDIVKTLEEI 249
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
337-601 3.39e-81

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: 256.31  E-value: 3.39e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKatGKVMVMKELI--RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLKveDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkraPMEKATtkkr 493
Cdd:cd13999  79 DLLHKKKiPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNS-----TTEKMT---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 tlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFwEKFVPTDCP 573
Cdd:cd13999 150 -----------GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGL-RPPIPPDCP 217
                       250       260
                ....*....|....*....|....*...
gi 5031869  574 PAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:cd13999 218 PELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
337-605 1.35e-79

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: 252.83  E-value: 1.35e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKelIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVK--IYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTV---VVADFGLSRLIVEerkrapmekattkk 492
Cdd:cd14156  79 LAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGreaVVTDFGLAREVGE-------------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKfVPtDC 572
Cdd:cd14156 145 --MPANDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFGLDVQAFKEM-VP-GC 220
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031869  573 PPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd14156 221 PEPFLDLAASCCRMDAFKRPSFAELLDELEDIA 253
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
334-601 2.65e-63

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 210.10  E-value: 2.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     334 GEVLGKGFFGqaiKVtHKATGKVMVMKELIRC---------DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:smart00221   4 GKKLGEGAFG---EV-YKGTLKGKGDGKEVEVavktlkedaSEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     405 TEYIEGGTLKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkr 482
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     483 apMEKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YadPDCLPRTLDFGLN 559
Cdd:smart00221 158 --YYKVKGGKLPIR---------------WMAPESLKEGKFTSKSDVWSFGVLLWEIFtlGEEpY--PGMSNAEVLEYLK 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 5031869     560 VKLFWEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:smart00221 219 KGYRLPK--PPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
334-601 3.86e-62

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 206.61  E-value: 3.86e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     334 GEVLGKGFFGQAIK---VTHKATGKVMV----MKEliRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:smart00219   4 GKKLGEGAFGEVYKgklKGKGGKKKVEVavktLKE--DASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     407 YIEGGTLKDFLRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkrapM 485
Cdd:smart00219  82 YMEGGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD----Y 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     486 EKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVYAdPDCLPRTLDFGLNVKLF 563
Cdd:smart00219 158 YRKRGGKLPIR---------------WMAPESLKEGKFTSKSDVWSFGVLLWEIFtlGEQPY-PGMSNEEVLEYLKNGYR 221
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 5031869     564 WEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:smart00219 222 LPQ--PPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
335-602 1.08e-61

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: 205.85  E-value: 1.08e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIK--VTHKATGKVMV-MKELIRC-DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd00192   1 KKLGEGAFGEVYKgkLKGGDGKTVDVaVKTLKEDaSESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSM---------DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERK 481
Cdd:cd00192  81 GDLLDFLRKSrpvfpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  482 RapmEKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV----YADPDCLPRTLD 555
Cdd:cd00192 161 Y---RKKTGGKLPIR---------------WMAPESLKDGIFTSKSDVWSFGVLLWEIFtlGATpypgLSNEEVLEYLRK 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  556 FGLNVKlfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd00192 223 GYRLPK-------PENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
334-592 5.48e-59

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 198.14  E-value: 5.48e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     334 GEVLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:smart00220   4 LEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkk 492
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL---------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     493 rtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRTLDFGLNVKLFWEKFVPt 570
Cdd:smart00220 148 -----DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLtGKPpFPGDDQLLELFKKIGKPKPPFPPPEW- 221
                          250       260
                   ....*....|....*....|..
gi 5031869     571 DCPPAFFPLAAICCRLEPESRP 592
Cdd:smart00220 222 DISPEAKDLIRKLLVKDPEKRL 243
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
334-597 8.65e-56

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 190.02  E-value: 8.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    334 GEVLGKGFFGQ---AIKVTHKATGKVMV----MKEliRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:pfam07714   4 GEKLGEGAFGEvykGTLKGEGENTKIKVavktLKE--GADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    407 YIEGGTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapM 485
Cdd:pfam07714  82 YMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDI--------Y 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    486 EKATTKKRTLRKndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YADPDC------------L 550
Cdd:pfam07714 154 DDDYYRKRGGGK----------LPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFtlGEQpYPGMSNeevlefledgyrL 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 5031869    551 PRtldfglnvklfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:pfam07714 224 PQ----------------PENCPDELYDLMKQCWAYDPEDRPTFSEL 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
337-539 2.09e-54

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: 184.78  E-value: 2.09e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEeLLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRS-MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekattkkrt 494
Cdd:cd00180  81 LLKEnKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDS---------------- 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  495 lrKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd00180 145 --DDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
147-239 1.71e-46

PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the LIMK protein family, and related domains. The LIMK family is composed of LIMK1 and LIMK2, which are common downstream effectors of several signalization pathways and function as signaling nodes that control cytoskeleton dynamics through the phosphorylation of cofilin family proteins. They also control microtubule dynamics. The LIMK1 PDZ domain binds tubulin and nischarin. LIMK1 also binds a carboxy-terminal motif of membrane type 1-matrix metalloproteinase (MT1-MMP, also known as MMP14) having features of a PDZ domain-binding site; MT1-MMP is a major protease involved in dissemination of carcinoma cells during cancer progression. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LIMK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467236 [Multi-domain]  Cd Length: 92  Bit Score: 158.97  E-value: 1.71e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  147 PYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRnAIHPGDRILEINGTPVRTLRVEEVEDAISQ 226
Cdd:cd06754   1 PHSVTLVSIPPTPEGKRGFSVSVEKGCSEHSHTVRVSELDPMHLSPDLK-SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
                        90
                ....*....|...
gi 5031869  227 TSQTLQLLIEHDP 239
Cdd:cd06754  80 TSKTLQLTIEHDP 92
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
330-601 4.81e-46

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: 163.46  E-value: 4.81e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEveLSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEk 487
Cdd:cd06606  81 VPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTK- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  488 attkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII---------GQVYA---------DPDC 549
Cdd:cd06606 160 -----------------SLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMAtgkppwselGNPVAalfkigssgEPPP 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  550 LPRTLDFGLnvKLFWEKfvptdcppaffplaaiCCRLEPESRP-AFSKLEDSF 601
Cdd:cd06606 223 IPEHLSEEA--KDFLRK----------------CLQRDPKKRPtADELLQHPF 257
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
334-536 2.55e-45

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: 161.49  E-value: 2.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKeLI---RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05117   5 GKVLGRGSFGVVRLAVHKKTGEEYAVK-IIdkkKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIK---LDKTVVVADFGLSRLIveerkrapmek 487
Cdd:cd05117  84 GELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAKIF----------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  488 attkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd05117 153 ----------EEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVIL 191
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
335-538 3.52e-45

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: 161.09  E-value: 3.52e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRC---DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd08215   6 RVIGKGSFGSAYLVRRKSDGKLYVLKE-IDLsnmSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TL----KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlIVEErkraPMEK 487
Cdd:cd08215  85 DLaqkiKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK-VLES----TTDL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  488 ATtkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd08215 160 AK---------------TVVGTPYYLSPELCENKPYNYKSDIWALGCVLYE 195
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
335-593 8.83e-44

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: 157.36  E-value: 8.83e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14014   6 RLLGRGGMGEVYRARDTLLGRPVAIKVLrpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapmEKATTK 491
Cdd:cd14014  86 SLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARA----------LGDSGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 KRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVKLFWEKFVPT 570
Cdd:cd14014 156 TQT---------GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLtGRPPFDGDSPAAVLAKHLQEAPPPPSPLNP 226
                       250       260
                ....*....|....*....|...
gi 5031869  571 DCPPAFFPLAAICCRLEPESRPA 593
Cdd:cd14014 227 DVPPALDAIILRALAKDPEERPQ 249
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
335-538 3.47e-43

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: 155.82  E-value: 3.47e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd05122   6 EKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGSLK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRS-MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapmekattkkr 493
Cdd:cd05122  86 DLLKNtNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSA------------------- 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  494 tlRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd05122 147 --QLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIE 189
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
334-592 3.14e-41

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: 150.32  E-value: 3.14e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEETQktFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14007   5 GKPLGKGKFGNVYLAREKKSGfivalKVISKSQLQKSGLEHQ--LRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmeka 488
Cdd:cd14007  83 PNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWS--------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 ttkkrtlRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVKLFWEKF 567
Cdd:cd14007 148 -------VHAPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLvGKPPFESKSHQETYKRIQNVDIKFPSS 220
                       250       260
                ....*....|....*....|....*
gi 5031869  568 VptdcPPAFFPLAAICCRLEPESRP 592
Cdd:cd14007 221 V----SPEAKDLISKLLQKDPSKRL 241
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
335-540 7.08e-41

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: 149.28  E-value: 7.08e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06614   6 EKIGEGASGEVYKATDRATGKEVAIKK-MRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkkr 493
Cdd:cd06614  85 DIITqNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKS------------ 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  494 tlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06614 153 --------KRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMA 191
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
337-604 2.22e-40

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: 148.57  E-value: 2.22e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKaTGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIG-VLYKDKKLnLLTEYIEGGTLK 414
Cdd:cd14066   1 IGSGGFGTVYKGVLE-NGTVVAVKRLnEMNCAASKKEFLTELEMLGRLRHPNLVRLLGyCLESDEKL-LVYEYMPNGSLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFL---RSMDPFPWQQKVRFAKGIASGMAYLHSMC---IIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKA 488
Cdd:cd14066  79 DRLhchKGSPPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSAV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TtkkrtlrkndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPDCLPRTLD-----FGLNVKL 562
Cdd:cd14066 159 K------------------GTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLtGKPAVDENRENASRKdlvewVESKGKE 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  563 FWEKF----------VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14066 221 ELEDIldkrlvdddgVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
335-593 4.81e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 153.24  E-value: 4.81e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEETQKTFLTEVKVMRSLDHPNVLKFI------GVLYkdkklnLLT 405
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGRPVALKVLrpeLAADPEARERFRREARALARLNHPNIVRVYdvgeedGRPY------LVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPM 485
Cdd:COG0515  87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  486 ekattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVKLFW 564
Cdd:COG0515 167 -------------------TVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLtGRPPFDGDSPAELLRAHLREPPPP 227
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  565 EKFVPTDCPPAffpLAAICCRL---EPESRPA 593
Cdd:COG0515 228 PSELRPDLPPA---LDAIVLRAlakDPEERYQ 256
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
67-125 7.52e-39

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 136.99  E-value: 7.52e-39
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869   67 KFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCH 125
Cdd:cd09465   1 KFGELCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGDTYALVQHTTLYCGKCH 59
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
337-540 8.92e-39

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: 143.43  E-value: 8.92e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-----IRCDEETQktFLTEVKVMRSLDHPNVLKfigvLYK----DKKLNLLTEY 407
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLrkkeiIKRKEVEH--TLNERNILERVNHPFIVK----LHYafqtEEKLYLVLDY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApme 486
Cdd:cd05123  75 VPGGELFSHLSKEGRFP-EERARFyAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRT--- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  487 kattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05123 151 -----------------YTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEML 187
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
335-601 5.29e-38

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: 141.63  E-value: 5.29e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKtFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06612   9 EKLGEGSYGSVYKAIHKETGQVVAIK-VVPVEEDLQE-IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGSVS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSM-DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkkr 493
Cdd:cd06612  87 DIMKITnKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMA------------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 tlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI------------IGQVYADPDCLPRTLDfglnvk 561
Cdd:cd06612 155 --------KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMaegkppysdihpMRAIFMIPNKPPPTLS------ 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031869  562 lfwekfVPTDCPPAFFPLAAICCRLEPESRP-AFSKLEDSF 601
Cdd:cd06612 221 ------DPEKWSPEFNDFVKKCLVKDPEERPsAIQLLQHPF 255
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
334-536 1.17e-37

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: 140.35  E-value: 1.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14003   5 GKTLGEGSFGKVKLARHKLTGEKVAIKiiDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattk 491
Cdd:cd14003  85 ELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF--------------- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  492 krtlRKNDRKKryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14003 150 ----RGGSLLK--TFCGTPAYAAPEVLLGRKYDgPKADVWSLGVIL 189
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
337-604 4.74e-37

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: 139.82  E-value: 4.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHK----ATGKVMVMKELIR-CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKD--KKLNLLTEYIE 409
Cdd:cd05038  12 LGEGHFGSVELCRYDplgdNTGEQVAVKSLQPsGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLIMEYLP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSM-DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmeka 488
Cdd:cd05038  92 SGSLRDYLQRHrDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPE---------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 ttkkrtlrkndrKKRYTVVGNP-----YWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADPDCLPRTLDFGLNVKLF 563
Cdd:cd05038 162 ------------DKEYYYVKEPgespiFWYAPECLRESRFSSASDVWSFGVTLYELF--TYGDPSQSPPALFLRMIGIAQ 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  564 WEKFV---------------PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05038 228 GQMIVtrllellksgerlprPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRL 283
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
330-604 5.58e-37

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: 138.64  E-value: 5.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKatGKVMVMKELiRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd05039   7 DLKLGELIGKGEFGDVMLGDYR--GQKVAVKCL-KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEERKRAPMEK 487
Cdd:cd05039  84 KGSLVDYLRSRGRavITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK---EASSNQDGGK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  488 ATTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEI--IGQV-YadpdclPRT--LDFGLNVKL 562
Cdd:cd05039 161 LPIK--------------------WTAPEALREKKFSTKSDVWSFGILLWEIysFGRVpY------PRIplKDVVPHVEK 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 5031869  563 FWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05039 215 GYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
335-604 9.29e-37

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: 138.27  E-value: 9.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05033  10 KVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLkSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMEN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPMEKAT 489
Cdd:cd05033  90 GSLDKFLRENDgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSR-----RLEDSEATYT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 TK--KRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIGqvYADpdclprtldfglnvKLFWE-- 565
Cdd:cd05033 165 TKggKIPIR---------------WTAPEAIAYRKFTSASDVWSFGIVMWEVMS--YGE--------------RPYWDms 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  566 -----KFV--------PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05033 214 nqdviKAVedgyrlppPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
332-539 1.77e-36

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: 137.95  E-value: 1.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEvLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd06611   9 IIGE-LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekatt 490
Cdd:cd06611  88 ALDSIMLELErGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVS----------------- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  491 kkrTLRKNDRKKRYTVVGNPYWMAPEMLNGKS-----YDETVDIFSFGIVLCEI 539
Cdd:cd06611 151 ---AKNKSTLQKRDTFIGTPYWMAPEVVACETfkdnpYDYKADIWSLGITLIEL 201
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
375-594 2.94e-36

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: 136.09  E-value: 2.94e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  375 TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNS 454
Cdd:cd14059  30 TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKS 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  455 HNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGI 534
Cdd:cd14059 110 PNVLVTYNDVLKISDFGTSKEL---------------------SEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGV 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  535 VLCEII-GQV-YADPDCLPRTLDFGLN-VKLfwekFVPTDCPPAFFPLAAICCRLEPESRPAF 594
Cdd:cd14059 169 VLWELLtGEIpYKDVDSSAIIWGVGSNsLQL----PVPSTCPDGFKLLMKQCWNSKPRNRPSF 227
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
336-538 6.12e-36

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: 135.80  E-value: 6.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06623   8 VLGQGSSGVVYKVRHKPTGKIYALKKIhVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVRFAKGIASGMAYLHSMC-IIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkr 493
Cdd:cd06623  88 DLLKKVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVL----------------- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  494 tlrKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd06623 151 ---ENTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLE 192
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
334-603 2.00e-35

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: 133.98  E-value: 2.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05085   1 GELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveERKRAPMEKATTKK 492
Cdd:cd05085  81 LSFLRkKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR----QEDDGVYSSSGLKQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 RTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEiigqvyadpdclprTLDFGL-------------N 559
Cdd:cd05085 157 IPIK---------------WTAPEALNYGRYSSESDVWSFGILLWE--------------TFSLGVcpypgmtnqqareQ 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031869  560 VKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEA 603
Cdd:cd05085 208 VEKGYRMSAPQRCPEDIYKIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
335-600 3.54e-35

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: 133.34  E-value: 3.54e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKT-CRETlpPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEERKRAPMEKATTK 491
Cdd:cd05041  80 LLTFLRkKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR---EEEDGEYTVSDGLK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 KRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIigqvYADPDClP-------RTLDFglnVKLFW 564
Cdd:cd05041 157 QIPIK---------------WTAPEALNYGRYTSESDVWSFGILLWEI----FSLGAT-PypgmsnqQTREQ---IESGY 213
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  565 EKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDS 600
Cdd:cd05041 214 RMPAPELCPEAVYRLMLQCWAYDPENRPSFSEIYNE 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
334-597 4.23e-35

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: 133.12  E-value: 4.23e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd06627   5 GDLIGRGAFGSVYKGLNLNTGEFVAIKqiSLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPmekattk 491
Cdd:cd06627  85 SLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDEN------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 krtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ-VYADPDCLPrtldfglnvKLFweKFVP 569
Cdd:cd06627 158 -------------SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLtGNpPYYDLQPMA---------ALF--RIVQ 213
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  570 TDCPPafFPLAA---------ICCRLEPESRPAFSKL 597
Cdd:cd06627 214 DDHPP--LPENIspelrdfllQCFQKDPTLRPSAKEL 248
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
334-597 1.17e-34

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: 131.98  E-value: 1.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKElirCDE----ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd05084   1 GERIGRGNFGEVFSGRLRADNTPVAVKS---CREtlppDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEERKRAPMEKA 488
Cdd:cd05084  78 GGDFLTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR---EEEDGVYAATG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEI--IGQV-YADPDClPRTLDFglnVKLFWE 565
Cdd:cd05084 155 GMKQIPVK---------------WTAPEALNYGRYSSESDVWSFGILLWETfsLGAVpYANLSN-QQTREA---VEQGVR 215
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  566 KFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05084 216 LPCPENCPDEVYRLMEQCWEYDPRKRPSFSTV 247
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
330-538 1.62e-34

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 131.76  E-value: 1.62e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApm 485
Cdd:cd08529  81 AENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFA-- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  486 ekattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd08529 159 ------------------QTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYE 193
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
336-597 1.24e-33

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: 129.39  E-value: 1.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIR-CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06605   8 ELGEGNGGVVSKVRHRPSGQIMAVKVIRLeIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVRFAKGIASGMAYLHS-MCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrapmekattkkr 493
Cdd:cd06605  88 KILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV---------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 tlrkNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI-IGQV-YADPDCLPRTLDFGLNVKLFWEKfvPTD 571
Cdd:cd06605 152 ----DSLAK--TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELaTGRFpYPPPNAKPSMMIFELLSYIVDEP--PPL 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031869  572 CPPAFFPLAAI-----CCRLEPESRPAFSKL 597
Cdd:cd06605 224 LPSGKFSPDFQdfvsqCLQKDPTERPSYKEL 254
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
335-540 1.29e-33

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: 129.72  E-value: 1.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd13996  12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEkVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQK---VRFAKGIASGMAYLHSMCIIHRDLNSHNCLI-KLDKTVVVADFGLSRLIveerkrapmeKAT 489
Cdd:cd13996  92 RDWIDRRNSSSKNDRklaLELFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVKIGDFGLATSI----------GNQ 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  490 TKKRTLRKNDRKKRY----TVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd13996 162 KRELNNLNNNNNGNTsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
337-542 3.29e-33

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: 128.34  E-value: 3.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEEtQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLhssPNCIEE-RKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFL-RSMDPFPWQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapmekatt 490
Cdd:cd13978  80 KSLLeREIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKL--------------- 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  491 KKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSY--DETVDIFSFGIVLCEIIGQ 542
Cdd:cd13978 145 GMKSISANRRRGTENLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTR 198
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
12-65 5.25e-33

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 120.36  E-value: 5.25e-33
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   12 CPGCGDHIAPSQiWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYW 65
Cdd:cd09463   1 CTGCGGRIQDSF-HYRVVQEAWHNSCFQCSVCQDLLTNWYYEKDGKLYCHKHYW 53
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
337-598 8.68e-33

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: 126.78  E-value: 8.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGqaikVTHKATGKVM-VMKELIRCDEEtQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd14058   1 VGRGSFG----VVCKARWRNQiVAVKIIESESE-KKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFP---WQQKVRFAKGIASGMAYLHSMC---IIHRDLNSHNCLIKLDKTVV-VADFGLSrliveerkrapmeka 488
Cdd:cd14058  76 VLHGKEPKPiytAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVLkICDFGTA--------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 tTKKRTLRKNDRkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqvyadpdclPRTLDF----GLNVKLFW 564
Cdd:cd14058 141 -CDISTHMTNNK-------GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVI----------TRRKPFdhigGPAFRIMW 202
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5031869  565 E----KFVP--TDCPPAFFPLAAICCRLEPESRPAFSKLE 598
Cdd:cd14058 203 AvhngERPPliKNCPKPIESLMTRCWSKDPEKRPSMKEIV 242
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
335-597 9.17e-33

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: 127.09  E-value: 9.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGffgqAIKVTHKA----TGKVMVMK--ELIRCDEETqKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd06610   7 EVIGSG----ATAVVYAAyclpKKEKVAIKriDLEKCQTSM-DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFA---KGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApm 485
Cdd:cd06610  82 SGGSLLDIMKSSYPRGGLDEAIIAtvlKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRT-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  486 ekattkkrtlrkndRKKRYTVVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCE-IIGQ---------------VYADPD 548
Cdd:cd06610 160 --------------RKVRKTFVGTPCWMAPEvMEQVRGYDFKADIWSFGITAIElATGAapyskyppmkvlmltLQNDPP 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  549 CLPRTLDFGLNVKLFwEKFVptdcppaffplaAICCRLEPESRPAFSKL 597
Cdd:cd06610 226 SLETGADYKKYSKSF-RKMI------------SLCLQKDPSKRPTAEEL 261
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
337-538 1.03e-32

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: 126.57  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI--RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISrkKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSRLIveerkrAPMEKATtk 491
Cdd:cd14009  81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSL------QPASMAE-- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  492 krtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd14009 153 -------------TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFE 186
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
325-597 1.27e-32

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: 127.07  E-value: 1.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  325 IFRPCDLIHGEVLGKGFFGQAIK------VTHKATGKVMVmKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYK 397
Cdd:cd05032   2 ELPREKITLIRELGQGSFGMVYEglakgvVKGEPETRVAI-KTVNENASMRERIeFLNEASVMKEFNCHHVVRLLGVVST 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  398 DKKLNLLTEYIEGGTLKDFLRS----------MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV 467
Cdd:cd05032  81 GQPTLVVMELMAKGDLKSYLRSrrpeaennpgLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  468 ADFGLSRLIVEerkrapmekattkkRTLRKNDRKKRYTVvgnpYWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVY 544
Cdd:cd05032 161 GDFGMTRDIYE--------------TDYYRKGGKGLLPV----RWMAPESLKDGVFTTKSDVWSFGVVLWEMAtlaEQPY 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  545 AdpdclprtldfGL-NVKLFweKFV--------PTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05032 223 Q-----------GLsNEEVL--KFVidgghldlPENCPDKLLELMRMCWQYNPKMRPTFLEI 271
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
337-602 1.87e-32

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: 125.47  E-value: 1.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMV--MKElircDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd05034   3 LGAGQFGEVWMGVWNGTTKVAVktLKP----GTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvEERKRAPMEKAttkk 492
Cdd:cd05034  79 DYLRTGEgrALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLI-EDDEYTAREGA---- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrkndrkkRYTVvgnpYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YADPDClPRTLDfglNVKLFWEKFVP 569
Cdd:cd05034 154 ----------KFPI----KWTAPEAALYGRFTIKSDVWSFGILLYEIVtyGRVpYPGMTN-REVLE---QVERGYRMPKP 215
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031869  570 TDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd05034 216 PGCPDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
335-604 1.99e-32

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: 126.14  E-value: 1.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05065  10 EVIGAGEFGEVCRGRLKLPGKreiFVAIKTLkSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMEN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKAT 489
Cdd:cd05065  90 GALDSFLRQNDgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSSL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 TKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYADPDclprTLDFGLNVKLFWEK 566
Cdd:cd05065 170 GGKIPIR---------------WTAPEAIAYRKFTSASDVWSYGIVMWEVMSygeRPYWDMS----NQDVINAIEQDYRL 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031869  567 FVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05065 231 PPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
335-604 2.70e-32

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: 125.75  E-value: 2.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05066  10 KVIGAGEFGEVCSGRLKLPGKreiPVAIKTLkAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMEN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekat 489
Cdd:cd05066  90 GSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVL------------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkkrtlrKNDRKKRYTVVGNPY---WMAPEMLNGKSYDETVDIFSFGIVLCEIIGqvYAD-PDCLPRTLDFGLNVKLFWE 565
Cdd:cd05066 157 -------EDDPEAAYTTRGGKIpirWTAPEAIAYRKFTSASDVWSYGIVMWEVMS--YGErPYWEMSNQDVIKAIEEGYR 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 5031869  566 KFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05066 228 LPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKL 266
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
328-600 3.21e-32

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: 125.25  E-value: 3.21e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGqaikVTH--KATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd05059   3 PSELTFLKELGSGQFG----VVHlgKWRGKIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrap 484
Cdd:cd05059  79 EYMANGCLLNYLRERRGkFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDD----- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  485 mekattkkrtlrkndrkkRYTV-VGNPY---WMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVYADPDCLPRTLDfgl 558
Cdd:cd05059 154 ------------------EYTSsVGTKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFseGKMPYERFSNSEVVE--- 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 5031869  559 NVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDS 600
Cdd:cd05059 213 HISQGYRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQ 254
Pkinase pfam00069
Protein kinase domain;
334-592 6.30e-32

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 123.12  E-value: 6.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    334 GEVLGKGFFGQAIKVTHKATGKVMVMKELI--RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHRDTGKIVAIKKIKkeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCiihrdlnshnclikldktvvvadfglsrliveerkrapmekattk 491
Cdd:pfam00069  84 SLFDLLSEKGAFSEREAKFIMKQILEGLESGSSLT--------------------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    492 krtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVKLFWEKFVPT 570
Cdd:pfam00069 119 -------------TFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLtGKPPFPGINGNEIYELIIDQPYAFPELPSN 185
                         250       260
                  ....*....|....*....|..
gi 5031869    571 dCPPAFFPLAAICCRLEPESRP 592
Cdd:pfam00069 186 -LSEEAKDLLKKLLKKDPSKRL 206
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
332-539 7.72e-32

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: 125.14  E-value: 7.72e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEvLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd06644  16 IIGE-LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekaTT 490
Cdd:cd06644  95 AVDAIMLELDRGLTEPQIQvICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVS---------------AK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  491 KKRTLRKNDrkkryTVVGNPYWMAPEM-----LNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06644 160 NVKTLQRRD-----SFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEM 208
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
12-65 9.97e-32

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 116.82  E-value: 9.97e-32
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   12 CPGCGDHIAPSQiWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYW 65
Cdd:cd09364   1 CAGCRGKILDSQ-YVQALNQDWHCDCFRCSVCSDSLSNWYFEKDGKLYCRKDYW 53
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
328-604 2.03e-31

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: 123.16  E-value: 2.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNL 403
Cdd:cd05063   4 PSHITKQKVIGAGEFGEVFRGILKMPGRkevAVAIKTLKPGYTEKQRQdFLSEASIMGQFSHHNIIRLEGVVTKFKPAMI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkr 482
Cdd:cd05063  84 ITEYMENGALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVL------ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  483 apmekattkkrtlrKNDRKKRYTVVGNPY---WMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYADpdclprtLDF 556
Cdd:cd05063 158 --------------EDDPEGTYTTSGGKIpirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfgeRPYWD-------MSN 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  557 GLNVKLFWEKF---VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05063 217 HEVMKAINDGFrlpAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
337-604 2.97e-31

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: 122.53  E-value: 2.97e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELiRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTL-KEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKrt 494
Cdd:cd05052  93 LRECNReeLNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIK-- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEI------------IGQVYadpdclpRTLDFGLNVKl 562
Cdd:cd05052 171 -----------------WTAPESLAYNKFSIKSDVWAFGVLLWEIatygmspypgidLSQVY-------ELLEKGYRME- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 5031869  563 fwekfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05052 226 -----RPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
332-597 4.09e-31

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: 122.49  E-value: 4.09e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRC----DEETQKTFL----TEVKVMRSLDHPNVLKFIGVLYKDKKL 401
Cdd:cd06629   4 VKGELIGKGTYGRVYLAMNATTGEMLAVKqvELPKTssdrADSRQKTVVdalkSEIDTLKDLDHPNIVQYLGFEETEDYF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSMDPFPwQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveer 480
Cdd:cd06629  84 SIFLEYVPGGSIGSCLRKYGKFE-EDLVRfFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGIS------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 KRAPMEKATTKKRTLRkndrkkrytvvGNPYWMAPEML--NGKSYDETVDIFSFGIVLCEIigqvYADPDCLPRTLDFGL 558
Cdd:cd06629 156 KKSDDIYGNNGATSMQ-----------GSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEM----LAGRRPWSDDEAIAA 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031869  559 NVKLFWEKF---VPTD---CPPAFFPLAAiCCRLEPESRPAFSKL 597
Cdd:cd06629 221 MFKLGNKRSappVPEDvnlSPEALDFLNA-CFAIDPRDRPTAAEL 264
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
331-604 5.03e-31

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: 122.26  E-value: 5.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKVTHKA----TGKVMV--MKELIRCDEETQKtFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN-- 402
Cdd:cd05035   1 LKLGKILGEGEFGSVMEAQLKQddgsQLKVAVktMKVDIHTYSEIEE-FLSEAACMKDFDHPNVMRLIGVCFTASDLNkp 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 ----LLTEYIEGGTLKDFLRSM------DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL 472
Cdd:cd05035  80 pspmVILPFMKHGDLHSYLLYSrlgglpEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  473 SRLIVEER--KRAPMEKATTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YADP 547
Cdd:cd05035 160 SRKIYSGDyyRQGRISKMPVK--------------------WIALESLADNVYTSKSDVWSFGVTMWEIAtrGQTpYPGV 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  548 DC--LPRTLDFGLNVKlfwekfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05035 220 ENheIYDYLRNGNRLK------QPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
334-536 7.26e-31

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: 121.51  E-value: 7.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKtFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14099   6 GKFLGKGGFAKCYEVTDMSTGKVyagkVVPKSSLTKPKQREK-LKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekat 489
Cdd:cd14099  85 NGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARL------------- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  490 tkkrtlrKNDRKKRYTVVGNPYWMAPEMLNGKS-YDETVDIFSFGIVL 536
Cdd:cd14099 152 -------EYDGERKKTLCGTPNYIAPEVLEKKKgHSFEVDIWSLGVIL 192
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
337-538 7.68e-31

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: 121.26  E-value: 7.68e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd06613   8 IGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGSLQDI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmeKATTKKRTlr 496
Cdd:cd06613  88 YQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQL----------TATIAKRK-- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  497 kndrkkryTVVGNPYWMAPEMLNGKS---YDETVDIFSFGIVLCE 538
Cdd:cd06613 156 --------SFIGTPYWMAPEVAAVERkggYDGKCDIWALGITAIE 192
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
334-603 8.60e-31

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: 121.39  E-value: 8.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVmKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05148  11 ERKLGSGYFGEVWEGLWKNRVRVAI-KILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkraPMEKATTK 491
Cdd:cd05148  90 LAFLRSPEgqVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKE-----DVYLSSDK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 KRtlrkndrkkrytvvgnPY-WMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YAdpdclprtldfGLNVKLFWEKF 567
Cdd:cd05148 165 KI----------------PYkWTAPEAASHGTFSTKSDVWSFGILLYEMFtyGQVpYP-----------GMNNHEVYDQI 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031869  568 V-------PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEA 603
Cdd:cd05148 218 TagyrmpcPAKCPQEIYKIMLECWAAEPEDRPSFKALREELDN 260
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
330-602 1.15e-30

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: 120.86  E-value: 1.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATgkvmvmKELIRC--DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDK-KLNLLTE 406
Cdd:cd05082   7 ELKLLQTIGKGEFGDVMLGDYRGN------KVAVKCikNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKgGLYIVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSM--DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAP 484
Cdd:cd05082  81 YMAKGSLVDYLRSRgrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLT-------KEAS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  485 MEKATTKKRTlrkndrkkrytvvgnpYWMAPEMLNGKSYDETVDIFSFGIVLCEI--IGQV----YADPDCLPRtldfgl 558
Cdd:cd05082 154 STQDTGKLPV----------------KWTAPEALREKKFSTKSDVWSFGILLWEIysFGRVpyprIPLKDVVPR------ 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031869  559 nVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd05082 212 -VEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
334-597 1.93e-30

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: 120.20  E-value: 1.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDE-----ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd06632   5 GQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDdkksrESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrliveerkrapMEKA 488
Cdd:cd06632  85 PGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFG-------------MAKH 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TTKKRTLRkndrkkryTVVGNPYWMAPEMLNGK--SYDETVDIFSFGivlCEIIGQVYADP---DCLPRTLDFglnvKLF 563
Cdd:cd06632 152 VEAFSFAK--------SFKGSPYWMAPEVIMQKnsGYGLAVDIWSLG---CTVLEMATGKPpwsQYEGVAAIF----KIG 216
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031869  564 WEKFVPTdCPPAFFPLA----AICCRLEPESRPAFSKL 597
Cdd:cd06632 217 NSGELPP-IPDHLSPDAkdfiRLCLQRDPEDRPTASQL 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
334-540 1.97e-30

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: 120.15  E-value: 1.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd06625   5 GKLLGQGAFGQVYLCYDADTGRELAVKqvEIDPINTEASKevkALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrliveerkrapmekA 488
Cdd:cd06625  85 PGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFG----------------A 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  489 TTKKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06625 149 SKRLQTICSSTGMK--SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEML 198
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
330-604 2.03e-30

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: 121.22  E-value: 2.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHK--------ATGKVMVMKEliRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKL 401
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKATAFrlkgragyTTVAVKMLKE--NASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLR------------------SMDPFPWQQKVR------FAKGIASGMAYLHSMCIIHRDLNSHNC 457
Cdd:cd05045  79 LLIVEYAKYGSLRSFLResrkvgpsylgsdgnrnsSYLDNPDERALTmgdlisFAWQISRGMQYLAEMKLVHRDLAARNV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  458 LIKLDKTVVVADFGLSRLIVEERKRApmekattkKRTlrkndrKKRYTVvgnpYWMAPEMLNGKSYDETVDIFSFGIVLC 537
Cdd:cd05045 159 LVAEGRKMKISDFGLSRDVYEEDSYV--------KRS------KGRIPV----KWMAIESLFDHIYTTQSDVWSFGVLLW 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  538 EII---GQVYadPDCLPRTLdFGLnVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05045 221 EIVtlgGNPY--PGIAPERL-FNL-LKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
337-540 2.06e-30

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: 119.94  E-value: 2.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKatGKVMVMKE---LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKD-KKLNLLTEYIEGGT 412
Cdd:cd14064   1 IGSGSFGKVYKGRCR--NKIVAIKRyraNTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFL----RSMDPfpwQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIKLDKTVVVADFGLSRLiVEERKRAPME 486
Cdd:cd14064  79 LFSLLheqkRVIDL---QSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRF-LQSLDEDNMT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  487 KATtkkrtlrkndrkkrytvvGNPYWMAPEML--NGKsYDETVDIFSFGIVLCEII 540
Cdd:cd14064 155 KQP------------------GNLRWMAPEVFtqCTR-YSIKADVFSYALCLWELL 191
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
328-597 4.57e-30

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: 119.28  E-value: 4.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd05112   3 PSELTFVQEIGSGQFGLVHLGYWLNKDKVAI--KTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSmdpfpwqQKVRFAK--------GIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEE 479
Cdd:cd05112  81 MEHGCLSDYLRT-------QRGLFSAetllgmclDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  480 RKRApmekATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVYADPDC---LPRTL 554
Cdd:cd05112 154 QYTS----STGTKFPVK---------------WSSPEVFSFSRYSSKSDVWSFGVLMWEVFseGKIPYENRSnseVVEDI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031869  555 DFGLNVklfwekFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05112 215 NAGFRL------YKPRLASTHVYEIMNHCWKERPEDRPSFSLL 251
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
330-604 9.71e-30

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: 119.06  E-value: 9.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVT-------HKATGKVMVMKELIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKL 401
Cdd:cd05053  13 RLTLGKPLGEGAFGQVVKAEavgldnkPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSMDPFPWQQK----------------VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTV 465
Cdd:cd05053  93 YVVVEYASKGNLREFLRARRPPGEEASpddprvpeeqltqkdlVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVM 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  466 VVADFGLSRLIveerkrapmekattkkrtlRKNDRKKRYTVVGNPY-WMAPEMLNGKSYDETVDIFSFGIVLCEII---G 541
Cdd:cd05053 173 KIADFGLARDI-------------------HHIDYYRKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFtlgG 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  542 QVYAdpdclprtldfGLNV-KLF--------WEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05053 234 SPYP-----------GIPVeELFkllkeghrMEK--PQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRI 292
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
338-604 1.05e-29

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: 117.75  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  338 GKGFFGQAIKVTHKATGKVMVMKELIRCDEETQktfltevkVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFL 417
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEKEAE--------ILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  418 RSMDP--FPWQQKVRFAKGIASGMAYLHS---MCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekaTTkk 492
Cdd:cd14060  74 NSNESeeMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASRFHSH----------TT-- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrkndrkkRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIigqvyadpdcLPRTLDF----GLNVK-LFWEK- 566
Cdd:cd14060 142 ----------HMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEM----------LTREVPFkgleGLQVAwLVVEKn 201
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031869  567 ---FVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14060 202 erpTIPSSCPRSFAELMRRCWEADVKERPSFKQIIGILESM 242
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
326-597 1.07e-29

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: 118.96  E-value: 1.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  326 FRPCDLIHGEVLGKGFFGQAIKVTHKA----TGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYK--DK 399
Cdd:cd14205   1 FEERHLKFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSagRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 KLNLLTEYIEGGTLKDFL-RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVE 478
Cdd:cd14205  81 NLRLIMEYLPYGSLRDYLqKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  479 ErkrapmekattkkrtlrkndrkKRYTVVGNP-----YWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADPDCLP-- 551
Cdd:cd14205 161 D----------------------KEYYKVKEPgespiFWYAPESLTESKFSVASDVWSFGVVLYELF--TYIEKSKSPpa 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  552 ------------RTLDFGLnVKLFWEKF---VPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd14205 217 efmrmigndkqgQMIVFHL-IELLKNNGrlpRPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
335-601 1.67e-29

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: 118.59  E-value: 1.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAI---------------KVTHKATGKVMVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYK 397
Cdd:cd05051  11 EKLGEGQFGEVHlceanglsdltsddfIGNDNKDEPVLVAVKMLRPDasKNAREDFLKEVKIMSQLKDPNIVRLLGVCTR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  398 DKKLNLLTEYIEGGTLKDFLRSMDPF------------PWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTV 465
Cdd:cd05051  91 DEPLCMIVEYMENGDLNQFLQKHEAEtqgasatnsktlSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  466 VVADFGLSRLIVEE-----RKRAPMekattkkrTLRkndrkkrytvvgnpyWMAPE-MLNGKsYDETVDIFSFGIVLCEI 539
Cdd:cd05051 171 KIADFGMSRNLYSGdyyriEGRAVL--------PIR---------------WMAWEsILLGK-FTTKSDVWAFGVTLWEI 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  540 --------------------IGQVYAD---PDCLPRtldfglnvklfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSK 596
Cdd:cd05051 227 ltlckeqpyehltdeqvienAGEFFRDdgmEVYLSR----------------PPNCPKEIYELMLECWRRDEEDRPTFRE 290

                ....*
gi 5031869  597 LEDSF 601
Cdd:cd05051 291 IHLFL 295
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
332-539 1.81e-29

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: 118.21  E-value: 1.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEvLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd06643   9 IVGE-LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekaTT 490
Cdd:cd06643  88 AVDAVMLELErPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVS---------------AK 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  491 KKRTLRKNDrkkryTVVGNPYWMAPEML-----NGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06643 153 NTRTLQRRD-----SFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEM 201
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
331-602 2.53e-29

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: 116.90  E-value: 2.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKVTHkaTGKVMVMKElIRCDEeTQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKkLNLLTEYIEG 410
Cdd:cd05083   8 LTLGEIIGEGEFGAVLQGEY--MGQKVAVKN-IKCDV-TAQAFLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPF--PWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveERKRAPMEKA 488
Cdd:cd05083  83 GNLVNFLRSRGRAlvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV---GSMGVDNSRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYAdPDCLPRTLDFGLNVKLFWEKFV 568
Cdd:cd05083 160 PVK--------------------WTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRA-PYPKMSVKEVKEAVEKGYRMEP 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031869  569 PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd05083 219 PEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
337-601 3.41e-29

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: 116.83  E-value: 3.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGkVMVMKELIRCDE--ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTGPNciEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMdPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL------SRLIVEERKRAPMEKA 488
Cdd:cd14027  80 HVLKKV-SVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLTKEEHNEQREVDG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TTKKRTlrkndrkkrytvvGNPYWMAPEML---NGKSyDETVDIFSFGIVLCEIIGQVYADPDCLPR-TLDFGLNVK-LF 563
Cdd:cd14027 159 TAKKNA-------------GTLYYMAPEHLndvNAKP-TEKSDVYSFAIVLWAIFANKEPYENAINEdQIIMCIKSGnRP 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031869  564 WEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:cd14027 225 DVDDITEYCPREIIDLMKLCWEANPEARPTFPGIEEKF 262
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
337-602 5.73e-29

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: 116.35  E-value: 5.73e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmKELiRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05068  16 LGSGQFGEVWEGLWNNTTPVAV-KTL-KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKAttkkrtl 495
Cdd:cd05068  94 LQGKGrSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREGA------- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  496 rkndrkkRYTVvgnpYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV----YADPDCLpRTLDFGLNVKlfwekfVP 569
Cdd:cd05068 167 -------KFPI----KWTAPEAANYNRFSIKSDVWSFGILLTEIVtyGRIpypgMTNAEVL-QQVERGYRMP------CP 228
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  570 TDCPPAFFPLAAICCRLEPESRPAFS----KLEDSFE 602
Cdd:cd05068 229 PNCPPQLYDIMLECWKADPMERPTFEtlqwKLEDFFV 265
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
334-536 5.86e-29

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: 115.81  E-value: 5.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLT---EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14081   6 GKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKverEIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekatt 490
Cdd:cd14081  86 GELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSL--------- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  491 kkrtLRkndrkkryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14081 157 ----LE--------TSCGSPHYACPEVIKGEKYDgRKADIWSCGVIL 191
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
335-540 7.80e-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: 116.43  E-value: 7.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgT 412
Cdd:cd07829   5 EKLGEGTYGVVYKAKDKKTGEIVALKKirLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYCDQ-D 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMekattk 491
Cdd:cd07829  84 LKKYLDKRPgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAF-----GIPL------ 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  492 krtlrkndrkKRYT-VVGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07829 153 ----------RTYThEVVTLWYRAPEILLGsKHYSTAVDIWSVGCIFAELI 193
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
335-597 8.76e-29

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: 115.81  E-value: 8.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd06609   7 ERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQqEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGSV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSmDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrAPMEkattkkr 493
Cdd:cd06609  87 LDLLKP-GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVS---------GQLT------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 tlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YAD----------PDCLPRTLDFGLNVK 561
Cdd:cd06609 150 ----STMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAkGEPpLSDlhpmrvlfliPKNNPPSLEGNKFSK 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  562 LFWEkFVptdcppaffplaAICCRLEPESRPAFSKL 597
Cdd:cd06609 226 PFKD-FV------------ELCLNKDPKERPSAKEL 248
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
339-540 1.06e-28

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: 115.78  E-value: 1.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  339 KGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDmirKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkrapmEKATTKKRTL 495
Cdd:cd05579  83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRR-----QIKLSIQKKS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  496 RKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05579 158 NGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFL 202
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
336-604 1.25e-28

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: 115.18  E-value: 1.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGqaiKVtHKAT--GKVMVMKELiRCDEE-----TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14061   1 VIGVGGFG---KV-YRGIwrGEEVAVKAA-RQDPDedisvTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLrSMDPFPWQQKVRFAKGIASGMAYLHS---MCIIHRDLNSHNCLIK--------LDKTVVVADFGLSRliv 477
Cdd:cd14061  76 RGGALNRVL-AGRKIPPHVLVDWAIQIARGMNYLHNeapVPIIHRDLKSSNILILeaienedlENKTLKITDFGLAR--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 EERKRAPMEKATTkkrtlrkndrkkrYTvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRTLD 555
Cdd:cd14061 152 EWHKTTRMSAAGT-------------YA------WMAPEVIKSSTFSKASDVWSYGVLLWELLtGEVpYKGIDGLAVAYG 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  556 FGLNvKLFWEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14061 213 VAVN-KLTLP--IPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
335-603 1.28e-28

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: 115.37  E-value: 1.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKkLNLLTEYIEGGTLK 414
Cdd:cd05067  13 ERLGAGQFGEVWMGYYNGHTKVAI--KSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEP-IYIITEYMENGSLV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvEERKRAPMEKATTKK 492
Cdd:cd05067  90 DFLKTPSgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLI-EDNEYTAREGAKFPI 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 RtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV----YADPDCLpRTLDFGLNVKlfwek 566
Cdd:cd05067 169 K------------------WTAPEAINYGTFTIKSDVWSFGILLTEIVthGRIpypgMTNPEVI-QNLERGYRMP----- 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031869  567 fVPTDCPPAFFPLAAICCRLEPESRPAF----SKLEDSFEA 603
Cdd:cd05067 225 -RPDNCPEELYQLMRLCWKERPEDRPTFeylrSVLEDFFTA 264
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
334-540 1.68e-28

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: 115.67  E-value: 1.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKvtHKATGKVMVMKELIRCD----EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14158  20 GNKLGEGGFGVVFK--GYINDKNVAVKKLAAMVdistEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMD---PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLikLDKTVV--VADFGLSRliveerkraP 484
Cdd:cd14158  98 NGSLLDRLACLNdtpPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANIL--LDETFVpkISDFGLAR---------A 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  485 MEKATTKKRTLRkndrkkrytVVGNPYWMAPEMLNGKSYDETvDIFSFGIVLCEII 540
Cdd:cd14158 167 SEKFSQTIMTER---------IVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEII 212
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
367-598 1.68e-28

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 114.79  E-value: 1.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  367 EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSM 445
Cdd:cd13992  37 RTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREiKMDWMFKSSFIKDIVKGMNYLHSS 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  446 CII-HRDLNSHNCLIKLDKTVVVADFGLSRLIvEERKRAPMEKATTKKRTLrkndrkkrytvvgnpyWMAPEMLNGKSYD 524
Cdd:cd13992 117 SIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLL-EEQTNHQLDEDAQHKKLL----------------WTAPELLRGSLLE 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  525 ETV----DIFSFGIVLCEIIGqvYADPdclprtLDFGLNVKLF-------WEKFVPTD------CPPAffpLAAIC--CR 585
Cdd:cd13992 180 VRGtqkgDVYSFAIILYEILF--RSDP------FALEREVAIVekvisggNKPFRPELavlldeFPPR---LVLLVkqCW 248
                       250
                ....*....|....
gi 5031869  586 LE-PESRPAFSKLE 598
Cdd:cd13992 249 AEnPEKRPSFKQIK 262
LIM2_LIMK cd09365
The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain ...
72-125 1.71e-28

The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188751 [Multi-domain]  Cd Length: 54  Bit Score: 107.84  E-value: 1.71e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   72 CHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCH 125
Cdd:cd09365   1 CHGCSQIITGPVMVAGDHKFHPECFSCSSCKAFIGDGDSYALVERSKLYCGVCY 54
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
337-602 2.15e-28

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 114.03  E-value: 2.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKvtHKATGKVMVMKELIRCDEETQ-KTFLTEVKVMRSLDHPNVLKFIGVLYKDKkLNLLTEYIEGGTLKD 415
Cdd:cd14062   1 IGSGSFGTVYK--GRWHGDVAVKKLNVTDPTPSQlQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-LAIVTQWCEGSSLYK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLsrliveerkrapmekATTKKrt 494
Cdd:cd14062  78 HLHVLEtKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGL---------------ATVKT-- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lRKNDRKKRYTVVGNPYWMAPE---MLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRTL---DFGL---NVKLf 563
Cdd:cd14062 141 -RWSGSQQFEQPTGSILWMAPEvirMQDENPYSFQSDVYAFGIVLYELLtGQLpYSHINNRDQILfmvGRGYlrpDLSK- 218
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 5031869  564 wekfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd14062 219 ----VRSDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
335-604 2.16e-28

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: 114.74  E-value: 2.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKatGKVMVMKELIRCDEE----TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14147   9 EVIGIGGFGKVYRGSWR--GELVAVKAARQDPDEdisvTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFL--RSMDPfpwQQKVRFAKGIASGMAYLHSMCI---IHRDLNSHNCLIKL--------DKTVVVADFGLSRliv 477
Cdd:cd14147  87 GPLSRALagRRVPP---HVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQpienddmeHKTLKITDFGLAR--- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 EERKRAPMEKAttkkrtlrkndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRTLD 555
Cdd:cd14147 161 EWHKTTQMSAA-------------------GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLtGEVpYRGIDCLAVAYG 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  556 FGLNvKLFWEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14147 222 VAVN-KLTLP--IPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
337-602 2.26e-28

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 113.86  E-value: 2.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTKVAI--KTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGSLLDF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvEERKRAPMEKATTKKRt 494
Cdd:cd14203  80 LKDGEgkYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI-EDNEYTARQGAKFPIK- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lrkndrkkrytvvgnpyWMAPEM-LNGKsYDETVDIFSFGIVLCEIIGQvyadpdclPRTLDFGLNVKLFWEKF------ 567
Cdd:cd14203 158 -----------------WTAPEAaLYGR-FTIKSDVWSFGILLTELVTK--------GRVPYPGMNNREVLEQVergyrm 211
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  568 -VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd14203 212 pCPPGCPESLHELMCQCWRKDPEERPTFEYLQSFLE 247
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
335-539 2.54e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 114.18  E-value: 2.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSLDHPNVLKFIG--VLYKDKKLNLLTEYIEG 410
Cdd:cd08217   6 ETIGKGSFGTVRKVRRKSDGKILVWKEIdyGKMSEKEKQQLVSEVNILRELKHPNIVRYYDriVDRANTTLYIVMEYCEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTL----KDFLRSMDPFPWQQKVRFAKGIASGMAYLH-----SMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERK 481
Cdd:cd08217  86 GDLaqliKKCKKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSS 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  482 RApmekattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08217 166 FA--------------------KTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYEL 203
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
334-604 3.13e-28

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: 114.63  E-value: 3.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQA----IKVTHKATGKVMV--MKELIRCDEETQKtFLTEVKVMRSLDHPNVLKFIGV-LYKDKKLNL--- 403
Cdd:cd05074  14 GRMLGKGEFGSVreaqLKSEDGSFQKVAVkmLKADIFSSSDIEE-FLREAACMKEFDHPNVIKLIGVsLRSRAKGRLpip 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 --LTEYIEGGTLKDFLRSM----DPF--PWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRL 475
Cdd:cd05074  93 mvILPFMKHGDLHTFLLMSrigeEPFtlPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKK 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  476 IV--EERKRAPMEKATTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-YAdpdcl 550
Cdd:cd05074 173 IYsgDYYRQGCASKLPVK--------------------WLALESLADNVYTTHSDVWAFGVTMWEIMtrGQTpYA----- 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  551 prtldfGLNVKLFWEKFV-------PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05074 228 ------GVENSEIYNYLIkgnrlkqPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
337-551 3.20e-28

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: 113.86  E-value: 3.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIR---CDEETQKTFLTEVKVMRSLDHPNVLKFIGVlYKDKK-LNLLTEYIEGGT 412
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKrhiVQTRQQEHIFSEKEILEECNSPFIVKLYRT-FKDKKyLYMLMEYCLGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPwQQKVRFAKG-IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrapmekattk 491
Cdd:cd05572  80 LWTILRDRGLFD-EYTARFYTAcVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLG-------------- 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  492 krtlrknDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVYADPDCLP 551
Cdd:cd05572 145 -------SGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLtgRPPFGGDDEDP 199
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
335-540 3.48e-28

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: 113.86  E-value: 3.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFgqaiKVTHKA----TGK-----VMVMKELIRcdEETQKtFLTEVKVMRSLDHPNVLKFIGVLYKDKK--LNL 403
Cdd:cd13983   7 EVLGRGSF----KTVYRAfdteEGIevawnEIKLRKLPK--AERQR-FKQEIEILKSLKHPNIIKFYDSWESKSKkeVIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIKLDKTVV-VADFGLSrliveer 480
Cdd:cd13983  80 ITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGEVkIGDLGLA------- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 krapmekatTKKRTlrkndrKKRYTVVGNPYWMAPEMLNGKsYDETVDIFSFGIVLCEII 540
Cdd:cd13983 153 ---------TLLRQ------SFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMA 196
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
334-605 6.25e-28

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: 113.56  E-value: 6.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVM-----VMKELIrCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN------ 402
Cdd:cd05075   5 GKTLGEGEFGSVMEGQLNQDDSVLkvavkTMKIAI-CTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESEgypspv 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 LLTEYIEGGTLKDFL---RSMDP---FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLI 476
Cdd:cd05075  84 VILPFMKHGDLHSFLlysRLGDCpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  477 V--EERKRAPMEKATTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV-Y--ADPDC 549
Cdd:cd05075 164 YngDYYRQGRISKMPVK--------------------WIAIESLADRVYTTKSDVWSFGVTMWEIAtrGQTpYpgVENSE 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  550 LPRTLDFGLNVKLfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd05075 224 IYDYLRQGNRLKQ------PPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKIL 273
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
332-549 7.44e-28

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: 113.01  E-value: 7.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQK-------TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN 402
Cdd:cd06628   3 IKGALIGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENKDrkksmldALQREIALLRELQHENIVQYLGSSSDANHLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 LLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkr 482
Cdd:cd06628  83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGIS--------- 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  483 apmeKATTKKRTLRKNdRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDC 549
Cdd:cd06628 154 ----KKLEANSLSTKN-NGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDC 215
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
336-604 9.99e-28

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: 112.39  E-value: 9.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATgKVMVMKELIRCDEE---TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14148   1 IIGVGGFGKVYKGLWRGE-EVAVKAARQDPDEDiavTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLrSMDPFPWQQKVRFAKGIASGMAYLHS---MCIIHRDLNSHNCLIK--------LDKTVVVADFGLSRlivEERK 481
Cdd:cd14148  80 LNRAL-AGKKVPPHVLVNWAVQIARGMNYLHNeaiVPIIHRDLKSSNILILepienddlSGKTLKITDFGLAR---EWHK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  482 RAPMEKATTkkrtlrkndrkkrYTvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRTLDFGLN 559
Cdd:cd14148 156 TTKMSAAGT-------------YA------WMAPEVIRLSLFSKSSDVWSFGVLLWELLtGEVpYREIDALAVAYGVAMN 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031869  560 vKLFWEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14148 217 -KLTLP--IPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
337-602 1.01e-27

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: 112.81  E-value: 1.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKkLNLLTEYIEGGTLKDF 416
Cdd:cd05073  19 LGAGQFGEVWMATYNKHTKVAV--KTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEP-IYIITEFMAKGSLLDF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMD----PFPwqQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlIVEERKRAPMEKATTKK 492
Cdd:cd05073  96 LKSDEgskqPLP--KLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLAR-VIEDNEYTAREGAKFPI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 RtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQV----YADPDCLpRTLDFGLNVKlfwek 566
Cdd:cd05073 173 K------------------WTAPEAINFGSFTIKSDVWSFGILLMEIVtyGRIpypgMSNPEVI-RALERGYRMP----- 228
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  567 fvPTD-CPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd05073 229 --RPEnCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
330-540 1.13e-27

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: 113.06  E-value: 1.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMK-----ELIRCDEEtqKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:cd05580   2 DFEFLKTLGTGSFGRVRLVKHKDSGKYYALKilkkaKIIKLKQV--EHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrap 484
Cdd:cd05580  80 MEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV-------- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  485 mekattKKRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05580 152 ------KDRT---------YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEML 192
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
336-604 1.23e-27

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: 113.06  E-value: 1.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHK----ATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYK--DKKLNLLTEYIE 409
Cdd:cd05081  11 QLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGpgRRSLRLVMEYLP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFL-RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrapmeka 488
Cdd:cd05081  91 SGCLRDFLqRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLD--------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 ttkkrtlrkndrkKRYTVVGNP-----YWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADPDCLP------------ 551
Cdd:cd05081 162 -------------KDYYVVREPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYELF--TYCDKSCSPsaeflrmmgcer 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  552 ------RTLDFglnVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05081 227 dvpalcRLLEL---LEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
334-534 2.60e-27

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: 111.63  E-value: 2.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYK------DKKLNLLTE 406
Cdd:cd06608  11 VEVIGEGTYGKVYKARHKKTGQLAAIK-IMDIIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKkdppggDDQLWLVME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSMD----PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkr 482
Cdd:cd06608  90 YCGGGSVTDLVKGLRkkgkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQL------ 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  483 apmekattkkrtlrKNDRKKRYTVVGNPYWMAPEMLNGK-----SYDETVDIFSFGI 534
Cdd:cd06608 164 --------------DSTLGRRNTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGI 206
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
331-618 3.63e-27

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: 112.37  E-value: 3.63e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKVT----------HKATGKVMVMKelircDEETQKTF---LTEVKVMRSLD-HPNVLKFIGVLY 396
Cdd:cd05099  14 LVLGKPLGEGCFGQVVRAEaygidksrpdQTVTVAVKMLK-----DNATDKDLadlISEMELMKLIGkHKNIINLLGVCT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  397 KDKKLNLLTEYIEGGTLKDFLRSMDP----------------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIK 460
Cdd:cd05099  89 QEGPLYVIVEYAAKGNLREFLRARRPpgpdytfditkvpeeqLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  461 LDKTVVVADFGLSRLIveerKRAPMEKATTKKRTLRKndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05099 169 EDNVMKIADFGLARGV----HDIDYYKKTSNGRLPVK--------------WMAPEALFDRVYTHQSDVWSFGILMWEIF 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  541 ---GQVYADpdcLPRTLDFglnvKLFWEKF---VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALSLYLGE--LG 612
Cdd:cd05099 231 tlgGSPYPG---IPVEELF----KLLREGHrmdKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVLAAVSEeyLD 303

                ....*.
gi 5031869  613 IPLPAE 618
Cdd:cd05099 304 LSMPFE 309
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
335-597 4.02e-27

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: 110.90  E-value: 4.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVM-----VMKELirCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd05047   1 DVIGEGNFGQVLKARIKKDGLRMdaaikRMKEY--ASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLR-----SMDP-----------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL 472
Cdd:cd05047  79 PHGNLLDFLRksrvlETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  473 SRliveerkrapMEKATTKKRTLRKNDRkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIgQVYADPDClpr 552
Cdd:cd05047 159 SR----------GQEVYVKKTMGRLPVR-----------WMAIESLNYSVYTTNSDVWSYGVLLWEIV-SLGGTPYC--- 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  553 tldfGLNVKLFWEKF-------VPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05047 214 ----GMTCAELYEKLpqgyrleKPLNCDDEVYDLMRQCWREKPYERPSFAQI 261
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
335-540 4.67e-27

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: 110.79  E-value: 4.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06647  13 EKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRS--MDPfpwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkk 492
Cdd:cd06647  93 DVVTEtcMDE---GQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS----------- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  493 rtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06647 159 ---------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 197
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
330-604 4.87e-27

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: 110.90  E-value: 4.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATgKVMVMKELIRCDEETQKTFLT---EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd14145   7 ELVLEEIIGIGGFGKVYRAIWIGD-EVAVKAARHDPDEDISQTIENvrqEAKLFAMLKHPNIIALRGVCLKEPNLCLVME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLrSMDPFPWQQKVRFAKGIASGMAYLHSMCI---IHRDLNSHNCLIKL--------DKTVVVADFGLSRl 475
Cdd:cd14145  86 FARGGPLNRVL-SGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEkvengdlsNKILKITDFGLAR- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  476 iveERKRapmekaTTKkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRT 553
Cdd:cd14145 164 ---EWHR------TTK------------MSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLtGEVpFRGIDGLAVA 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  554 LDFGLNvKLFWEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14145 223 YGVAMN-KLSLP--IPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
335-605 6.47e-27

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: 110.26  E-value: 6.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMV---MKELIR-CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNL-LTEYIE 409
Cdd:cd05058   1 EVIGKGHFGCVYHGTLIDSDGQKIhcaVKSLNRiTDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLvVLPYMK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPW-QQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKa 488
Cdd:cd05058  81 HGDLRNFIRSETHNPTvKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNH- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 ttkkrtlrkndRKKRYTVvgnpYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQ---VYADPDclprtlDFGLNVKLFWE 565
Cdd:cd05058 160 -----------TGAKLPV----KWMALESLQTQKFTTKSDVWSFGVLLWELMTRgapPYPDVD------SFDITVYLLQG 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 5031869  566 KFV--PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd05058 219 RRLlqPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQIF 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
336-539 6.56e-27

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: 110.21  E-value: 6.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd08220   7 VVGRGAYGTVYLCRRKDDNKLVIIKQ-IPVEQMTKeerQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFL--RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVV-VADFGLSRLIveerkrapmekat 489
Cdd:cd08220  86 LFEYIqqRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVkIGDFGISKIL------------- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08220 153 --------SSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
337-603 6.85e-27

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: 110.52  E-value: 6.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05072  15 LGAGQFGEVWMGYYNNSTKVAV--KTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLDF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQ--QKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvEERKRAPMEKATTKKRt 494
Cdd:cd05072  93 LKSDEGGKVLlpKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVI-EDNEYTAREGAKFPIK- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVyadPDCLPRTLDFGLNVKLFWEKFVPTDC 572
Cdd:cd05072 171 -----------------WTAPEAINFGSFTIKSDVWSFGILLYEIVtyGKI---PYPGMSNSDVMSALQRGYRMPRMENC 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031869  573 PPAFFPLAAICCRLEPESRPAF----SKLEDSFEA 603
Cdd:cd05072 231 PDELYDIMKTCWKEKAEERPTFdylqSVLDDFYTA 265
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
336-604 7.70e-27

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: 110.13  E-value: 7.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKatGKVMVMKELIRCDEE----TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14146   1 IIGVGGFGKVYRATWK--GQEVAVKAARQDPDEdikaTAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVR---------FAKGIASGMAYLHS---MCIIHRDLNSHNCLI--KLD------KTVVVADFG 471
Cdd:cd14146  79 TLNRALAAANAAPGPRRARripphilvnWAVQIARGMLYLHEeavVPILHRDLKSSNILLleKIEhddicnKTLKITDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  472 LSRlivEERKRAPMEKATTkkrtlrkndrkkrYTvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDC 549
Cdd:cd14146 159 LAR---EWHRTTKMSAAGT-------------YA------WMAPEVIKSSLFSKGSDIWSYGVLLWELLtGEVpYRGIDG 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  550 LPRTLDFGLNvKLFWEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14146 217 LAVAYGVAVN-KLTLP--IPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
337-601 8.09e-27

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: 109.75  E-value: 8.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMV---MKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGT 412
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKSGKEVevaVKTLKQEHEKAGKKeFLREASVMAQLDHPCIVRLIGVC-KGEPLMLVMELAPLGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPME--KATT 490
Cdd:cd05060  82 LLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRAL-----GAGSDyyRATT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 KKRTLRKndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYAD---PDCLpRTLDFGLNVklfw 564
Cdd:cd05060 157 AGRWPLK--------------WYAPECINYGKFSSKSDVWSYGVTLWEAFsygAKPYGEmkgPEVI-AMLESGERL---- 217
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  565 EKfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:cd05060 218 PR--PEECPQEIYSIMLSCWKYRPEDRPTFSELESTF 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
334-537 8.92e-27

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: 109.72  E-value: 8.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCdEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14095   5 GRVIGDGNFAVVKECRDKATDKEYALKiiDKAKC-KGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD----KTVVVADFGLSrLIVEErkraPMek 487
Cdd:cd14095  84 DLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLA-TEVKE----PL-- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  488 attkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFG----IVLC 537
Cdd:cd14095 157 ----------------FTVCGTPTYVAPEILAETGYGLKVDIWAAGvityILLC 194
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
337-540 1.06e-26

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: 110.11  E-value: 1.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTEYIeGGTL 413
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALKKvaLRKLEGGIPNQALREIKALQACqGHPYVVKLRDVFPHGTGFVLVFEYM-LSSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKattkk 492
Cdd:cd07832  87 SEVLRDEErPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYSHQ----- 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  493 rtlrkndrkkrytvVGNPYWMAPEMLNGK-SYDETVDIFSFGIVLCEII 540
Cdd:cd07832 162 --------------VATRWYRAPELLYGSrKYDEGVDLWAVGCIFAELL 196
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
335-547 1.10e-26

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: 109.87  E-value: 1.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCD------EETQKtfltEVKVMRSLDH---PNVLKFIGVLYKDKKLNLLT 405
Cdd:cd06917   7 ELVGRGSYGAVYRGYHVKTGRVVALK-VLNLDtddddvSDIQK----EVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRsmdpfPWQQKVRFAKGIAS----GMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerk 481
Cdd:cd06917  82 DYCEGGSIRTLMR-----AGPIAERYIAVIMRevlvALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQ--- 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  482 rapmekattkkrtlrknDRKKRYTVVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEIigqVYADP 547
Cdd:cd06917 154 -----------------NSSKRSTFVGTPYWMAPEvITEGKYYDTKADIWSLGITTYEM---ATGNP 200
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
335-597 1.84e-26

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: 109.60  E-value: 1.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAI----KVTHKATGKVMVMKELIR-CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYK--DKKLNLLTEY 407
Cdd:cd05080  10 RDLGEGHFGKVSlycyDPTNDGTGEMVAVKALKAdCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQLIMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLrSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVE--ERKRapm 485
Cdd:cd05080  90 VPLGSLRDYL-PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEghEYYR--- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  486 ekattkkrtLRKNDRkkrytvvgNP-YWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADPDCLPRT--------LDF 556
Cdd:cd05080 166 ---------VREDGD--------SPvFWYAPECLKEYKFYYASDVWSFGVTLYELL--THCDSSQSPPTkflemigiAQG 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  557 GLNVKLFWEKF-------VPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05080 227 QMTVVRLIELLergerlpCPDKCPQEVYHLMKNCWETEASFRPTFENL 274
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
335-536 2.00e-26

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: 108.63  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRC---DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14073   7 ETLGKGTYGKVKLAIERATGREVAIKSIKKDkieDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattk 491
Cdd:cd14073  87 ELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLY--------------- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  492 krtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14073 152 ------SKDKLLQTFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLL 191
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
334-597 2.23e-26

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: 109.39  E-value: 2.23e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKelircdeeTQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05048  24 GELLGPSSEESAISVAIKTLKENASPK--------TQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMAHGDL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFP---------------WQQK-VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd05048  96 HEFLVRHSPHSdvgvssdddgtasslDQSDfLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLSRDIY 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 eerkrapmekATTKKRTLRKNDRKKRytvvgnpyWMAPE-MLNGKSYDETvDIFSFGIVLCEIIG---QVYadpdclprt 553
Cdd:cd05048 176 ----------SSDYYRVQSKSLLPVR--------WMPPEaILYGKFTTES-DVWSFGVVLWEIFSyglQPY--------- 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  554 ldFGLN----VKLFWEKFV---PTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05048 228 --YGYSnqevIEMIRSRQLlpcPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
337-540 2.25e-26

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: 108.68  E-value: 2.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDpFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrAPmekattkkrtlr 496
Cdd:cd06648  95 VTHTR-MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKE---VP------------ 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031869  497 kndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06648 159 -----RRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMV 197
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
337-604 3.92e-26

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 108.48  E-value: 3.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKA----TGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKD--KKLNLLTEYIE 409
Cdd:cd05079  12 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLkKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFL-RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmeka 488
Cdd:cd05079  92 SGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI------------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 ttkkrtlrkNDRKKRYTV---VGNP-YWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADPDCLPRTLDFGLN----- 559
Cdd:cd05079 160 ---------ETDKEYYTVkddLDSPvFWYAPECLIQSKFYIASDVWSFGVTLYELL--TYCDSESSPMTLFLKMIgpthg 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  560 -------VKLFWEKF---VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05079 229 qmtvtrlVRVLEEGKrlpRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
335-536 5.03e-26

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: 107.56  E-value: 5.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14098   6 DRLGSGTFAEVKKAVEVETGKMraikQIVKRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV--ADFGLSRLIveerkrapmeka 488
Cdd:cd14098  86 GDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVkiSDFGLAKVI------------ 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  489 ttKKRTLRKndrkkryTVVGNPYWMAPEMLNGKS------YDETVDIFSFGIVL 536
Cdd:cd14098 154 --HTGTFLV-------TFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLV 198
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
330-597 5.33e-26

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: 108.55  E-value: 5.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVM-----VMKELirCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNL 403
Cdd:cd05089   3 DIKFEDVIGEGNFGQVIKAMIKKDGLKMnaaikMLKEF--ASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLR-----SMDP-----------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV 467
Cdd:cd05089  81 AIEYAPYGNLLDFLRksrvlETDPafakehgtastLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  468 ADFGLSRliveerkrapMEKATTKKRTLRKNDRkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIgQVYADP 547
Cdd:cd05089 161 ADFGLSR----------GEEVYVKKTMGRLPVR-----------WMAIESLNYSVYTTKSDVWSFGVLLWEIV-SLGGTP 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  548 DClprtldfGLNVKLFWEKF-------VPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05089 219 YC-------GMTCAELYEKLpqgyrmeKPRNCDDEVYELMRQCWRDRPYERPPFSQI 268
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
335-580 5.59e-26

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: 107.83  E-value: 5.59e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd06640  10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIdLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSmDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkkr 493
Cdd:cd06640  90 LDLLRA-GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQI------------ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 tlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI------------IGQVYADPDCLPRTL--DFGLN 559
Cdd:cd06640 157 --------KRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELakgeppnsdmhpMRVLFLIPKNNPPTLvgDFSKP 228
                       250       260
                ....*....|....*....|.
gi 5031869  560 VKLFWEKFVPTDcpPAFFPLA 580
Cdd:cd06640 229 FKEFIDACLNKD--PSFRPTA 247
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
335-540 6.11e-26

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: 107.84  E-value: 6.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14046  12 QVLGKGAFGQVVKVRNKLDGRYYAIKKIkLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKSTL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEERKRAPMEKATTKKR 493
Cdd:cd14046  92 RDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAT---SNKLNVELATQDINKS 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  494 TLRKNDRKKRYTV-VGNPYWMAPEMLNGK--SYDETVDIFSFGIVLCEII 540
Cdd:cd14046 169 TSAALGSSGDLTGnVGTALYVAPEVQSGTksTYNEKVDMYSLGIIFFEMC 218
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
334-603 7.23e-26

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: 107.50  E-value: 7.23e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVlgkgFFGQAIKVTHKATGKVMVMKELIR---CDEEtQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05044   9 GEV----FEGTAKDILGDGSGETKVAVKTLRkgaTDQE-KAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELMEG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQ-------QKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL----DKTVVVADFGLSRLIVee 479
Cdd:cd05044  84 GDLLSYLRAARPTAFTpplltlkDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkdyrERVVKIGDFGLARDIY-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  480 rkrapmekattkkrtlrKNDR-KKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYAdpdclPRTld 555
Cdd:cd05044 162 -----------------KNDYyRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTlgqQPYP-----ARN-- 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  556 fglNVKLFweKFV--------PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEA 603
Cdd:cd05044 218 ---NLEVL--HFVraggrldqPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQN 268
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
335-542 8.02e-26

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: 106.95  E-value: 8.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK---ELIRCDEETqKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGg 411
Cdd:cd14002   7 ELIGEGSFGKVYKGRRKYTGQVVALKfipKRGKSEKEL-RNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekaTTK 491
Cdd:cd14002  85 ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAM------------SCN 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  492 KRTLRkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI-IGQ 542
Cdd:cd14002 153 TLVLT--------SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELfVGQ 196
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
328-539 8.81e-26

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: 106.89  E-value: 8.81e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGqAIKVThKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd05113   3 PKDLTFLKELGTGQFG-VVKYG-KWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMe 486
Cdd:cd05113  81 MANGCLLNYLREMRKrFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSV- 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  487 katTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05113 160 ---GSKFPVR---------------WSPPEVLMYSKFSSKSDVWAFGVLMWEV 194
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
330-602 9.46e-26

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: 107.12  E-value: 9.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIK-VTHKATG---KVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLT 405
Cdd:cd05056   7 DITLGRCIGEGQFGDVYQgVYMSPENekiAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVI-TENPVWIVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFL-RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkrap 484
Cdd:cd05056  86 ELAPLGELRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDES---- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  485 MEKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIigqvyadpdclprtLDFGlnVKLF- 563
Cdd:cd05056 162 YYKASKGKLPIK---------------WMAPESINFRRFTSASDVWMFGVCMWEI--------------LMLG--VKPFq 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  564 WEKF--------------VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd05056 211 GVKNndvigriengerlpMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
328-542 1.07e-25

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: 106.65  E-value: 1.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQKT------FLTEVKVMRSLDHPNVLKFIGVL--YKDK 399
Cdd:cd06653   1 PVNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQ-VPFDPDSQETskevnaLECEIQLLKNLRHDRIVQYYGCLrdPEEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 KLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvee 479
Cdd:cd06653  80 KLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRI--- 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  480 rKRAPMEKATTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQ 542
Cdd:cd06653 157 -QTICMSGTGIK-------------SVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTE 205
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
330-536 1.32e-25

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 106.92  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMK-----ELIRcdEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:cd05581   2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldkrHIIK--EKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrA 483
Cdd:cd05581  80 LEYAPNGDLLEYIRKYGSLD-EKCTRFyTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPD---S 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  484 PMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd05581 156 SPESTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCII 208
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
325-601 1.50e-25

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: 106.73  E-value: 1.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  325 IFRPCDLIHGEVLGKGFFGQAIK---VTHKATGKVMVMKELIRCDE--ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKdK 399
Cdd:cd05057   3 IVKETELEKGKVLGSGAFGTVYKgvwIPEGEKVKIPVAIKVLREETgpKANEEILDEAYVMASVDHPHLVRLLGICLS-S 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 KLNLLTEYIEGGTLKDFLRS-MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVE 478
Cdd:cd05057  82 QVQLITQLMPLGCLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  479 ERKRApmeKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYADPDC--LPRT 553
Cdd:cd05057 162 DEKEY---HAEGGKVPIK---------------WMALESIQYRIYTHKSDVWSYGVTVWELMtfgAKPYEGIPAveIPDL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  554 LDFGLNVKLfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:cd05057 224 LEKGERLPQ------PPICTIDVYMVLVKCWMIDAESRPTFKELANEF 265
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
337-539 2.00e-25

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: 106.74  E-value: 2.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLY--KDKKLNLLTEYIEGGT 412
Cdd:cd06621   9 LGEGAGGSVTKCRLRNTKTIFALK-TITTDpnPDVQKQILRELEINKSCASPYIVKYYGAFLdeQDSSIGIAMEYCEGGS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQ--QKV--RFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmeka 488
Cdd:cd06621  88 LDSIYKKVKKKGGRigEKVlgKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVN---------- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  489 ttkkrtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06621 158 ------------SLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEV 196
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
335-599 2.44e-25

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: 105.50  E-value: 2.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIK-VTHKATGKVM-VMKELIRCDEETQKT----FLTEVKVMRSLDHPNVLKFIGVLYkDKKLNLLTEYI 408
Cdd:cd05040   1 EKLGDGSFGVVRRgEWTTPSGKVIqVAVKCLKSDVLSQPNamddFLKEVNAMHSLDHPNLIRLYGVVL-SSPLMMVTELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMek 487
Cdd:cd05040  80 PLGSLLDRLRkDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDHYVM-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  488 attkkrtlrkNDRKKRytvvgnPY-WMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADPDCLprtldfGLNVKLFWEK 566
Cdd:cd05040 158 ----------QEHRKV------PFaWCAPESLKTRKFSHASDVWMFGVTLWEMF--TYGEEPWL------GLNGSQILEK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031869  567 F--------VPTDCPPAFFPLAAICCRLEPESRPAFSKLED 599
Cdd:cd05040 214 IdkegerleRPDDCPQDIYNVMLQCWAHKPADRPTFVALRD 254
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
335-540 2.46e-25

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 106.25  E-value: 2.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd07833   7 GVVGEGAYGVVLKCRNKATGEIVAIKKFkeSEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVERTL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRS---MDP-----FPWQqkvrfakgIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvEERKRAP 484
Cdd:cd07833  87 LELLEASpggLPPdavrsYIWQ--------LLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARAL-TARPASP 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  485 mekattkkrtlrkndrkkrYT-VVGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07833 158 -------------------LTdYVATRWYRAPELLVGdTNYGKPVDVWAIGCIMAELL 196
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
337-543 2.65e-25

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


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 105.71  E-value: 2.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATG-----KVMVMKELIR-----CDEETQKTFL----TEVKVMRSLDHPNVLKFIGVLY--KDKK 400
Cdd:cd14008   1 LGRGSFGKVKLALDTETGqlyaiKIFNKSRLRKrregkNDRGKIKNALddvrREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  401 LNLLTEYIEGGTLKDFLR--SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLive 478
Cdd:cd14008  81 LYLVLEYCEGGPVMELDSgdRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM--- 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  479 erkrapMEKATTkkrTLRKNdrkkrytvVGNPYWMAPEMLNG--KSYD-ETVDIFSFGIVL-CEIIGQV 543
Cdd:cd14008 158 ------FEDGND---TLQKT--------AGTPAFLAPELCDGdsKTYSgKAADIWALGVTLyCLVFGRL 209
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
331-605 3.07e-25

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: 105.79  E-value: 3.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIK--------VTHKATGKVMVMkelircDEETQKT---FLTEVKVMRSLDHPNVLKFIGVLYKDK 399
Cdd:cd14204   9 LSLGKVLGEGEFGSVMEgelqqpdgTNHKVAVKTMKL------DNFSQREieeFLSEAACMKDFNHPNVIRLLGVCLEVG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 -----KLNLLTEYIEGGTLKDFLRS----MDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVA 468
Cdd:cd14204  83 sqripKPMVILPFMKYGDLHSFLLRsrlgSGPqhVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  469 DFGLSRLIVEerkrapmekattkkrtlrkNDRKKRYTVVGNPY-WMAPEMLNGKSYDETVDIFSFGIVLCEIigqvyADP 547
Cdd:cd14204 163 DFGLSKKIYS-------------------GDYYRQGRIAKMPVkWIAVESLADRVYTVKSDVWAFGVTMWEI-----ATR 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  548 DCLPRTldfGLNVKLFWEKFV-------PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd14204 219 GMTPYP---GVQNHEIYDYLLhghrlkqPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLL 280
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
337-594 3.34e-25

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: 105.82  E-value: 3.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKvthkatgkvMVMKELIRCDEETQ---KT------------FLTEVKVMRSLDHPNVLKFIGVLYKDKKL 401
Cdd:cd05061  14 LGQGSFGMVYE---------GNARDIIKGEAETRvavKTvnesaslrerieFLNEASVMKGFTCHHVVRLLGVVSKGQPT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSM---------DPFP-WQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFG 471
Cdd:cd05061  85 LVVMELMAHGDLKSYLRSLrpeaennpgRPPPtLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  472 LSRLIVEERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIG------QVYA 545
Cdd:cd05061 165 MTRDIYETDYYRKGGKGLLPVR------------------WMAPESLKDGVFTTSSDMWSFGVVLWEITSlaeqpyQGLS 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  546 DPDCLPRTLDFGlnvklFWEKfvPTDCPPAFFPLAAICCRLEPESRPAF 594
Cdd:cd05061 227 NEQVLKFVMDGG-----YLDQ--PDNCPERVTDLMRMCWQFNPKMRPTF 268
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
335-597 3.35e-25

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: 105.54  E-value: 3.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKtFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd06641  10 EKIGKGSFGEVFKGIDNRTQKVVAIKiiDLEEAEDEIED-IQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSmDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkk 492
Cdd:cd06641  89 ALDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQI----------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFglnvklfwekFVPTDC 572
Cdd:cd06641 157 ---------KRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLF----------LIPKNN 217
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031869  573 PP--------AFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd06641 218 PPtlegnyskPLKEFVEACLNKEPSFRPTAKEL 250
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
331-597 3.63e-25

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: 106.23  E-value: 3.63e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQA----IKVTHKATGK-----------VMVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIG 393
Cdd:cd05095   7 LTFKEKLGEGQFGEVhlceAEGMEKFMDKdfalevsenqpVLVAVKMLRADanKNARNDFLKEIKIMSRLKDPNIIRLLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  394 VLYKDKKLNLLTEYIEGGTLKDFLRSMDP------------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL 461
Cdd:cd05095  87 VCITDDPLCMITEYMENGDLNQFLSRQQPegqlalpsnaltVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  462 DKTVVVADFGLSRLIVEERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAPE-MLNGKsYDETVDIFSFGIVLCEII 540
Cdd:cd05095 167 NYTIKIADFGMSRNLYSGDYYRIQGRAVLPIR------------------WMSWEsILLGK-FTTASDVWAFGVTLWETL 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031869  541 G----QVYA---DPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05095 228 TfcreQPYSqlsDEQVIENTGEFFRDQGRQTYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEI 291
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
334-539 4.05e-25

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: 105.21  E-value: 4.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGqAIKVTHKATGKVMVMK--ELIRCDEET-QKTFLT---EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd06631   6 GNVLGKGAYG-TVYCGLTSTGQLIAVKqvELDTSDKEKaEKEYEKlqeEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapMEK 487
Cdd:cd06631  85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCI------NLS 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  488 ATTKKRTLRkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06631 159 SGSQSQLLK--------SMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEM 202
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
337-602 5.05e-25

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 105.15  E-value: 5.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05071  17 LGQGCFGEVWMGTWNGTTRVAI--KTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMSKGSLLDF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LR----SMDPFPwqQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkk 492
Cdd:cd05071  94 LKgemgKYLRLP--QLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLI---------------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVyADPDCLPR-TLDfglNVKLFWEKFVP 569
Cdd:cd05071 156 ---EDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTtkGRV-PYPGMVNReVLD---QVERGYRMPCP 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031869  570 TDCPPAFFPLAAICCRLEPESRPAFSKLEDSFE 602
Cdd:cd05071 229 PECPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
335-540 6.08e-25

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: 105.58  E-value: 6.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06655  25 EKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRS--MDPfpwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkk 492
Cdd:cd06655 105 DVVTEtcMDE---AQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQS----------- 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  493 rtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06655 171 ---------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 209
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
334-540 7.09e-25

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: 104.31  E-value: 7.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd06626   5 GNKIGEGTFGKVYTAVNLDTGELMAMKEirFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLN------SHNCLIKLdktvvvADFGLSRLIveerkrapm 485
Cdd:cd06626  85 TLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKpaniflDSNGLIKL------GDFGSAVKL--------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  486 ekattkKRTLRKNDRKKRYTVVGNPYWMAPEMLNG---KSYDETVDIFSFGIVLCEII 540
Cdd:cd06626 150 ------KNNTTTMAPGEVNSLVGTPAYMAPEVITGnkgEGHGRAADIWSLGCVVLEMA 201
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
335-597 9.30e-25

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 104.67  E-value: 9.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQ-------------AIKVTHKATGKVMVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDK 399
Cdd:cd05097  11 EKLGEGQFGEvhlceaeglaeflGEGAPEFDGQPVLVAVKMLRADvtKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 KLNLLTEYIEGGTLKDFL------------RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV 467
Cdd:cd05097  91 PLCMITEYMENGDLNQFLsqreiestfthaNNIPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  468 ADFGLSRLIVEERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAPE-MLNGKsYDETVDIFSFGIVLCEIIG----- 541
Cdd:cd05097 171 ADFGMSRNLYSGDYYRIQGRAVLPIR------------------WMAWEsILLGK-FTTASDVWAFGVTLWEMFTlckeq 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  542 --QVYADPDCLPRTLDFGLNV--KLFWEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05097 232 pySLLSDEQVIENTGEFFRNQgrQIYLSQ--TPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
337-536 9.75e-25

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: 103.75  E-value: 9.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRC---DEETQKTFlTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14072   8 IGKGNFAKVKLARHVLTGREVAIKIIDKTqlnPSSLQKLF-REVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQ-KVRFaKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApmekattkk 492
Cdd:cd14072  87 FDYLVAHGRMKEKEaRAKF-RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLD--------- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  493 rtlrkndrkkryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14072 157 ------------TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVIL 189
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
335-540 9.92e-25

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: 104.72  E-value: 9.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVT-HKATGKVMVMKElircdeeTQKT-FLTEVKVMRS--LDHPNVLKFIGV----LYKDKKLNLLTE 406
Cdd:cd14053   1 EIKARGRFGAVWKAQyLNRLVAVKIFPL-------QEKQsWLTEREIYSLpgMKHENILQFIGAekhgESLEAEYWLITE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFL--RSMDpfpWQQKVRFAKGIASGMAYLHS----------MCIIHRDLNSHNCLIKLDKTVVVADFGLSr 474
Cdd:cd14053  74 FHERGSLCDYLkgNVIS---WNELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLA- 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  475 LIVEERKraPMEKATTKKRTlrkndrkKRYtvvgnpywMAPEMLNGK-SYDET----VDIFSFGIVLCEII 540
Cdd:cd14053 150 LKFEPGK--SCGDTHGQVGT-------RRY--------MAPEVLEGAiNFTRDaflrIDMYAMGLVLWELL 203
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
335-540 1.17e-24

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: 104.42  E-value: 1.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06654  26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRS--MDPfpwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkk 492
Cdd:cd06654 106 DVVTEtcMDE---GQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS----------- 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  493 rtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06654 172 ---------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 210
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
332-539 1.43e-24

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: 103.66  E-value: 1.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRC------DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd06630   3 LKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCrnssseQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIklDKT---VVVADFGLSrliveerkr 482
Cdd:cd06630  83 EWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV--DSTgqrLRIADFGAA--------- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  483 APMEKATTKKRTLRKNdrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06630 152 ARLASKGTGAGEFQGQ-------LLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEM 201
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
337-540 1.64e-24

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 103.16  E-value: 1.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHK--ATGKVMVMKELIR-CDEETQK----TFLTEVKVMRSLDHPNVLKFIGVLYKDK-KLNLLTEYI 408
Cdd:cd13994   1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRrDDESKRKdyvkRLTSEYIISSKLHHPNIVKVLDLCQDLHgKWCLVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS-RLIVEERKRAPMEK 487
Cdd:cd13994  81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKESPMSA 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  488 AttkkrtlrkndrkkrytVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVLCEII 540
Cdd:cd13994 161 G-----------------LCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALF 197
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
335-540 1.76e-24

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: 104.03  E-value: 1.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd06656  25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRS--MDPfpwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkk 492
Cdd:cd06656 105 DVVTEtcMDE---GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS----------- 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  493 rtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06656 171 ---------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 209
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
328-597 1.85e-24

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 103.69  E-value: 1.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFG---QAIKVTHKATGKVMVMKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYKD-KKLN 402
Cdd:cd05043   5 RERVTLSDLLQEGTFGrifHGILRDEKGKEEEVLVKTVKDHASEIQVTmLLQESSLLYGLSHQNLLPILHVCIEDgEKPM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 LLTEYIEGGTLKDFLRSMDPFPW--------QQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSR 474
Cdd:cd05043  85 VLYPYMNWGNLKLFLQQCRLSEAnnpqalstQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  475 LIVeerkraPMEkattkkrtlrkndrkkrYTVVG-NPY----WMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYA- 545
Cdd:cd05043 165 DLF------PMD-----------------YHCLGdNENrpikWMSLESLVNKEYSSASDVWSFGVLLWELMtlgQTPYVe 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  546 -DPDCLPRTLDFGLNVKLfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05043 222 iDPFEMAAYLKDGYRLAQ------PINCPDELFAVMACCWALDPEERPSFQQL 268
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
335-540 1.98e-24

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: 103.74  E-value: 1.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGg 411
Cdd:cd07860   6 EKIGEGTYGVVYKARNKLTGEVVALKK-IRLDTETEgvpSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQ- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMEKAT 489
Cdd:cd07860  84 DLKKFMDASALtgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF-----GVPVRTYT 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 TKKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07860 159 HEVVTL---------------WYRAPEILLGcKYYSTAVDIWSLGCIFAEMV 195
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
337-595 2.00e-24

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: 103.24  E-value: 2.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIK--VTHKATGK------VMVMKELirCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd05036  14 LGQGAFGEVYEgtVSGMPGDPsplqvaVKTLPEL--CSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQK-------VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL---DKTVVVADFGLSRLIVe 478
Cdd:cd05036  92 AGGDLKSFLRENRPRPEQPSsltmldlLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCkgpGRVAKIGDFGMARDIY- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  479 erkRAPMekattkkrtLRKNDRK----KrytvvgnpyWMAPE-MLNGKSYDETvDIFSFGIVLCEIIGQVYADPDClpRT 553
Cdd:cd05036 171 ---RADY---------YRKGGKAmlpvK---------WMPPEaFLDGIFTSKT-DVWSFGVLLWEIFSLGYMPYPG--KS 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  554 ldfglNVKLFweKFV--------PTDCPPAFFPLAAICCRLEPESRPAFS 595
Cdd:cd05036 227 -----NQEVM--EFVtsggrmdpPKNCPGPVYRIMTQCWQHIPEDRPNFS 269
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
363-538 2.09e-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: 103.14  E-value: 2.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  363 IRCDEETQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAY 441
Cdd:cd14010  30 IKCVDKSKRPEVLnEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHY 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  442 LHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKrtlrKNDRKKRYTVVGNPYWMAPEMLNGK 521
Cdd:cd14010 110 IHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEILKELFGQFSDEGN----VNKVSKKQAKRGTPYYMAPELFQGG 185
                       170
                ....*....|....*..
gi 5031869  522 SYDETVDIFSFGIVLCE 538
Cdd:cd14010 186 VHSFASDLWALGCVLYE 202
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
337-595 2.37e-24

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: 103.37  E-value: 2.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVThkATGKV------MVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd05050  13 IGQGAFGRVFQAR--APGLLpyepftMVAVKMLKEEasADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFpWQ-----------------------QKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTV 465
Cdd:cd05050  91 AYGDLNEFLRHRSPR-AQcslshstssarkcglnplplsctEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMVV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  466 VVADFGLSRLIVEERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIG---Q 542
Cdd:cd05050 170 KIADFGLSRNIYSADYYKASENDAIPIR------------------WMPPESIFYNRYTTESDVWAYGVVLWEIFSygmQ 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  543 VYadpdclprtldFGLN----VKLFWEKFV---PTDCPPAFFPLAAICCRLEPESRPAFS 595
Cdd:cd05050 232 PY-----------YGMAheevIYYVRDGNVlscPDNCPLELYNLMRLCWSKLPSDRPSFA 280
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
335-601 2.38e-24

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: 102.95  E-value: 2.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKtfltEVKVMRSLDHPNVLKFIGV----------------LYKD 398
Cdd:cd14047  12 ELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAER----EVKALAKLDHPNIVRYNGCwdgfdydpetsssnssRSKT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  399 KKLNLLTEYIEGGTLKDFLRSM-----DPFPWQQKVRfakGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLs 473
Cdd:cd14047  88 KCLFIQMEFCEKGTLESWIEKRngeklDKVLALEIFE---QITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGL- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  474 rliveerkrapmekATTKKRTLRKNDRKkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqvyadpdclpRT 553
Cdd:cd14047 164 --------------VTSLKNDGKRTKSK------GTLSYMSPEQISSQDYGKEVDIYALGLILFELL-----------HV 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  554 LDFGLNVKLFWEKFVPTDCPPAF---FPL-AAICCRL---EPESRPAFSKLEDSF 601
Cdd:cd14047 213 CDSAFEKSKFWTDLRNGILPDIFdkrYKIeKTIIKKMlskKPEDRPNASEILRTL 267
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
335-599 2.47e-24

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: 103.53  E-value: 2.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQktflTEVKVMRSL-DHPNVLKFIGVLYKDKK-----LNLLT 405
Cdd:cd06639  28 ETIGKGTYGKVYKVTNKKDGSlaaVKILDPISDVDEEIE----AEYNILRSLpNHPNVVKFYGMFYKADQyvggqLWLVL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMdpfpWQQKVRFAKGIAS--------GMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd06639 104 ELCNGGSVTELVKGL----LKCGQRLDEAMISyilygallGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 EERkrapmekattkkrtLRKNdrkkryTVVGNPYWMAPEMLNGK-----SYDETVDIFSFGIVLCEIigqvyADPDclPR 552
Cdd:cd06639 180 SAR--------------LRRN------TSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIEL-----ADGD--PP 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  553 TLDFGLNVKLFWekfVPTDCPP----------AFFPLAAICCRLEPESRPAFSKLED 599
Cdd:cd06639 233 LFDMHPVKALFK---IPRNPPPtllnpekwcrGFSHFISQCLIKDFEKRPSVTHLLE 286
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
334-542 3.81e-24

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: 102.43  E-value: 3.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQKT------FLTEVKVMRSLDHPNVLKFIGVLY--KDKKLNLLT 405
Cdd:cd06652   7 GKLLGQGAFGRVYLCYDADTGRELAVKQ-VQFDPESPETskevnaLECEIQLLKNLLHERIVQYYGCLRdpQERTLSIFM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPM 485
Cdd:cd06652  86 EYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASK-----RLQTIC 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  486 EKATTKKrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQ 542
Cdd:cd06652 161 LSGTGMK------------SVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTE 205
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
337-540 4.06e-24

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: 103.14  E-value: 4.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd06659  29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LrSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkrtlr 496
Cdd:cd06659 109 V-SQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI-------------------- 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031869  497 KNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06659 168 SKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMV 211
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
335-539 5.51e-24

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: 102.40  E-value: 5.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQktflTEVKVMRSL-DHPNVLKFIGVLYKDKKLN-----LLT 405
Cdd:cd06638  24 ETIGKGTYGKVFKVLNKKNGSkaaVKILDPIHDIDEEIE----AEYNILKALsDHPNVVKFYGMYYKKDVKNgdqlwLVL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMdpfpWQQKVRFAKGIAS--------GMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd06638 100 ELCNGGSVTDLVKGF----LKRGERMEEPIIAyilhealmGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  478 EERKRapmekattkkrtlrkndrkkRYTVVGNPYWMAPEMLN-----GKSYDETVDIFSFGIVLCEI 539
Cdd:cd06638 176 STRLR--------------------RNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIEL 222
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
336-597 9.05e-24

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: 100.93  E-value: 9.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd08530   7 KLGKGSYGSVYKVKRLSDNQVYALKEvnLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLR----SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekat 489
Cdd:cd08530  87 SKLISkrkkKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVL------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkKRTLrkndrkkRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYadpdclP---RTLDfGLNVKLFWEK 566
Cdd:cd08530 154 --KKNL-------AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRP------PfeaRTMQ-ELRYKVCRGK 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  567 FVPtdcPPAFFP--LAAICCRL---EPESRPAFSKL 597
Cdd:cd08530 218 FPP---IPPVYSqdLQQIIRSLlqvNPKKRPSCDKL 250
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
334-536 1.01e-23

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: 100.79  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14185   5 GRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIeSEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD----KTVVVADFGLSRLIVeerkrapmeka 488
Cdd:cd14185  85 LFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNpdksTTLKLADFGLAKYVT----------- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  489 ttkkrtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14185 154 ------------GPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVIL 189
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
324-601 1.11e-23

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: 101.19  E-value: 1.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  324 QIFRPCDLIHGEVLGKGFFG---QAIKVTHKATGKVMVMKELIRcDEETQKTFlTEVK----VMRSLDHPNVLKFIGVLy 396
Cdd:cd05111   2 RIFKETELRKLKVLGSGVFGtvhKGIWIPEGDSIKIPVAIKVIQ-DRSGRQSF-QAVTdhmlAIGSLDHAYIVRLLGIC- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  397 KDKKLNLLTEYIEGGTLKDFLR----SMDPfpwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL 472
Cdd:cd05111  79 PGASLQLVTQLLPLGSLLDHVRqhrgSLGP---QLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  473 SRLiveerkrapmekattkkrtLRKNDRKKRYTVVGNPY-WMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYAD-- 546
Cdd:cd05111 156 ADL-------------------LYPDDKKYFYSEAKTPIkWMALESIHFGKYTHQSDVWSYGVTVWEMMtfgAEPYAGmr 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  547 PDCLPRTLDFGlnvklfwEKFV-PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSF 601
Cdd:cd05111 217 LAEVPDLLEKG-------ERLAqPQICTIDVYMVMVKCWMIDENIRPTFKELANEF 265
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
331-597 1.18e-23

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: 101.79  E-value: 1.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKVTHKATGK--------VMVMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKL 401
Cdd:cd05055  37 LSFGKTLGAGAFGKVVEATAYGLSKsdavmkvaVKMLKPTAHSSE--REALMSELKIMSHLgNHENIVNLLGACTIGGPI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRS-MDPF-PWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvee 479
Cdd:cd05055 115 LVITEYCCYGDLLNFLRRkRESFlTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDI--- 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  480 rkrapmekattkkrtlrKNDrkKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYADpdcLPR 552
Cdd:cd05055 192 -----------------MND--SNYVVKGNARlpvkWMAPESIFNCVYTFESDVWSYGILLWEIFslgSNPYPG---MPV 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031869  553 TLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05055 250 DSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQI 294
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
335-543 1.25e-23

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: 101.68  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIK--VTHKATGK-VMVMKELIRCDE----ETQKTFLTEVkvmrSLDHPNVLKFIGVLYK----DKKLNL 403
Cdd:cd14055   1 KLVGKGRFAEVWKakLKQNASGQyETVAVKIFPYEEyaswKNEKDIFTDA----SLKHENILQFLTAEERgvglDRQYWL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSmDPFPWQQKVRFAKGIASGMAYLHS---------MCIIHRDLNSHNCLIKLDKTVVVADFGLSr 474
Cdd:cd14055  77 ITAYHENGSLQDYLTR-HILSWEDLCKMAGSLARGLAHLHSdrtpcgrpkIPIAHRDLKSSNILVKNDGTCVLADFGLA- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  475 lIVEERKRAPMEKATTKKrtlrkndrkkrytvVGNPYWMAPEMLNGK-------SYDETvDIFSFGIVL------CEIIG 541
Cdd:cd14055 155 -LRLDPSLSVDELANSGQ--------------VGTARYMAPEALESRvnledleSFKQI-DVYSMALVLwemasrCEASG 218

                ..
gi 5031869  542 QV 543
Cdd:cd14055 219 EV 220
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
356-597 1.46e-23

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: 101.55  E-value: 1.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  356 VMVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMD------------ 421
Cdd:cd05096  47 LLVAVKILRPDanKNARNDFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHlddkeengndav 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  422 ----PFP---WQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapmekattkkrT 494
Cdd:cd05096 127 ppahCLPaisYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSR-------------------N 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 LRKNDRkkrYTVVGNPY----WMAPE-MLNGKsYDETVDIFSFGIVLCEII----GQVYA---DPDCLPRTLDFGLNVKL 562
Cdd:cd05096 188 LYAGDY---YRIQGRAVlpirWMAWEcILMGK-FTTASDVWAFGVTLWEILmlckEQPYGeltDEQVIENAGEFFRDQGR 263
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031869  563 FWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05096 264 QVYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
335-597 1.74e-23

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: 100.52  E-value: 1.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKtFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd06642  10 ERIGKGSFGEVYKGIDNRTKEVVAIKiiDLEEAEDEIED-IQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRsmdPFPWQQK--VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekatt 490
Cdd:cd06642  89 ALDLLK---PGPLEETyiATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQI--------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 kkrtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFglnvklfwekFVPT 570
Cdd:cd06642 157 -----------KRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLF----------LIPK 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031869  571 DCPPA--------FFPLAAICCRLEPESRPAFSKL 597
Cdd:cd06642 216 NSPPTlegqhskpFKEFVEACLNKDPRFRPTAKEL 250
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
337-603 1.76e-23

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: 100.53  E-value: 1.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05070  17 LGNGQFGEVWMGTWNGNTKVAI--KTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMSKGSLLDF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkrt 494
Cdd:cd05070  94 LKDGEgrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLI------------------ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQvyadpdclPRTLDFGLNVKLFWEKF------- 567
Cdd:cd05070 156 -EDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTK--------GRVPYPGMNNREVLEQVergyrmp 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5031869  568 VPTDCPPAFFPLAAICCRLEPESRPAF----SKLEDSFEA 603
Cdd:cd05070 227 CPQDCPISLHELMIHCWKKDPEERPTFeylqGFLEDYFTA 266
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
337-604 1.85e-23

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 100.88  E-value: 1.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQkTFLTEVKVMRSLDHPNVLKFIGVLYKDKkLNLLTEYIEGGTLKDF 416
Cdd:cd14149  20 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQ-AFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKH 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLsrliveerkrapmekATTKKRTl 495
Cdd:cd14149  98 LHVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL---------------ATVKSRW- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  496 rkNDRKKRYTVVGNPYWMAPE---MLNGKSYDETVDIFSFGIVLCEI-------------------IGQVYADPDClprt 553
Cdd:cd14149 162 --SGSQQVEQPTGSILWMAPEvirMQDNNPFSFQSDVYSYGIVLYELmtgelpyshinnrdqiifmVGRGYASPDL---- 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  554 ldfglnVKLFwekfvpTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14149 236 ------SKLY------KNCPKAMKRLVADCIKKVKEERPLFPQILSSIELL 274
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
334-605 1.85e-23

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: 100.52  E-value: 1.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKvtHKATGKVMV-MKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKdKKLNLLTEYIEGGT 412
Cdd:cd14151  13 GQRIGSGSFGTVYK--GKWHGDVAVkMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLsrliveerkrapmekATTK 491
Cdd:cd14151  90 LYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL---------------ATVK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 KRTLRKNDRKKrytVVGNPYWMAPE---MLNGKSYDETVDIFSFGIVLCEII-GQV-YADPDCLPRTLDF----GLNVKL 562
Cdd:cd14151 155 SRWSGSHQFEQ---LSGSILWMAPEvirMQDKNPYSFQSDVYAFGIVLYELMtGQLpYSNINNRDQIIFMvgrgYLSPDL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031869  563 fweKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd14151 232 ---SKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLA 271
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
335-540 1.92e-23

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: 100.06  E-value: 1.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATG------KVMVMKELIRCDEETqktFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSGArevvavKCVSKSSLNKASTEN---LLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI-KLDKTVV-VADFGLSRLIveerkrapme 486
Cdd:cd14121  78 SGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLsSRYNPVLkLADFGFAQHL---------- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  487 KATTKKRTLRkndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14121 148 KPNDEAHSLR-----------GSPLYMAPEMILKKKYDARVDLWSVGVILYECL 190
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
337-603 1.93e-23

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: 100.53  E-value: 1.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVmkELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTKVAI--KTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMGKGSLLDF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkrt 494
Cdd:cd05069  97 LKEGDGkyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI------------------ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVyADPDCLPRtlDFGLNVKLFWEKFVPTDC 572
Cdd:cd05069 159 -EDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtkGRV-PYPGMVNR--EVLEQVERGYRMPCPQGC 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031869  573 PPAFFPLAAICCRLEPESRPAF----SKLEDSFEA 603
Cdd:cd05069 235 PESLHELMKLCWKKDPDERPTFeyiqSFLEDYFTA 269
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
336-597 2.02e-23

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: 100.62  E-value: 2.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEET-QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd05046  12 TLGRGEFGEVFLAKAKGIEeeggeTLVLVKALQKTKDENlQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLR---------SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveer 480
Cdd:cd05046  92 LGDLKQFLRatkskdeklKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLS------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 krapmekattkKRTLRKNDRKKRYTVVgnPY-WMAPEMLNGKSYDETVDIFSFGIVLCEIIGQV------YADPDCLPRt 553
Cdd:cd05046 165 -----------KDVYNSEYYKLRNALI--PLrWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGelpfygLSDEEVLNR- 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031869  554 LDFGlnvKLFWEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05046 231 LQAG---KLELP--VPEGCPSRLYKLMTRCWAVNPKDRPSFSEL 269
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
354-598 2.50e-23

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: 99.93  E-value: 2.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  354 GKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMD-PFPWQQKVRFA 432
Cdd:cd14045  30 GRTVAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDiPLNWGFRFSFA 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  433 KGIASGMAYLHSMCIIHRDLNSHNCLIKlDKTVV-VADFGLSRLiveeRKRAPMEKATTKKRTLRKndrkkrytvvgnpY 511
Cdd:cd14045 110 TDIARGMAYLHQHKIYHGRLKSSNCVID-DRWVCkIADYGLTTY----RKEDGSENASGYQQRLMQ-------------V 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  512 WMAPEMLNGKSYDETV--DIFSFGIVLCEIIGQVYADPDCLPrTLDFGLNVKLFWEKFVPTD----CPPAFFPLAAICCR 585
Cdd:cd14045 172 YLPPENHSNTDTEPTQatDVYSYAIILLEIATRNDPVPEDDY-SLDEAWCPPLPELISGKTEnscpCPADYVELIRRCRK 250
                       250
                ....*....|...
gi 5031869  586 LEPESRPAFSKLE 598
Cdd:cd14045 251 NNPAQRPTFEQIK 263
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
330-604 2.52e-23

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: 100.12  E-value: 2.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQaikvTHKAT--GKVMV-MKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd14063   1 ELEIKEVIGKGRFGR----VHRGRwhGDVAIkLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRS-MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKtVVVADFGLSRLI-VEERKRAP 484
Cdd:cd14063  77 LCKGRTLYSLIHErKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGR-VVITDFGLFSLSgLLQPGRRE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  485 MekattkkrtlrkndrkkryTVVGNPYW---MAPEMLNG----------KSYDETVDIFSFGIVLCEIIgqVYADP-DCL 550
Cdd:cd14063 156 D-------------------TLVIPNGWlcyLAPEIIRAlspdldfeesLPFTKASDVYAFGTVWYELL--AGRWPfKEQ 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  551 PRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14063 215 PAESIIWQVGCGKKQSLSQLDIGREVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
336-540 3.10e-23

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: 99.23  E-value: 3.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLY--KDKKLNLLTEYIe 409
Cdd:cd05118   6 KIGEGAFGTVWLARDKVTGEKVAIK-KIKNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEhrGGNHLCLVFELM- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVV-VADFGLSRLIVEerkrapmek 487
Cdd:cd05118  84 GMNLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLkLADFGLARSFTS--------- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  488 attkkrtlrkndrkKRYTVVGNPYW-MAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd05118 155 --------------PPYTPYVATRWyRAPEVLLGAKpYGSSIDIWSLGCILAELL 195
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
334-537 3.40e-23

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 99.26  E-value: 3.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEE---TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14116  10 GRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEkagVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPmekatt 490
Cdd:cd14116  90 GTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS-------VHAP------ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  491 kkrtlrkndRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGiVLC 537
Cdd:cd14116 157 ---------SSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLG-VLC 193
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
336-541 4.38e-23

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: 100.68  E-value: 4.38e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRC--DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN-----LLTEYI 408
Cdd:cd07834   7 PIGSGAYGVVCSAYDKRTGRKVAIKKISNVfdDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPEEfndvyIVTELM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EggT-LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPM-E 486
Cdd:cd07834  87 E--TdLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDEDKGFLtE 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  487 KATTKkrtlrkndrkkrytvvgnpYWMAPE-MLNGKSYDETVDIFSFGIVLCEIIG 541
Cdd:cd07834 165 YVVTR-------------------WYRAPElLLSSKKYTKAIDIWSVGCIFAELLT 201
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
336-540 4.46e-23

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: 101.21  E-value: 4.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCD----EETQKtFLTEVKVMRSLDHPNVLKfigvLY---KDKK-LNLLTEY 407
Cdd:cd05573   8 VIGRGAFGEVWLVRDKDTGQVYAMKILRKSDmlkrEQIAH-VRAERDILADADSPWIVR----LHyafQDEDhLYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS-RLI--------V 477
Cdd:cd05573  83 MPGGDLMNLLIKYDVFP-EETARFyIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtKMNksgdresyL 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  478 EERKRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05573 162 NDSVNTLFQDNVLARRRPHKQRRVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEML 224
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
330-539 4.54e-23

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: 99.46  E-value: 4.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQ--------AIKVTHKATGKVMVMKELirCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKL 401
Cdd:cd05049   6 TIVLKRELGEGAFGKvflgecynLEPEQDKMLVAVKTLKDA--SSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSMDP--------------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV 467
Cdd:cd05049  84 LMVFEYMEHGDLNKFLRSHGPdaaflasedsapgeLTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKI 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  468 ADFGLSRLIVeerkrapmekattkkrtlrKNDrkkRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05049 164 GDFGMSRDIY-------------------STD---YYRVGGHTMlpirWMPPESILYRKFTTESDVWSFGVVLWEI 217
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
337-539 4.58e-23

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: 98.73  E-value: 4.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCD------EETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd08218   8 IGEGSFGKALLVKSKEDGKQYVIKEINISKmspkerEESRK----EVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMEKA 488
Cdd:cd08218  84 GDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL-----NSTVELA 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  489 TTkkrtlrkndrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08218 159 RT---------------CIGTPYYLSPEICENKPYNNKSDIWALGCVLYEM 194
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
331-606 4.60e-23

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: 100.09  E-value: 4.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQ-----AIKVTHKATGKVM-VMKELIRCD--EETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKL 401
Cdd:cd05098  15 LVLGKPLGEGCFGQvvlaeAIGLDKDKPNRVTkVAVKMLKSDatEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSMDP-----------FPWQQK-----VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTV 465
Cdd:cd05098  95 YVIVEYASKGNLREYLQARRPpgmeycynpshNPEEQLsskdlVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVM 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  466 VVADFGLSRLIveerKRAPMEKATTKKRTLRKndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQ 542
Cdd:cd05098 175 KIADFGLARDI----HHIDYYKKTTNGRLPVK--------------WMAPEALFDRIYTHQSDVWSFGVLLWEIFtlgGS 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  543 VYADpdcLPRTLDFGLnVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL-EDSFEALSL 606
Cdd:cd05098 237 PYPG---VPVEELFKL-LKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLvEDLDRIVAL 297
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
330-599 4.68e-23

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: 99.57  E-value: 4.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKeLIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd06619   2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVK-VIPLDitVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLkDFLRSMdpfPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrapmek 487
Cdd:cd06619  81 MDGGSL-DVYRKI---PEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV---------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  488 attkkrtlrkNDRKKRYtvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDcLPRTLDFGLNVKLFwEKF 567
Cdd:cd06619 147 ----------NSIAKTY--VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQ-IQKNQGSLMPLQLL-QCI 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5031869  568 VPTDCP--------PAFFPLAAICCRLEPESRPAFSKLED 599
Cdd:cd06619 213 VDEDPPvlpvgqfsEKFVHFITQCMRKQPKERPAPENLMD 252
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
330-540 5.08e-23

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 100.66  E-value: 5.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMK-----ELIRCDEetQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKclkkrEILKMKQ--VQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAP 484
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA-------KKVP 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869   485 mekattkKRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:PTZ00263 170 -------DRT---------FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFI 209
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
337-603 5.08e-23

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: 99.27  E-value: 5.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05092  18 FGKVFLAECHNLLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHGDLNRF 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP---------------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLI----- 476
Cdd:cd05092  98 LRSHGPdakildggegqapgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIystdy 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  477 --VEERKRAPMEkattkkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqVYADP------- 547
Cdd:cd05092 178 yrVGGRTMLPIR-------------------------WMPPESILYRKFTTESDIWSFGVVLWEIF--TYGKQpwyqlsn 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  548 ----DCLPRTLDFglnvklfwEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEA 603
Cdd:cd05092 231 teaiECITQGREL--------ER--PRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
336-599 5.14e-23

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: 99.23  E-value: 5.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGK--VMVMKELIR--CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05064  12 ILGTGRFGELCRGCLKLPSKreLPVAIHTLRagCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrliveerkRAPMEKATT 490
Cdd:cd05064  92 ALDSFLRKHEgQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFR----------RLQEDKSEA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 KKRTLRkndrkKRYTVVgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYAD---PDCLpRTLDFGLNVKlfw 564
Cdd:cd05064 162 IYTTMS-----GKSPVL----WAAPEAIQYHHFSSASDVWSFGIVMWEVMSygeRPYWDmsgQDVI-KAVEDGFRLP--- 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031869  565 ekfVPTDCPPAFFPLAAICCRLEPESRPAFSKLED 599
Cdd:cd05064 229 ---APRNCPNLLHQLMLDCWQKERGERPRFSQIHS 260
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
337-604 5.34e-23

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 98.94  E-value: 5.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQkTFLTEVKVMRSLDHPNVLKFIGVLYKdKKLNLLTEYIEGGTLKDF 416
Cdd:cd14150   8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQ-AFKNEMQVLRKTRHVNILLFMGFMTR-PNFAIITQWCEGSSLYRH 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATtkkrtl 495
Cdd:cd14150  86 LHVTETrFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQVEQPS------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  496 rkndrkkrytvvGNPYWMAPE---MLNGKSYDETVDIFSFGIVLCEIIGQV--YADPDCLPRTLdFGLNVKLFWEKF--V 568
Cdd:cd14150 160 ------------GSILWMAPEvirMQDTNPYSFQSDVYAYGVVLYELMSGTlpYSNINNRDQII-FMVGRGYLSPDLskL 226
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  569 PTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14150 227 SSNCPKAMKRLLIDCLKFKREERPLFPQILVSIELL 262
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
330-536 5.68e-23

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: 99.06  E-value: 5.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKEL-------------------IRCDEETQKtfltEVKVMRSLDHPNVLK 390
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkerekrlekeISRDIRTIR----EAALSSLLNHPHICR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  391 FIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADF 470
Cdd:cd14077  78 LRDFLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDF 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  471 GLSRLIveerkrapmekatTKKRTLRkndrkkryTVVGNPYWMAPEMLNGKSY-DETVDIFSFGIVL 536
Cdd:cd14077 158 GLSNLY-------------DPRRLLR--------TFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVL 203
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
335-536 5.72e-23

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: 98.49  E-value: 5.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQaIKVTHKATGKVMVMKEL----IRcDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14161   9 ETLGKGTYGR-VKKARDSSGRLVAIKSIrkdrIK-DEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekatt 490
Cdd:cd14161  87 GDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLY-------------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  491 kkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSY-DETVDIFSFGIVL 536
Cdd:cd14161 153 -------NQDKFLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLL 192
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
337-539 6.99e-23

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: 98.65  E-value: 6.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVT---HKATGKVMVMKEL----IRCDEETQKtfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd08222   8 LGSGNFGTVYLVSdlkATADEELKVLKEIsvgeLQPDETVDA--NREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSM----DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKlDKTVVVADFGLSRLIVeerkrapm 485
Cdd:cd08222  86 GGDLDDKISEYkksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK-NNVIKVGDFGISRILM-------- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  486 ekATTKKRTlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08222 157 --GTSDLAT----------TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEM 198
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
337-538 7.29e-23

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: 98.50  E-value: 7.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMK-----ELIrcDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd08224   8 IGKGQFSVVYRARCLLDGRLVALKkvqifEMM--DAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TL----KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApmek 487
Cdd:cd08224  86 DLsrliKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAA---- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  488 attkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd08224 162 ----------------HSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYE 196
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
373-602 8.73e-23

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: 98.57  E-value: 8.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  373 FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSM----------DPFPWQQKVRFAKGIASGMAYL 442
Cdd:cd05062  56 FLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLrpemennpvqAPPSLKKMIQMAGEIADGMAYL 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  443 HSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAPEMLNGKS 522
Cdd:cd05062 136 NANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVR------------------WMSPESLKDGV 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  523 YDETVDIFSFGIVLCEIIG------QVYADPDCLPRTLDFGLNVKlfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSK 596
Cdd:cd05062 198 FTTYSDVWSFGVVLWEIATlaeqpyQGMSNEQVLRFVMEGGLLDK-------PDNCPDMLFELMRMCWQYNPKMRPSFLE 270

                ....*.
gi 5031869  597 LEDSFE 602
Cdd:cd05062 271 IISSIK 276
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
336-597 8.97e-23

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: 99.29  E-value: 8.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAI--KVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd08216   5 EIGKCFKGGGVvhLAKHKPTNTLVAVKKinLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRS--MDPFPwQQKVRFA-KGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRapmeka 488
Cdd:cd08216  85 SCRDLLKThfPEGLP-ELAIAFIlRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKR------ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TTKKRTLRKNDRKkrytvvgNPYWMAPEML--NGKSYDETVDIFSFGIVLCEII-GQV-YADPD-----------CLPRT 553
Cdd:cd08216 158 QRVVHDFPKSSEK-------NLPWLSPEVLqqNLLGYNEKSDIYSVGITACELAnGVVpFSDMPatqmllekvrgTTPQL 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  554 LD------FGLNVKLFWEKFVPTDCP-------------PAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd08216 231 LDcstyplEEDSMSQSEDSSTEHPNNrdtrdipyqrtfsEAFHQFVELCLQRDPELRPSASQL 293
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
328-542 9.61e-23

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: 98.23  E-value: 9.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQKT------FLTEVKVMRSLDHPNVLKFIGVL--YKDK 399
Cdd:cd06651   6 PINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQ-VQFDPESPETskevsaLECEIQLLKNLQHERIVQYYGCLrdRAEK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 KLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrlivee 479
Cdd:cd06651  85 TLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-------- 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  480 rkrapmekATTKKRTLRKNDRKKRyTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQ 542
Cdd:cd06651 157 --------ASKRLQTICMSGTGIR-SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE 210
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
334-536 1.11e-22

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: 97.75  E-value: 1.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGqAIKVTHKATGKVMVMKELIrCDEETQKTFLT-----EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14162   5 GKTLGHGSYA-VVKKAYSTKHKCKVAIKIV-SKKKAPEDYLQkflprEIEVIKGLKHPNLICFYEAIETTSRVYIIMELA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkRAPmeKA 488
Cdd:cd14162  83 ENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR-------GVM--KT 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  489 TTKKRTLRKndrkkryTVVGNPYWMAPEMLNGKSYDETV-DIFSFGIVL 536
Cdd:cd14162 154 KDGKPKLSE-------TYCGSYAYASPEILRGIPYDPFLsDIWSMGVVL 195
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
336-536 1.70e-22

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: 97.08  E-value: 1.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATgKVMVMKELI---RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14071   7 TIGKGNFAVVKLARHRIT-KTEVAIKIIdksQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApmekattkk 492
Cdd:cd14071  86 IFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLK--------- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  493 rtlrkndrkkryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14071 157 ------------TWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVL 189
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
335-556 1.86e-22

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: 97.73  E-value: 1.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQaikvthkatgkvmVMKELIRCDEETQKTFLT--------EVKV--MRSLDHPNVLKFIGVLYKDK----K 400
Cdd:cd14056   1 KTIGKGRYGE-------------VWLGKYRGEKVAVKIFSSrdedswfrETEIyqTVMLRHENILGFIAADIKSTgswtQ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  401 LNLLTEYIEGGTLKDFLRS--MDPfpwQQKVRFAKGIASGMAYLHSM--------CIIHRDLNSHNCLIKLDKTVVVADF 470
Cdd:cd14056  68 LWLITEYHEHGSLYDYLQRntLDT---EEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  471 GLSrlIVEERKRAPMEKATTKKrtlrkndrkkrytvVGNPYWMAPEML----NGKSYD--ETVDIFSFGIVLCEIIGQVY 544
Cdd:cd14056 145 GLA--VRYDSDTNTIDIPPNPR--------------VGTKRYMAPEVLddsiNPKSFEsfKMADIYSFGLVLWEIARRCE 208
                       250
                ....*....|..
gi 5031869  545 ADPDCLPRTLDF 556
Cdd:cd14056 209 IGGIAEEYQLPY 220
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
337-540 2.71e-22

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: 97.51  E-value: 2.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEETQktFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05612   9 IGTGTFGRVHLVRDRISEhyyalKVMAIPEVIRLKQEQH--VHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekattk 491
Cdd:cd05612  87 ELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRD------------- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  492 kRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05612 154 -RT---------WTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEML 192
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
331-615 3.61e-22

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: 98.17  E-value: 3.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQ-----AIKVTHKATGKVMVMKELIRCDEETQKTF---LTEVKVMRSL-DHPNVLKFIGVLYKDKKL 401
Cdd:cd05100  14 LTLGKPLGEGCFGQvvmaeAIGIDKDKPNKPVTVAVKMLKDDATDKDLsdlVSEMEMMKMIgKHKNIINLLGACTQDGPL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSMDP-----------FPWQQK-----VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTV 465
Cdd:cd05100  94 YVLVEYASKGNLREYLRARRPpgmdysfdtckLPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  466 VVADFGLSRliveERKRAPMEKATTKKRTLRKndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYA 545
Cdd:cd05100 174 KIADFGLAR----DVHNIDYYKKTTNGRLPVK--------------WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGS 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  546 DPDCLPRTLDFGLnVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL-EDSFEALSL-----YLgELGIPL 615
Cdd:cd05100 236 PYPGIPVEELFKL-LKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLvEDLDRVLTVtstdeYL-DLSVPF 309
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
334-540 4.89e-22

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: 96.87  E-value: 4.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQK-----TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd07841   5 GKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdginfTALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EG---GTLKDflRSMDPFPWQQKVrFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrAPM 485
Cdd:cd07841  85 ETdleKVIKD--KSIVLTPADIKS-YMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFG-----SPN 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  486 EKATTKkrtlrkndrkkrytVVgNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07841 157 RKMTHQ--------------VV-TRWYRAPELLFGaRHYGVGVDMWSVGCIFAELL 197
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
337-539 5.63e-22

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: 97.03  E-value: 5.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTF---LTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgTL 413
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWqdiIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLG-SA 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrAPMEkattkk 492
Cdd:cd06633 108 SDLLEvHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA------SPAN------ 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrkndrkkryTVVGNPYWMAPEM---LNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06633 176 ------------SFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIEL 213
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
383-601 6.98e-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: 95.50  E-value: 6.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  383 LDHPNVLKFIGVLYKDK------KLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN 456
Cdd:cd14012  55 LRHPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGN 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  457 CLI---KLDKTVVVADFGLSrliveerkrapmekattkkRTLRKNDRKKRYTVVGNPYWMAPEM-LNGKSYDETVDIFSF 532
Cdd:cd14012 135 VLLdrdAGTGIVKLTDYSLG-------------------KTLLDMCSRGSLDEFKQTYWLPPELaQGSKSPTRKTDVWDL 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  533 GIVLCEIIgqvyadpdclprtldFGLNVklfWEKF-------VPTDCPPAFFPLAAICCRLEPESRP-AFSKLEDSF 601
Cdd:cd14012 196 GLLFLQML---------------FGLDV---LEKYtspnpvlVSLDLSASLQDFLSKCLSLDPKKRPtALELLPHEF 254
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
332-536 7.52e-22

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: 95.48  E-value: 7.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEvLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14075   6 IRGE-LGSGNFSQVKLGIHQLTKEKVAIKILdkTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYAS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQ-KVRFAKgIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmeka 488
Cdd:cd14075  85 GGELYTKISTEGKLSESEaKPLFAQ-IVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFS--------------- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  489 ttkkrTLRKNDRKKRyTVVGNPYWMAPEMLNGKSY-DETVDIFSFGIVL 536
Cdd:cd14075 149 -----THAKRGETLN-TFCGSPPYAAPELFKDEHYiGIYVDIWALGVLL 191
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
335-540 7.91e-22

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: 95.82  E-value: 7.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGg 411
Cdd:cd07835   5 EKIGEGTYGVVYKARDKLTGEIVALKK-IRLETEDEgvpSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLDL- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSM--DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMEKAT 489
Cdd:cd07835  83 DLKKYMDSSplTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF-----GVPVRTYT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 TKKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07835 158 HEVVTL---------------WYRAPEILLGsKHYSTPVDIWSVGCIFAEMV 194
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
337-540 8.39e-22

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: 95.64  E-value: 8.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVThKATGKVMVMKELIRcdEETQKT---FLTEVKVMRSLDHPNVLKFIGvLYKDKKLNLLT-EYIEGGT 412
Cdd:cd14664   1 IGRGGAGTVYKGV-MPNGTLVAVKRLKG--EGTQGGdhgFQAEIQTLGMIRHRNIVRLRG-YCSNPTTNLLVyEYMPNGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDP----FPWQQKVRFAKGIASGMAYLHSMC---IIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapm 485
Cdd:cd14664  77 LGELLHSRPEsqppLDWETRQRIALGSARGLAYLHHDCsplIIHRDVKSNNILLDEEFEAHVADFGLAKLMDD------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  486 ekattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14664 150 ------------KDSHVMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELI 192
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
335-539 8.67e-22

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: 95.97  E-value: 8.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKatGKVMVMKELircDEETQKTFLTEVKVMRS--LDHPNVLKFIGVLYKD----KKLNLLTEYI 408
Cdd:cd13998   1 EVIGKGRFGEVWKASLK--NEPVAVKIF---SSRDKQSWFREKEIYRTpmLKHENILQFIAADERDtalrTELWLVTAFH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRsMDPFPWQQKVRFAKGIASGMAYLHS---------MCIIHRDLNSHNCLIKLDKTVVVADFGLS-RLive 478
Cdd:cd13998  76 PNGSL*DYLS-LHTIDWVSLCRLALSVARGLAHLHSeipgctqgkPAIAHRDLKSKNILVKNDGTCCIADFGLAvRL--- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  479 ERKRAPMEKATTKKrtlrkndrkkrytvVGNPYWMAPEMLNG-------KSYDEtVDIFSFGIVLCEI 539
Cdd:cd13998 152 SPSTGEEDNANNGQ--------------VGTKRYMAPEVLEGainlrdfESFKR-VDIYAMGLVLWEM 204
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
373-539 8.84e-22

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: 96.28  E-value: 8.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  373 FLTEVKVMR--SLDHPNVLKFIGVlykDKKLN--------LLTEYIEGGTLKDFLR--SMDpfpWQQKVRFAKGIASGMA 440
Cdd:cd14054  34 FQNEKDIYElpLMEHSNILRFIGA---DERPTadgrmeylLVLEYAPKGSLCSYLRenTLD---WMSSCRMALSLTRGLA 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  441 YLHSM---------CIIHRDLNSHNCLIKLDKTVVVADFGLSrLIVeerkrapmeKATTKKRTLRKNDRKKRYTVVGNPY 511
Cdd:cd14054 108 YLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLA-MVL---------RGSSLVRGRPGAAENASISEVGTLR 177
                       170       180       190
                ....*....|....*....|....*....|....*
gi 5031869  512 WMAPEMLNG-------KSYDETVDIFSFGIVLCEI 539
Cdd:cd14054 178 YMAPEVLEGavnlrdcESALKQVDVYALGLVLWEI 212
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
336-540 1.13e-21

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: 94.80  E-value: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd08221   7 VLGRGAFGEAVLYRKTEDNSLVVWKEvnLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNclIKLDKT--VVVADFGLSRLIVEERKRAPmekat 489
Cdd:cd08221  87 HDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLN--IFLTKAdlVKLGDFGISKVLDSESSMAE----- 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  490 tkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd08221 160 ---------------SIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELL 195
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
345-543 1.21e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 99.10  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   345 AIKVTHKatgkvmvmkELIRcDEETQKTFLTEVKVMRSLDHPNVlkfIGVlY---KDKKLN-LLTEYIEGGTLKDFLRSM 420
Cdd:NF033483  36 AVKVLRP---------DLAR-DPEFVARFRREAQSAASLSHPNI---VSV-YdvgEDGGIPyIVMEYVDGRTLKDYIREH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   421 DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekaTTKKRTlrkNdr 500
Cdd:NF033483 102 GPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSS----------TTMTQT---N-- 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 5031869   501 kkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV 543
Cdd:NF033483 167 ----SVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLtGRP 206
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
361-569 1.35e-21

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: 94.68  E-value: 1.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  361 ELIRCDEETQKT-------FLTEVKVMRSLDHPNVLKFI----GVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKV 429
Cdd:cd14033  28 EVAWCELQTRKLskgerqrFSEEVEMLKGLQHPNIVRFYdswkSTVRGHKCIILVTELMTSGTLKTYLKRFREMKLKLLQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  430 RFAKGIASGMAYLHSMC--IIHRDLNSHNCLIK-LDKTVVVADFGLSRLiveerKRAPMEKattkkrtlrkndrkkryTV 506
Cdd:cd14033 108 RWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATL-----KRASFAK-----------------SV 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  507 VGNPYWMAPEMLNGKsYDETVDIFSFGIVLCEIIGQVYADPDC-----LPRTLDFGLNVKLFWEKFVP 569
Cdd:cd14033 166 IGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSECqnaaqIYRKVTSGIKPDSFYKVKVP 232
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
336-539 1.44e-21

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: 95.55  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCD----EETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14209   8 TLGTGSFGRVMLVRHKETGNYYAMKILDKQKvvklKQVEHT-LNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEYVPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattK 491
Cdd:cd14209  87 EMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV--------------K 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  492 KRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd14209 153 GRT---------WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 191
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
337-538 1.51e-21

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 97.02  E-value: 1.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEETQktFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05600  19 VGQGGYGSVFLARKKDTGeicalKIMKKKVLFKLNEVNH--VLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQkVRF--AKGIASGMAyLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERK----RAPM 485
Cdd:cd05600  97 DFRTLLNNSGILSEEH-ARFyiAEMFAAISS-LHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKiesmKIRL 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  486 EKAT-------TKK------RTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd05600 175 EEVKntaflelTAKerrniyRAMRKEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFE 240
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
337-601 1.54e-21

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: 95.03  E-value: 1.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTF-LTEVKVMRSLD---HPNVLKFIGVLYKDK-----KLNLLTE 406
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKVrVPLSEEGIPLStIREIALLKQLEsfeHPNVVRLLDVCHGPRtdrelKLTLVFE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGgTLKDFLRSMDPF---PWQQKvRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRA 483
Cdd:cd07838  87 HVDQ-DLATYLDKCPKPglpPETIK-DLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSFEMALT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  484 PmekattkkrtlrkndrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI-----IGQVYADPDCLPRTLDF-G 557
Cdd:cd07838 165 S---------------------VVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELfnrrpLFRGSSEADQLGKIFDViG 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  558 L--------NVKLFWEKFVP------TDCPPAFFPLAA----ICCRLEPESRP-AFSKLEDSF 601
Cdd:cd07838 224 LpseeewprNSALPRSSFPSytprpfKSFVPEIDEEGLdllkKMLTFNPHKRIsAFEALQHPY 286
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
294-538 1.74e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 96.43  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   294 PGPSSPKEPllfsrdiSRSESLRCSSSYSQQIFrpCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTF 373
Cdd:PLN00034  48 PPPSSSSSS-------SSSSSASGSAPSAAKSL--SELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   374 LT-EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFpwqqKVRFAKGIASGMAYLHSMCIIHRDL 452
Cdd:PLN00034 119 ICrEIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQF----LADVARQILSGIAYLHRRHIVHRDI 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   453 NSHNCLIKLDKTVVVADFGLSRLIVEErkrapMEKATTKkrtlrkndrkkrytvVGNPYWMAPEM----LNGKSYDETV- 527
Cdd:PLN00034 195 KPSNLLINSAKNVKIADFGVSRILAQT-----MDPCNSS---------------VGTIAYMSPERintdLNHGAYDGYAg 254
                        250
                 ....*....|.
gi 5031869   528 DIFSFGIVLCE 538
Cdd:PLN00034 255 DIWSLGVSILE 265
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
335-540 1.94e-21

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: 95.84  E-value: 1.94e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKilrkEVIIAKDEVAHT-VTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapmeKAT 489
Cdd:cd05595  80 GELFFHLSRERVFT-EDRARFyGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCK------------EGI 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  490 TKKRTLRkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05595 147 TDGATMK--------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 189
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
335-539 2.02e-21

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: 94.91  E-value: 2.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIR----CDEETQktfLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd07830   5 KQLGDGTFGSVYLARNKETGELVAIKKMKKkfysWEECMN---LREVKSLRKLnEHPNIVKLKEVFRENDELYFVFEYME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GgTLKDFLRSMD--PFP--------WQqkvrfakgIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEE 479
Cdd:cd07830  82 G-NLYQLMKDRKgkPFSesvirsiiYQ--------ILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAR---EI 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  480 RKRAPmekattkkrtlrkndrkkrYTV-VGNPYWMAPEM-LNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd07830 150 RSRPP-------------------YTDyVSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAEL 192
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
330-597 2.05e-21

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: 95.06  E-value: 2.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNL 403
Cdd:cd05088   8 DIKFQDVIGEGNFGQVLKARIKKDGlrmdaAIKRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLR-----SMDP-----------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV 467
Cdd:cd05088  86 AIEYAPHGNLLDFLRksrvlETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  468 ADFGLSRliveerkrapMEKATTKKRTLRKNDRkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVY 544
Cdd:cd05088 166 ADFGLSR----------GQEVYVKKTMGRLPVR-----------WMAIESLNYSVYTTNSDVWSYGVLLWEIVslgGTPY 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  545 ADPDCLPRTLDFGLNVKLfwEKfvPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05088 225 CGMTCAELYEKLPQGYRL--EK--PLNCDDEVYDLMRQCWREKPYERPSFAQI 273
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
334-536 2.06e-21

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 94.32  E-value: 2.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKEL------IRCDEETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd14069   6 VQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkrapGDCPENIKK----EVCIQKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDflrSMDP---FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLsrliveerkrAP 484
Cdd:cd14069  82 ASGGELFD---KIEPdvgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGL----------AT 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  485 MEKATTKKRTLrkNDRkkrytvVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14069 149 VFRYKGKERLL--NKM------CGTLPYVAPELLAKKKYRaEPVDVWSCGIVL 193
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
334-536 2.21e-21

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: 94.01  E-value: 2.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRcdEETQKTFLT-----EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14663   5 GRTLGEGTFAKVKFARNTKTGESVAIKIIDK--EQVAREGMVeqikrEIAIMKLLRHPNIVELHEVMATKTKIFFVMELV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiVEERKRAPMeka 488
Cdd:cd14663  83 TGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAL-SEQFRQDGL--- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  489 ttkkrtlrkndrkkRYTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14663 159 --------------LHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVIL 193
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
336-535 2.22e-21

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: 94.14  E-value: 2.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd14087   8 LIGRGSFSRVVRVEHRVTRQPYAIK-MIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELFD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSrlivEERKRAPMEKATtkk 492
Cdd:cd14087  87 RIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLA----STRKKGPNCLMK--- 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 5031869  493 rtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14087 160 ------------TTCGTPEYIAPEILLRKPYTQSVDMWAVGVI 190
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
337-539 2.23e-21

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: 93.83  E-value: 2.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQK-TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLkd 415
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAK-FIKCRKAKDReDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMD-PFPWQQK--VRFAKGIASGMAYLHSMCIIHRDLNSHN--CLIKLDKTVVVADFGLSRliveerkrapmekatt 490
Cdd:cd14103  78 FERVVDdDFELTERdcILFMRQICEGVQYMHKQGILHLDLKPENilCVSRTGNQIKIIDFGLAR---------------- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  491 kkrtlRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGiVLCEI 539
Cdd:cd14103 142 -----KYDPDKKLKVLFGTPEFVAPEVVNYEPISYATDMWSVG-VICYV 184
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
335-540 2.55e-21

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: 94.56  E-value: 2.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYKD------KKLNLLTEY 407
Cdd:cd14048  12 QCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREkVLREVRALAKLDHPGIVRYFNAWLERppegwqEKMDEVYLY 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IE-----GGTLKDFLR---SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrlivee 479
Cdd:cd14048  92 IQmqlcrKENLKDWMNrrcTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV------ 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  480 rkrAPMEKATTKKRTLRKNDRKKRYT-VVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14048 166 ---TAMDQGEPEQTVLTPMPAYAKHTgQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
335-535 3.98e-21

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: 93.45  E-value: 3.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLk 414
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGEL- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 dFLRSMD---PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN--CLIKLDKTVVVADFGLSRliveerkrapmekat 489
Cdd:cd14190  89 -FERIVDedyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENilCVNRTGHQVKIIDFGLAR--------------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  490 tkkrtlRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14190 153 ------RYNPREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVI 192
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
335-540 4.49e-21

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: 94.65  E-value: 4.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKfyaVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrapmEKAT 489
Cdd:cd05603  81 GELFFHLQRERCFL-EPRARFyAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEP------EETT 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  490 TkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05603 154 S--------------TFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEML 190
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
336-540 4.99e-21

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: 93.09  E-value: 4.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIR--CDE-ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd05578   7 VIGKGSFGKVCIVQKKDTKKMFAMKYMNKqkCIEkDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKdflrsmdpFPWQQKVRFAKG--------IASGMAYLHSMCIIHRDLNSHNCLikLDKT--VVVADFGLSRlIVEERkr 482
Cdd:cd05578  87 LR--------YHLQQKVKFSEEtvkfyiceIVLALDYLHSKNIIHRDIKPDNIL--LDEQghVHITDFNIAT-KLTDG-- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  483 apmEKATtkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05578 154 ---TLAT---------------STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEML 193
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
335-592 6.58e-21

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: 93.34  E-value: 6.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKelircdeetqKTFLT------EVKVMRSLDHPNVLKFIGVLY------KDKKLN 402
Cdd:cd14137  10 KVIGSGSFGVVYQAKLLETGEVVAIK----------KVLQDkryknrELQIMRRLKHPNIVKLKYFFYssgekkDEVYLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 LLTEYIEGgTL----KDFLRSMDPFP--------WQqkvrfakgIASGMAYLHSMCIIHRDLNSHNCLIKLDK-TVVVAD 469
Cdd:cd14137  80 LVMEYMPE-TLyrviRHYSKNKQTIPiiyvklysYQ--------LFRGLAYLHSLGICHRDIKPQNLLVDPETgVLKLCD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  470 FGLSRLIVeerkraPMEKATTkkrtlrkndrkkrYtvVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCE-IIGQV---- 543
Cdd:cd14137 151 FGSAKRLV------PGEPNVS-------------Y--ICSRYYRAPElIFGATDYTTAIDIWSAGCVLAElLLGQPlfpg 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  544 -----------------------YADPDCLPRTLDfglNVK-LFWEKFVPTDCPPAFFPLAAICCRLEPESRP 592
Cdd:cd14137 210 essvdqlveiikvlgtptreqikAMNPNYTEFKFP---QIKpHPWEKVFPKRTPPDAIDLLSKILVYNPSKRL 279
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
331-610 7.40e-21

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: 93.93  E-value: 7.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKV------THKATGKVMVMKELIRcDEETQKTF---LTEVKVMRSL-DHPNVLKFIGVLYKDKK 400
Cdd:cd05101  26 LTLGKPLGEGCFGQVVMAeavgidKDKPKEAVTVAVKMLK-DDATEKDLsdlVSEMEMMKMIgKHKNIINLLGACTQDGP 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  401 LNLLTEYIEGGTLKDFLRSM----------------DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKT 464
Cdd:cd05101 105 LYVIVEYASKGNLREYLRARrppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  465 VVVADFGLSRLIveerKRAPMEKATTKKRTLRKndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII---G 541
Cdd:cd05101 185 MKIADFGLARDI----NNIDYYKKTTNGRLPVK--------------WMAPEALFDRVYTHQSDVWSFGVLMWEIFtlgG 246
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  542 QVYADpdcLPRTLDFGLnVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL-EDSFEALSLYLGE 610
Cdd:cd05101 247 SPYPG---IPVEELFKL-LKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLvEDLDRILTLTTNE 312
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
334-536 9.75e-21

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: 92.25  E-value: 9.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATG-KVMVMKELI---RCDEETQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14080   5 GKTIGEGSYSKVKLAEYTKSGlKEKVACKIIdkkKAPKDFLEKFLPrELEILRKLRHPNIIQVYSIFERGSKVFIFMEYA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmeka 488
Cdd:cd14080  85 EHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPD---------- 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  489 tTKKRTLRKndrkkryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14080 155 -DDGDVLSK-------TFCGSAAYAAPEILQGIPYDpKKYDIWSLGVIL 195
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
334-535 9.97e-21

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: 92.02  E-value: 9.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIR---CDEEtqKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14184   6 GKVIGDGNFAVVKECVERSTGKEFALKIIDKakcCGKE--HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI----KLDKTVVVADFGLSRLIveerkRAPMe 486
Cdd:cd14184  84 GDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV-----EGPL- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  487 kattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14184 158 -----------------YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVI 189
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
337-540 1.26e-20

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: 92.79  E-value: 1.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LrSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrAPmekattkkrtlr 496
Cdd:cd06658 110 V-THTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKE---VP------------ 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031869  497 kndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06658 174 -----KRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMI 212
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
337-540 1.32e-20

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: 92.63  E-value: 1.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN------LLTEY 407
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKK-IRMENEKEgfpITAIREIKLLQKLDHPNVVRLKEIVTSKGSAKykgsiyMVFEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGgTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRapme 486
Cdd:cd07840  86 MDH-DLTGLLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNA---- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  487 KATTKKRTLrkndrkkrytvvgnpyWM-APEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07840 161 DYTNRVITL----------------WYrPPELLLGaTRYGPEVDMWSVGCILAELF 200
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
336-536 1.34e-20

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: 92.01  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIG--VLYKD--KKLNLLTEYIeG 410
Cdd:cd13985   7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDsaILSSEgrKEVLLLMEYC-P 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSM--DPFPWQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIKLDKTVVVADFG---LSRLIVEERKRA 483
Cdd:cd13985  86 GSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsatTEHYPLERAEEV 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  484 PMEKATTKKRTlrkndrkkrytvvgNPYWMAPEMLN---GKSYDETVDIFSFGIVL 536
Cdd:cd13985 166 NIIEEEIQKNT--------------TPMYRAPEMIDlysKKPIGEKADIWALGCLL 207
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
330-540 1.49e-20

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: 93.61  E-value: 1.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd05593  16 DFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPM 485
Cdd:cd05593  95 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-------KEGIT 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  486 EKATTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05593 168 DAATMK-------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 209
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
337-535 1.56e-20

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: 91.18  E-value: 1.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAK-FIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI--KLDKTVVVADFGLSRLIveerkrapmekattkkrt 494
Cdd:cd14006  80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLadRPSPQIKIIDFGLARKL------------------ 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031869  495 lrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14006 142 ---NPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVL 179
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
335-536 1.63e-20

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: 91.68  E-value: 1.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELircDEETQKTFL----TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14078   9 ETIGSGGFAKVKLATHILTGEKVAIKIM---DKKALGDDLprvkTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekATT 490
Cdd:cd14078  86 GELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLC--------------AKP 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  491 KkrtlrKNDRKKRYTVVGNPYWMAPEMLNGKSY-DETVDIFSFGIVL 536
Cdd:cd14078 152 K-----GGMDHHLETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLL 193
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
334-536 1.73e-20

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: 91.56  E-value: 1.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATG-KVMV-------MKELiRCDEETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd14079   7 GKTLGVGSFGKVKLAEHELTGhKVAVkilnrqkIKSL-DMEEKIRR----EIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapm 485
Cdd:cd14079  82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNI---------- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  486 ekaTTKKRTLRkndrkkryTVVGNPYWMAPEMLNGKSY-DETVDIFSFGIVL 536
Cdd:cd14079 152 ---MRDGEFLK--------TSCGSPNYAAPEVISGKLYaGPEVDVWSCGVIL 192
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
337-540 1.74e-20

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: 92.39  E-value: 1.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LrSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRapmekattkkrtlr 496
Cdd:cd06657 108 V-THTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR-------------- 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031869  497 kndrkkRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd06657 173 ------RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV 210
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
327-540 1.84e-20

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: 93.16  E-value: 1.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  327 RPCDLIHGEVLGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEEtqKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKK 400
Cdd:cd05602   5 KPSDFHFLKVIGKGSFGKVLLARHKSDEkfyavKVLQKKAILKKKEE--KHIMSERNVLlKNVKHPFLVGLHFSFQTTDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  401 LNLLTEYIEGGTLKDFLRSMDPFpWQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEe 479
Cdd:cd05602  83 LYFVLDYINGGELFYHLQRERCF-LEPRARFyAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE- 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  480 rkrapmEKATTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05602 161 ------PNGTTS-------------TFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEML 202
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
335-539 2.39e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 91.17  E-value: 2.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL------IRCDEETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd08225   6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIdltkmpVKEKEASKK----EVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLkdflrsMDPFPWQQKVRFAKG--------IASGMAYLHSMCIIHRDLNSHNclIKLDKTVVVA---DFGLSRLIV 477
Cdd:cd08225  82 DGGDL------MKRINRQRGVLFSEDqilswfvqISLGLKHIHDRKILHRDIKSQN--IFLSKNGMVAklgDFGIARQLN 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  478 EErkrapMEKAttkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08225 154 DS-----MELA---------------YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYEL 195
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
335-543 2.63e-20

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: 91.33  E-value: 2.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHK-ATGKVMVMKELIR--CDEETQKTFLTEVKVMRSLD---HPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14052   6 ELIGSGEFSQVYKVSERvPTGKVYAVKKLKPnyAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELC 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFL------RSMDPFP-WQQKVRfakgIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerK 481
Cdd:cd14052  86 ENGSLDVFLselgllGRLDEFRvWKILVE----LSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA-------T 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  482 RAPMEKATTkkrtlRKNDRKkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQV 543
Cdd:cd14052 155 VWPLIRGIE-----REGDRE----------YIAPEILSEHMYDKPADIFSLGLILLEAAANV 201
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
335-540 2.66e-20

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: 92.33  E-value: 2.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05604   2 KVIGKGSFGKVLLAKRKRDGKyyaVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapmEKATT 490
Cdd:cd05604  82 GELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCK-----------EGISN 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 KKRTLrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05604 151 SDTTT---------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEML 191
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
335-540 2.89e-20

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: 92.03  E-value: 2.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPnvlkFIGVL-Y----KDKkLNLLT 405
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKilkkEVIIAKDEVAHT-LTENRVLQNTRHP----FLTSLkYsfqtNDR-LCFVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEERKRAp 484
Cdd:cd05571  75 EYVNGGELFFHLSRERVFS-EDRTRFyGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCK---EEISYG- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  485 mekATTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05571 150 ---ATTK-------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 189
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
335-539 3.05e-20

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: 91.02  E-value: 3.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATG-KVMVMKELI-------RCDEETQKTF---LTEVKVMRS-LDHPNVLKFIGVLYKDKKLN 402
Cdd:cd08528   6 ELLGSGAFGCVYKVRKKSNGqTLLALKEINmtnpafgRTEQERDKSVgdiISEVNIIKEqLRHPNIVRYYKTFLENDRLY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 LLTEYIEGGTLKDFLRSMDP----FPWQQKVRFAKGIASGMAYLH-SMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliv 477
Cdd:cd08528  86 IVMELIEGAPLGEHFSSLKEknehFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLAK--- 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  478 eeRKRAPMEKATtkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08528 163 --QKGPESSKMT---------------SVVGTILYSCPEIVQNEPYGEKADIWALGCILYQM 207
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
337-539 3.39e-20

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: 90.59  E-value: 3.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI---RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgTL 413
Cdd:cd06607   9 IGHGSFGAVYYARNKRTSEVVAIKKMSysgKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCLG-SA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLR-SMDPFpwqQKVRFA---KGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrAPMEkat 489
Cdd:cd06607  88 SDIVEvHKKPL---QEVEIAaicHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLV------CPAN--- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  490 tkkrtlrkndrkkryTVVGNPYWMAPE----MLNGKsYDETVDIFSFGIVLCEI 539
Cdd:cd06607 156 ---------------SFVGTPYWMAPEvilaMDEGQ-YDGKVDVWSLGITCIEL 193
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
335-537 3.59e-20

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: 90.86  E-value: 3.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14167   9 EVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIeNEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCL---IKLDKTVVVADFGLSRLiveERKRAPMEkatt 490
Cdd:cd14167  89 FDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKI---EGSGSVMS---- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  491 kkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFG----IVLC 537
Cdd:cd14167 162 --------------TACGTPGYVAPEVLAQKPYSKAVDCWSIGviayILLC 198
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
339-540 3.79e-20

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: 90.62  E-value: 3.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  339 KGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTfLTEVKVMRSLDH-----PNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05611   6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQ-VTNVKAERAIMMiqgesPYVAKLYYSFQSKDYLYLVMEYLNGGDC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkkr 493
Cdd:cd05611  85 ASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRH------------ 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  494 tlrkndrKKRYtvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05611 153 -------NKKF--VGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFL 190
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
328-539 3.92e-20

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: 90.31  E-value: 3.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKelIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd05114   3 PSELTFMKELGSGLFGVVRLGKWRAQYKVAIKA--IREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRsmdpfpwQQKVRFAK--------GIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEE 479
Cdd:cd05114  81 MENGCLLNYLR-------QRRGKLSRdmllsmcqDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDD 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  480 RKRAPMEKATTKKrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05114 154 QYTSSSGAKFPVK-------------------WSPPEVFNYSKFSSKSDVWSFGVLMWEV 194
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
337-598 4.38e-20

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: 90.41  E-value: 4.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIK--VTHKATGKVMVMKELIR--CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGT 412
Cdd:cd05116   3 LGSGNFGTVKKgyYQMKKVVKTVAVKILKNeaNDPALKDELLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMAELGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRapMEKATTKK 492
Cdd:cd05116  82 LNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENY--YKAQTHGK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 RTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVyadpdclPRTLDFGLNVKLFWEK---- 566
Cdd:cd05116 160 WPVK---------------WYAPECMNYYKFSSKSDVWSFGVLMWEAFsyGQK-------PYKGMKGNEVTQMIEKgerm 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031869  567 FVPTDCPPAFFPLAAICCRLEPESRPAFSKLE 598
Cdd:cd05116 218 ECPAGCPPEMYDLMKLCWTYDVDERPGFAAVE 249
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
336-536 4.87e-20

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: 90.53  E-value: 4.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL---------IRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd14084  13 TLGSGACGEVKLAYDKSTCKKVAIKIInkrkftigsRREINKPRNI-ETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN---------CLIKldktvvVADFGLSRLIV 477
Cdd:cd14084  92 LMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENvllssqeeeCLIK------ITDFGLSKILG 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  478 EerkRAPMEkattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKS---YDETVDIFSFGIVL 536
Cdd:cd14084 166 E---TSLMK------------------TLCGTPTYLAPEVLRSFGtegYTRAVDCWSLGVIL 206
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
337-541 5.86e-20

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 89.75  E-value: 5.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEETQKtFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd13997   8 IGSGSFSEVFKVRSKVDGCLYAVKKSkkpFRGPKERAR-ALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELCENGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDP---FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL-----SRLIVEErkrap 484
Cdd:cd13997  87 LQDALEELSPiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLatrleTSGDVEE----- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  485 mekattkkrtlrkndrkkrytvvGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEIIG 541
Cdd:cd13997 162 -----------------------GDSRYLAPELLNEnYTHLPKADIFSLGVTVYEAAT 196
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
336-540 5.89e-20

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: 91.22  E-value: 5.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEEtQKTFLTEVKV-MRSLDHPnvlkF-IGVLY----KDKkLNLLT 405
Cdd:cd05575   2 VIGKGSFGKVLLARHKAEGKLYAVKvlqkKAILKRNE-VKHIMAERNVlLKNVKHP----FlVGLHYsfqtKDK-LYFVL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrap 484
Cdd:cd05575  76 DYVNGGELFFHLQRERHFP-EPRARFyAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSD--- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  485 mekaTTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05575 152 ----TTS-------------TFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEML 190
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
334-536 6.07e-20

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: 89.92  E-value: 6.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTE--VKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14097   6 GRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEreVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIK------LDKTVV-VADFGLSrlIVEERKRAP 484
Cdd:cd14097  86 ELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKssiidnNDKLNIkVTDFGLS--VQKYGLGED 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  485 MEKATtkkrtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14097 164 MLQET-----------------CGTPIYMAPEVISAHGYSQQCDIWSIGVIM 198
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
335-540 6.40e-20

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: 91.52  E-value: 6.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAI---KVTHKATGKVMVMKELIRC----DEETQKTFLTEVKVmrsLDHPNVLKFIGVLY----KDKKLNL 403
Cdd:cd05614   6 KVLGTGAYGKVFlvrKVSGHDANKLYAMKVLRKAalvqKAKTVEHTRTERNV---LEHVRQSPFLVTLHyafqTDAKLHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPwQQKVRFAKG-IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkr 482
Cdd:cd05614  83 ILDYVSGGELFTHLYQRDHFS-EDEVRFYSGeIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTE--- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  483 apmekattkkrtlrknDRKKRYTVVGNPYWMAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd05614 159 ----------------EKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELL 201
LIM2_LIMK1 cd09464
The second LIM domain of LIMK1 (LIM domain Kinase 1); The second LIM domain of LIMK1 (LIM ...
72-125 6.91e-20

The second LIM domain of LIMK1 (LIM domain Kinase 1); The second LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188848  Cd Length: 55  Bit Score: 83.38  E-value: 6.91e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869   72 CHGCS-LLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCH 125
Cdd:cd09464   1 CHGCSeTITTGLVMVAGEQKYHPECFSCLRCGAFIGDGDTYALVEHSKLYCGHCY 55
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
322-542 7.72e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 90.98  E-value: 7.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   322 SQQIFRPCdlihGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCD------EETQK--------TFLTEVKVMRSLDHPN 387
Cdd:PTZ00024   6 ISERYIQK----GAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtKDRQLvgmcgihfTTLRELKIMNEIKHEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   388 VLKFIGVLYKDKKLNLLTEYIEGgTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVV 467
Cdd:PTZ00024  82 IMGLVDVYVEGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869   468 ADFGLSRliveeRKRAPMEKATTKKRTLRKNDRKKRYTVVgNPYWMAPEMLNGKS-YDETVDIFSFGIVLCEIIGQ 542
Cdd:PTZ00024 161 ADFGLAR-----RYGYPPYSDTLSKDETMQRREEMTSKVV-TLWYRAPELLMGAEkYHFAVDMWSVGCIFAELLTG 230
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
330-563 7.86e-20

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: 91.14  E-value: 7.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKEL----IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd05619   6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALkkdvVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapm 485
Cdd:cd05619  86 EYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK----------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  486 EKATTKKRTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQ--------------VYADPDCL 550
Cdd:cd05619 155 ENMLGDAKT---------STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEmLIGQspfhgqdeeelfqsIRMDNPFY 225
                       250
                ....*....|....*.
gi 5031869  551 PRTLDF---GLNVKLF 563
Cdd:cd05619 226 PRWLEKeakDILVKLF 241
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
335-540 1.06e-19

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: 89.85  E-value: 1.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEggtl 413
Cdd:cd07836   6 EKLGEGTYATVYKGRNRTTGEIVALKEIhLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD---- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMD------PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMEK 487
Cdd:cd07836  82 KDLKKYMDthgvrgALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF-----GIPVNT 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  488 ATTKKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07836 157 FSNEVVTL---------------WYRAPDVLLGsRTYSTSIDIWSVGCIMAEMI 195
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
336-539 1.07e-19

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: 89.26  E-value: 1.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ--KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd08219   7 VVGEGSFGRALLVQHVNSDQKYAMKE-IRLPKSSSavEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 --KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkraPMEKATTk 491
Cdd:cd08219  86 mqKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTS-----PGAYACT- 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  492 krtlrkndrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08219 160 --------------YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYEL 193
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
337-617 1.11e-19

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 90.50  E-value: 1.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd06650  13 LGAGNGGVVFKVSHKPSGLVMARKLIhLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQ 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVRFAKGIASGMAYLHSMC-IIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRapmekattkkrt 494
Cdd:cd06650  93 VLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN------------ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI-IGQV-YADPDCLPRTLDFGLNVklfweKFVPTDC 572
Cdd:cd06650 161 ----------SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMaVGRYpIPPPDAKELELMFGCQV-----EGDAAET 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031869  573 PPAFFPLAAICCRLEPESRPAFSkledSFEALSLYLGELGIPLPA 617
Cdd:cd06650 226 PPRPRTPGRPLSSYGMDSRPPMA----IFELLDYIVNEPPPKLPS 266
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
335-537 1.13e-19

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: 88.97  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfltEVKVMRSLDHPNVLKFIGVlYKDK-KLNLLTEYIE 409
Cdd:cd14083   9 EVLGTGAFSEVVLAEDKATGKLVAIKcidkKALKGKEDSLEN---EIAVLRKIKHPNIVQLLDI-YESKsHLYLVMELVT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSRLIVEERkrapME 486
Cdd:cd14083  85 GGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLSKMEDSGV----MS 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  487 kattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFG----IVLC 537
Cdd:cd14083 161 ------------------TACGTPGYVAPEVLAQKPYGKAVDCWSIGvisyILLC 197
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
337-592 1.75e-19

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: 88.93  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI---RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd08228  10 IGRGQFSEVYRATCLLDRKPVALKKVQifeMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 ----KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApmekat 489
Cdd:cd08228  90 sqmiKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAA------ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYADPdclprtldfgLNVKLFWEK 566
Cdd:cd08228 164 --------------HSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAalqSPFYGDK----------MNLFSLCQK 219
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031869  567 FVPTDCPP--------AFFPLAAICCRLEPESRP 592
Cdd:cd08228 220 IEQCDYPPlptehyseKLRELVSMCIYPDPDQRP 253
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
334-537 2.18e-19

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: 88.38  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14117  11 GRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQiekEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPmekatt 490
Cdd:cd14117  91 GELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS-------VHAP------ 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  491 kkrTLRkndrkkRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGiVLC 537
Cdd:cd14117 158 ---SLR------RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIG-VLC 194
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
336-542 2.21e-19

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: 89.58  E-value: 2.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMR-SLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05570   2 VLGKGSFGKVMLAERKKTDELYAIKvlkkEVIIEDDDVECT-MTEKRVLAlANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLkdflrsMdpFPWQQKVRF--------AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKr 482
Cdd:cd05570  81 GDL------M--FHIQRARRFteerarfyAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGN- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  483 apmekaTTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQ 542
Cdd:cd05570 152 ------TTS-------------TFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEmLAGQ 193
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
330-540 2.29e-19

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: 88.63  E-value: 2.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKK-IRLESEEEgvpSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEggtlKDFLRSMDPFPWQQKV------RFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveer 480
Cdd:cd07861  80 FLS----MDLKKYLDSLPKGKYMdaelvkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF---- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  481 kRAPMEKATTKKRTLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd07861 152 -GIPVRVYTHEVVTL---------------WYRAPEVLLGSPrYSTPVDIWSIGTIFAEMA 196
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
335-535 2.42e-19

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: 88.05  E-value: 2.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14193  10 EILGGGRFGQVHKCEEKSSGLKLAAK-IIKARSQKEKEEVkNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 kdFLRSMDP---FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN--CLIKLDKTVVVADFGLSrliveeRKRAPMEKa 488
Cdd:cd14193  89 --FDRIIDEnynLTELDTILFIKQICEGIQYMHQMYILHLDLKPENilCVSREANQVKIIDFGLA------RRYKPREK- 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  489 ttkkrtLRKNdrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14193 160 ------LRVN--------FGTPEFLAPEVVNYEFVSFPTDMWSLGVI 192
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
337-603 2.49e-19

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: 88.46  E-value: 2.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGK-VMVMKELIRCDEETQKT--FLTEVKVMRSLDHPNVLKFIGVLyKDKKLNLLTEYIEGGTL 413
Cdd:cd05115  12 LGSGNFGCVKKGVYKMRKKqIDVAIKVLKQGNEKAVRdeMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVMEMASGGPL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSM-DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKATTKK 492
Cdd:cd05115  91 NKFLSGKkDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLS-------KALGADDSYYKA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 RTLRKNDRKkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVyadpdclPRTLDFGLNVKLFWEK---- 566
Cdd:cd05115 164 RSAGKWPLK----------WYAPECINFRKFSSRSDVWSYGVTMWEAFsyGQK-------PYKKMKGPEVMSFIEQgkrm 226
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  567 FVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEA 603
Cdd:cd05115 227 DCPAECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRT 263
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
336-542 2.88e-19

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: 88.98  E-value: 2.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL----IRCDEETQKTfLTEVKVMR-SLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05592   2 VLGKGSFGKVMLAELKGTNQYFAIKALkkdvVLEDDDVECT-MIERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrapmekat 489
Cdd:cd05592  81 GDLMFHIQQSGRFD-EDRARFyGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENI------------ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  490 tkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQ 542
Cdd:cd05592 148 --------YGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEmLIGQ 193
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
337-540 3.09e-19

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: 88.73  E-value: 3.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATG-KVMVMKELIRCDEET-QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd14159   1 IGEGGFGCVYQAVMRNTEyAVKRLKEDSELDWSVvKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLR---SMDPFPWQQKVRFAKGIASGMAYLH--SMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerKRAPmeKAT 489
Cdd:cd14159  81 DRLHcqvSCPCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGLARF-----SRRP--KQP 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  490 TKKRTLRKNDrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14159 154 GMSSTLARTQ-----TVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELL 199
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
337-535 4.16e-19

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: 88.34  E-value: 4.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEetQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14085  11 LGRGATSVVYRCRQKGTQKPYAVKKLKKTVD--KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL---DKTVVVADFGLSRLIVEErkrapmekATTKkr 493
Cdd:cd14085  89 IVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKIVDQQ--------VTMK-- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 5031869  494 tlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14085 159 -----------TVCGTPGYCAPEILRGCAYGPEVDMWSVGVI 189
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
337-548 4.47e-19

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: 87.35  E-value: 4.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIR---CDEETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14665   8 IGSGNFGVARLMRDKQTKELVAVKYIERgekIDENVQR----EIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLikLDKT----VVVADFGLSrliveerkrapmekat 489
Cdd:cd14665  84 FERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTL--LDGSpaprLKICDFGYS---------------- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 tkKRTLRKNDRKkryTVVGNPYWMAPEMLNGKSYDETV-DIFSFGIVLCEIIGQVYA--DPD 548
Cdd:cd14665 146 --KSSVLHSQPK---STVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPfeDPE 202
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
324-605 5.26e-19

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: 88.16  E-value: 5.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  324 QIFRPCDLIHGEVLGKGFFGQAIKVTHKATG---KVMVMKELIR--CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKd 398
Cdd:cd05108   2 RILKETEFKKIKVLGSGAFGTVYKGLWIPEGekvKIPVAIKELReaTSPKANKEILDEAYVMASVDNPHVCRLLGICLT- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  399 KKLNLLTEYIEGGTLKDFLRS-MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd05108  81 STVQLITQLMPFGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 EERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRT---- 553
Cdd:cd05108 161 AEEKEYHAEGGKVPIK------------------WMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASeiss 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  554 -LDFGlnvklfwEKF-VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd05108 223 iLEKG-------ERLpQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMA 269
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
337-539 5.61e-19

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: 87.41  E-value: 5.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQDI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmeKATTKKRTlr 496
Cdd:cd06645  99 YHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQI----------TATIAKRK-- 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  497 kndrkkryTVVGNPYWMAPEML---NGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06645 167 --------SFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIEL 204
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
335-539 8.23e-19

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: 86.98  E-value: 8.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDH-PNVLKFIGVLYK------DKKLNLLTEY 407
Cdd:cd06636  22 EVVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKLEINMLKKYSHhRNIATYYGAFIKksppghDDQLWLVMEF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQK--VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapm 485
Cdd:cd06636 101 CGAGSVTDLVKNTKGNALKEDwiAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--------- 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  486 ekattkKRTLrkndrKKRYTVVGNPYWMAPEMLN-----GKSYDETVDIFSFGIVLCEI 539
Cdd:cd06636 172 ------DRTV-----GRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 219
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
337-548 1.08e-18

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: 86.36  E-value: 1.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIR---CDEETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14662   8 IGSGNFGVARLMRNKETKELVAVKYIERglkIDENVQR----EIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLikLDKTVV----VADFGLSrliveerkrapmekat 489
Cdd:cd14662  84 FERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTL--LDGSPAprlkICDFGYS---------------- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 tKKRTLRKNDRkkryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVLCEIIGQVYA--DPD 548
Cdd:cd14662 146 -KSSVLHSQPK----STVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPfeDPD 202
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
332-601 1.08e-18

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: 86.53  E-value: 1.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKAT-----GKVMVMKELIRCDEETQKTflTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd14187  10 VRGRFLGKGGFAKCYEITDADTkevfaGKIVPKSLLLKPHQKEKMS--MEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapme 486
Cdd:cd14187  88 LCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLA------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  487 kattkkrTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQVYADPDCLPRTLdfgLNVKLFwE 565
Cdd:cd14187 155 -------TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTlLVGKPPFETSCLKETY---LRIKKN-E 223
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  566 KFVPTDCPPAFFPLAAICCRLEPESRPAFSK-LEDSF 601
Cdd:cd14187 224 YSIPKHINPVAASLIQKMLQTDPTARPTINElLNDEF 260
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
327-539 1.09e-18

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: 86.72  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  327 RPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKE-LIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGV-LYKDKKLNLL 404
Cdd:cd06620   3 KNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKViHIDAKSSVRKQILRELQILHECHSPYIVSFYGAfLNENNNIIIC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMC-IIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRa 483
Cdd:cd06620  83 MEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHrIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSIAD- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  484 pmekattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06620 162 ---------------------TFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIEL 196
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
335-541 1.16e-18

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 88.37  E-value: 1.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRcDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05629   7 KVIGKGAFGEVRLVQKKDTGKIYAMKTLLK-SEMFKKDQLAHVKAERDVlaesDSPWVVSLYYSFQDAQYLYLIMEFLPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPwQQKVRF--AKGIASgMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS-------------RL 475
Cdd:cd05629  86 GDLMTMLIKYDTFS-EDVTRFymAECVLA-IEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsayyqKL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  476 IVEERKRAPMEKATT--------------KKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-II 540
Cdd:cd05629 164 LQGKSNKNRIDNRNSvavdsinltmsskdQIATWKKNRRLMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFEcLI 243

                .
gi 5031869  541 G 541
Cdd:cd05629 244 G 244
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
337-597 2.16e-18

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: 85.47  E-value: 2.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd06646  17 VGSGTYGDVYKARNLHTGELAAVK-IIKLEPGDDFSLIQqEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrapmekATTKKRTl 495
Cdd:cd06646  96 IYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKIT----------ATIAKRK- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  496 rkndrkkryTVVGNPYWMAPEML----NGkSYDETVDIFSFGIVLCEIigqvyadPDCLPRTLDFGLNVKLFW---EKFV 568
Cdd:cd06646 165 ---------SFIGTPYWMAPEVAavekNG-GYNQLCDIWAVGITAIEL-------AELQPPMFDLHPMRALFLmskSNFQ 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031869  569 P------TDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd06646 228 PpklkdkTKWSSTFHNFVKISLTKNPKKRPTAERL 262
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
335-597 2.28e-18

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: 85.94  E-value: 2.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDE--ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd07846   7 GLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDdkMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrAPMEKATtkk 492
Cdd:cd07846  87 LDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA-----APGEVYT--- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrkndrkkryTVVGNPYWMAPEMLNGK-SYDETVDIFSFGIVLCEI------------IGQVYADPDCL----PRTLD 555
Cdd:cd07846 159 ------------DYVATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMltgeplfpgdsdIDQLYHIIKCLgnliPRHQE 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  556 FGLNVKLF-------------WEKFVPTDCPPAfFPLAAICCRLEPESRPAFSKL 597
Cdd:cd07846 227 LFQKNPLFagvrlpevkevepLERRYPKLSGVV-IDLAKKCLHIDPDKRPSCSEL 280
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
335-539 2.62e-18

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: 85.56  E-value: 2.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGg 411
Cdd:cd07839   6 EKIGEGTYGTVFKAKNRETHEIVALKR-VRLDDDDEgvpSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQ- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMEKATT 490
Cdd:cd07839  84 DLKKYFDSCNGDIDPEIVKsFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF-----GIPVRCYSA 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 KKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEI 539
Cdd:cd07839 159 EVVTL---------------WYRPPDVLFGaKLYSTSIDMWSAGCIFAEL 193
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
336-539 2.64e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 85.18  E-value: 2.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVlkfigVLYKDK------KLNLLTEY 407
Cdd:cd08223   7 VIGKGSYGEVWLVRHKRDRKQYVIKklNLKNASKRERKAAEQEAKLLSKLKHPNI-----VSYKESfegedgFLYIVMGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPm 485
Cdd:cd08223  82 CEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  486 ekattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08223 161 -------------------TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEM 195
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
335-542 2.64e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 85.64  E-value: 2.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEgg 411
Cdd:PLN00009   8 EKIGEGTYGVVYKARDRVTNETIALKK-IRLEQEDEgvpSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLD-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   412 tlKDFLRSMDPFP-WQQKVRFAKG----IASGMAYLHSMCIIHRDLNSHNCLI-KLDKTVVVADFGLSRLIveerkRAPM 485
Cdd:PLN00009  85 --LDLKKHMDSSPdFAKNPRLIKTylyqILRGIAYCHSHRVLHRDLKPQNLLIdRRTNALKLADFGLARAF-----GIPV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869   486 EKATTKKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEIIGQ 542
Cdd:PLN00009 158 RTFTHEVVTL---------------WYRAPEILLGsRHYSTPVDIWSVGCIFAEMVNQ 200
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
335-542 2.75e-18

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: 86.15  E-value: 2.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL----IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALkkdvVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPmekatt 490
Cdd:cd05620  81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRAS------ 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  491 kkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQ 542
Cdd:cd05620 155 --------------TFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEmLIGQ 193
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
335-540 2.79e-18

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: 86.14  E-value: 2.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIR-CDEETQKT--FLTEVKVMRSLDHPnvlkFIGVLY----KDKKLNLLTEY 407
Cdd:cd05574   7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDKeEMIKRNKVkrVLTEREILATLDHP----FLPTLYasfqTSTHLCFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRS--MDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKraP 484
Cdd:cd05574  83 CPGGELFRLLQKqpGKRLP-EEVARFyAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPP--P 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  485 MEKATTKKRTLRKNDRKKRYTV-----------VGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05574 160 VRKSLRKGSRRSSVKSIEKETFvaepsarsnsfVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEML 226
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
337-539 3.08e-18

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: 85.25  E-value: 3.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKE-LIRCDEETQ-KTFLTEVKVMRSLDHPNVlkfigVLYKDKKLN--LLTEYIEGG- 411
Cdd:cd14049  14 LGKGGYGKVYKVRNKLDGQYYAIKKiLIKKVTKRDcMKVLREVKVLAGLQHPNI-----VGYHTAWMEhvQLMLYIQMQl 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 ---TLKDFLRSMDPFPWQQK--------------VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL-DKTVVVADFGLS 473
Cdd:cd14049  89 celSLWDWIVERNKRPCEEEfksapytpvdvdvtTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGsDIHVRIGDFGLA 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  474 --RLIVEERKRAPMEKATTKKRTLRkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd14049 169 cpDILQDGNDSTTMSRLNGLTHTSG----------VGTCLYAAPEQLEGSHYDFKSDMYSIGVILLEL 226
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
334-597 3.16e-18

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: 85.62  E-value: 3.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGK--------VMVMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKK-LNL 403
Cdd:cd05054  12 GKPLGRGAFGKVIQASAFGIDKsatcrtvaVKMLKEGATASE--HKALMTELKILIHIgHHLNVVNLLGACTKPGGpLMV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSM--------------------------DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNC 457
Cdd:cd05054  90 IVEFCKFGNLSNYLRSKreefvpyrdkgardveeeedddelykEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNI 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  458 LIKLDKTVVVADFGLSRLIVEE----RK---RAPMEkattkkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIF 530
Cdd:cd05054 170 LLSENNVVKICDFGLARDIYKDpdyvRKgdaRLPLK-------------------------WMAPESIFDKVYTTQSDVW 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  531 SFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05054 225 SFGVLLWEIFSLGASPYPGVQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSEL 291
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
332-537 3.47e-18

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: 84.65  E-value: 3.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKELircdEETQKTFLtEVKV-MRSLDHPNVLKFIGV---LYKDKK-LNLLTE 406
Cdd:cd14089   4 ISKQVLGLGINGKVLECFHKKTGEKFALKVL----RDNPKARR-EVELhWRASGCPHIVRIIDVyenTYQGRKcLLVVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFL--RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDL---------NSHNCLIKLdktvvvADFGLSrl 475
Cdd:cd14089  79 CMEGGELFSRIqeRADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLkpenllyssKGPNAILKL------TDFGFA-- 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  476 iveerkrapmeKATTKKRTLRKndrkKRYTvvgnPYWMAPEMLNGKSYDETVDIFSFG----IVLC 537
Cdd:cd14089 151 -----------KETTTKKSLQT----PCYT----PYYVAPEVLGPEKYDKSCDMWSLGvimyILLC 197
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
334-540 3.51e-18

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: 85.83  E-value: 3.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEET--QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKlnllteyIEGG 411
Cdd:cd07866  13 LGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDgfPITALREIKILKKLKHPNVVPLIDMAVERPD-------KSKR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSmdpFPWQ----------QKVRFA--------KGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS 473
Cdd:cd07866  86 KRGSVYMV---TPYMdhdlsgllenPSVKLTesqikcymLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLA 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  474 RLIvEERKRAPMEKATTKKRtlrkndrkkRYT-VVGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07866 163 RPY-DGPPPNPKGGGGGGTR---------KYTnLVVTRWYRPPELLLGeRRYTTAVDIWGIGCVFAEMF 221
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
336-547 3.59e-18

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: 85.57  E-value: 3.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKeLIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd06615   8 ELGAGNGGVVTKVLHRPSGLIMARK-LIHLEikPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYL---HSmcIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrapMEKatt 490
Cdd:cd06615  87 DQVLKKAGRIPENILGKISIAVLRGLTYLrekHK--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS-----MAN--- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  491 kkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADP 547
Cdd:cd06615 157 --------------SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIP 199
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
337-536 5.53e-18

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: 83.85  E-value: 5.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKAT-----GKVMVMKEL--IRCDEETQKTfltEVKVMRSLDHPNVLKFIGVLYKD--KKLNLLTEY 407
Cdd:cd14119   1 LGEGSYGKVKEVLDTETlcrraVKILKKRKLrrIPNGEANVKR---EIQILRRLNHRNVIKLVDVLYNEekQKLYMVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDP-FP-WQQKVRFAKGIaSGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFG----LSRLIVEERK 481
Cdd:cd14119  78 CVGGLQEMLDSAPDKrLPiWQAHGYFVQLI-DGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDLFAEDDTC 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  482 RapmekattkkrtlrkndrkkryTVVGNPYWMAPEMLNG-KSYDE-TVDIFSFGIVL 536
Cdd:cd14119 157 T----------------------TSQGSPAFQPPEIANGqDSFSGfKVDIWSAGVTL 191
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
337-539 5.53e-18

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: 84.84  E-value: 5.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVthKATGKVMVMKELIRCDEET--QKTFLTEVKVMRsldHPNVLKFIGVLYKDK----KLNLLTEYIEG 410
Cdd:cd14144   3 VGKGRYGEVWKG--KWRGEKVAVKIFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHEN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRS--MDPfpwQQKVRFAKGIASGMAYLHSM--------CIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEr 480
Cdd:cd14144  78 GSLYDFLRGntLDT---QSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISE- 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  481 krapmekatTKKRTLRKNDRkkrytvVGNPYWMAPEML----NGKSYDE--TVDIFSFGIVLCEI 539
Cdd:cd14144 154 ---------TNEVDLPPNTR------VGTKRYMAPEVLdeslNRNHFDAykMADMYSFGLVLWEI 203
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
335-539 6.75e-18

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: 84.42  E-value: 6.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKvtHKATGKVMVMKELIRCDEetqKTFLTEVKVMRS--LDHPNVLKFIGVLYKDK----KLNLLTEYI 408
Cdd:cd14143   1 ESIGKGRFGEVWR--GRWRGEDVAVKIFSSREE---RSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSDYH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMdPFPWQQKVRFAKGIASGMAYLHsMCII---------HRDLNSHNCLIKLDKTVVVADFGLsrlivee 479
Cdd:cd14143  76 EHGSLFDYLNRY-TVTVEGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDLKSKNILVKKNGTCCIADLGL------- 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  480 rkrAPMEKATTKKRTLRKNDRkkrytvVGNPYWMAPEML----NGKSYD--ETVDIFSFGIVLCEI 539
Cdd:cd14143 147 ---AVRHDSATDTIDIAPNHR------VGTKRYMAPEVLddtiNMKHFEsfKRADIYALGLVFWEI 203
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
373-597 7.50e-18

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: 84.29  E-value: 7.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  373 FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDP-----------------FPWQQKVRFAKGI 435
Cdd:cd05090  54 FQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQI 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  436 ASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRtlrkndrkkrytvvgnpyWMAP 515
Cdd:cd05090 134 AAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIR------------------WMPP 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  516 EMLNGKSYDETVDIFSFGIVLCEIIG---QVYadpdclprtldFGLNVKLFWEKF-------VPTDCPPAFFPLAAICCR 585
Cdd:cd05090 196 EAIMYGKFSSDSDIWSFGVVLWEIFSfglQPY-----------YGFSNQEVIEMVrkrqllpCSEDCPPRMYSLMTECWQ 264
                       250
                ....*....|..
gi 5031869  586 LEPESRPAFSKL 597
Cdd:cd05090 265 EIPSRRPRFKDI 276
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
336-540 7.79e-18

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 84.16  E-value: 7.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTF---LTEVKVMRSLdHPNVLKFIGVLYKDK-KLNLLTEYIEGG 411
Cdd:cd05608   8 VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYegaMVEKRILAKV-HSRFIVSLAYAFQTKtDLCLVMTIMNGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDP----FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapMEK 487
Cdd:cd05608  87 DLRYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA-----------VEL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  488 ATTKKRTlrkndrkKRYTvvGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05608 156 KDGQTKT-------KGYA--GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMI 199
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
336-540 8.62e-18

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: 83.60  E-value: 8.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAI---KVTHKATGKVMVMKEL----IRCDEETQKTFLTEVKVMRSL-DHPnvlkFIGVLY----KDKKLNL 403
Cdd:cd05583   1 VLGTGAYGKVFlvrKVGGHDAGKLYAMKVLkkatIVQKAKTAEHTMTERQVLEAVrQSP----FLVTLHyafqTDAKLHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPwQQKVRFAKG-IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkr 482
Cdd:cd05583  77 ILDYVNGGELFTHLYQREHFT-ESEVRIYIGeIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPG--- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  483 apmekattkkrtlrKNDRKkrYTVVGNPYWMAPEMLNGKS--YDETVDIFSFGIVLCEII 540
Cdd:cd05583 153 --------------ENDRA--YSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELL 196
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
335-539 9.45e-18

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: 83.13  E-value: 9.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQKTfLTEV-KVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIeG 410
Cdd:cd14050   7 SKLGEGSFGEVFKVRSREDGKlyaVKRSRSRFRGEKDRKRK-LEEVeRHEKLGEHPNCVRFIKAWEEKGILYIQTELC-D 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrLIVEerkrapmekatt 490
Cdd:cd14050  85 TSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFG---LVVE------------ 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  491 kkrtLRKNDRKkrYTVVGNPYWMAPEMLNGkSYDETVDIFSFGIVLCEI 539
Cdd:cd14050 150 ----LDKEDIH--DAQEGDPRYMAPELLQG-SFTKAADIFSLGITILEL 191
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
324-605 9.58e-18

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: 84.35  E-value: 9.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  324 QIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQK-----TFLTEVKVMRSLDHPNVLKFIGVLYKd 398
Cdd:cd05110   2 RILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGpkanvEFMDEALIMASMDHPHLVRLLGVCLS- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  399 KKLNLLTEYIEGGTLKDFLRS-MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd05110  81 PTIQLVTQLMPHGCLLDYVHEhKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 EERKRApmeKATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYADPDC--LPR 552
Cdd:cd05110 161 GDEKEY---NADGGKMPIK---------------WMALECIHYRKFTHQSDVWSYGVTIWELMtfgGKPYDGIPTreIPD 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  553 TLDFGLNVKLfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd05110 223 LLEKGERLPQ------PPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMA 269
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
340-540 1.35e-17

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: 83.61  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  340 GFFGQAIKVTHKATGKVMVMKEL----IRCDEETQKTFlTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd05609  11 GAYGAVYLVRHRETRQRFAMKKInkqnLILRNQIQQVF-VERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDCAT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQ-QKVRFAKGIAsGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKATT---- 490
Cdd:cd05609  90 LLKNIGPLPVDmARMYFAETVL-ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLS-------KIGLMSLTTNlyeg 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  491 --KKRTLRKNDRKkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05609 162 hiEKDTREFLDKQ----VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 209
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
337-539 1.38e-17

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: 83.55  E-value: 1.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd05093  18 FGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKF 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDP-------------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkra 483
Cdd:cd05093  98 LRAHGPdavlmaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYS----- 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  484 pmekattkkrtlrkndrKKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05093 173 -----------------TDYYRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEI 215
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
333-535 1.43e-17

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: 83.09  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  333 HGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14192   8 PHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LkdFLRSMDP---FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN--CLIKLDKTVVVADFGLSrliveeRKRAPMEK 487
Cdd:cd14192  88 L--FDRITDEsyqLTELDAILFTRQICEGVHYLHQHYILHLDLKPENilCVNSTGNQIKIIDFGLA------RRYKPREK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  488 attkkrtLRKNdrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14192 160 -------LKVN--------FGTPEFLAPEVVNYDFVSFPTDMWSVGVI 192
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
330-540 1.81e-17

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: 84.31  E-value: 1.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd05594  26 DFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKdFLRSMDPFPWQQKVRF-AKGIASGMAYLHS-MCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRA 483
Cdd:cd05594 105 EYANGGELF-FHLSRERVFSEDRARFyGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC-------KEG 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  484 PMEKATTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05594 177 IKDGATMK-------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 220
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
330-599 1.89e-17

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: 83.24  E-value: 1.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEET--QKTFLTEVKV-MRSLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd06617   2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKR-IRATVNSqeQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGgTLKDFLRSMdpFPWQQKV------RFAKGIASGMAYLHS-MCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEE 479
Cdd:cd06617  81 VMDT-SLDKFYKKV--YDKGLTIpedilgKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  480 rkRAPMEKATTKkrtlrkndrkkrytvvgnPYwMAPEMLNG----KSYDETVDIFSFGIVLCEI---------------- 539
Cdd:cd06617 158 --VAKTIDAGCK------------------PY-MAPERINPelnqKGYDVKSDVWSLGITMIELatgrfpydswktpfqq 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  540 IGQVYADPDclPrtldfglnvKLFWEKFvptdcPPAFFPLAAICCRLEPESRPAFSKLED 599
Cdd:cd06617 217 LKQVVEEPS--P---------QLPAEKF-----SPEFQDFVNKCLKKNYKERPNYPELLQ 260
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
334-536 2.13e-17

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: 82.43  E-value: 2.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKatGKVMVMKELIRC--DEETQKTFLTEVKVMRsLDHPN---VLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd13979   8 QEPLGSGGFGSVYKATYK--GETVAVKIVRRRrkNRASRQSFWAELNAAR-LRHENivrVLAAETGTDFASLGLIIMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFL-RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkRAPMEK 487
Cdd:cd13979  85 GNGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKL-----GEGNEV 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  488 ATtkkrtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd13979 160 GT------------PRSHIGGTYTYRAPELLKGERVTPKADIYSFGITL 196
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
337-538 2.22e-17

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: 83.19  E-value: 2.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLY-KDKKLN-------LLT 405
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKK-VLMENEKEGfpiTALREIKILQLLKHENVVNLIEICRtKATPYNrykgsiyLVF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGgTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrap 484
Cdd:cd07865  99 EFCEH-DLAGLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFS------- 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  485 mekattkkrtLRKNDRKKRYT--VVgNPYWMAPEMLNG-KSYDETVDIFSFGIVLCE 538
Cdd:cd07865 171 ----------LAKNSQPNRYTnrVV-TLWYRPPELLLGeRDYGPPIDMWGAGCIMAE 216
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
337-597 2.29e-17

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 82.97  E-value: 2.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEIrLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSLDK 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FL---RSMDPFPWQQKVRFAKGIASGMAYL-HSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrAPMEKATTK 491
Cdd:cd06622  89 LYaggVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVS---------GNLVASLAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 krtlrkndrkkryTVVGNPYWMAPEMLNGK------SYDETVDIFSFGIVLCEIIGQVYADPdclPRTLDfglNVKLFWE 565
Cdd:cd06622 160 -------------TNIGCQSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMALGRYPYP---PETYA---NIFAQLS 220
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 5031869  566 KFV---PTDCPPAFFPLA----AICCRLEPESRPAFSKL 597
Cdd:cd06622 221 AIVdgdPPTLPSGYSDDAqdfvAKCLNKIPNRRPTYAQL 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
335-536 2.37e-17

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 82.37  E-value: 2.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDE--ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14202   8 DLIGHGAFAVVFKGRHKEKHDLEVAVKCINKKNlaKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK---------TVVVADFGLSRLIVEERKRA 483
Cdd:cd14202  88 LADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARYLQNNMMAA 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  484 pmekattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14202 168 ---------------------TLCGSPMYMAPEVIMSQHYDAKADLWSIGTII 199
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
330-539 2.55e-17

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: 82.75  E-value: 2.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAI-----KVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLL 404
Cdd:cd05094   6 DIVLKRELGEGAFGKVFlaecyNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDP--------FPWQ--------QKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVA 468
Cdd:cd05094  86 FEYMKHGDLNKFLRAHGPdamilvdgQPRQakgelglsQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  469 DFGLSRLIVEerkrapmekattkkrtlrkndrKKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05094 166 DFGMSRDVYS----------------------TDYYRVGGHTMlpirWMPPESIMYRKFTTESDVWSFGVILWEI 218
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
324-605 2.62e-17

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: 82.76  E-value: 2.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  324 QIFRPCDLIHGEVLGKGFFGQAIKVTHKATG---KVMVMKELIR--CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKd 398
Cdd:cd05109   2 RILKETELKKVKVLGSGAFGTVYKGIWIPDGenvKIPVAIKVLRenTSPKANKEILDEAYVMAGVGSPYVCRLLGICLT- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  399 KKLNLLTEYIEGGTLKDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRL-- 475
Cdd:cd05109  81 STVQLVTQLMPYGCLLDYVReNKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLld 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  476 IVEERKRAPMEKATTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIgQVYADP------DC 549
Cdd:cd05109 161 IDETEYHADGGKVPIK--------------------WMALESILHRRFTHQSDVWSYGVTVWELM-TFGAKPydgipaRE 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  550 LPRTLDFGLNVKLfwekfvPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd05109 220 IPDLLEKGERLPQ------PPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMA 269
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
335-535 2.65e-17

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: 82.73  E-value: 2.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSRLiveerkrapmekattk 491
Cdd:cd14166  89 DRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKM---------------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031869  492 krtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14166 153 ------EQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVI 190
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
337-540 2.67e-17

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: 82.80  E-value: 2.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQ--KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVikKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHTVLN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkrt 494
Cdd:cd07847  89 ELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARIL------------------ 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  495 lrkNDRKKRYT-VVGNPYWMAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd07847 151 ---TGPGDDYTdYVATRWYRAPELLVGDTqYGPPVDVWAIGCVFAELL 195
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
336-542 2.80e-17

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: 83.51  E-value: 2.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKD-KKLNLLTEYIEG 410
Cdd:cd05615  17 VLGKGSFGKVMLAERKGSDELyaikILKKDVVIQDDDVECT-MVEKRVLALQDKPPFLTQLHSCFQTvDRLYFVMEYVNG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKATT 490
Cdd:cd05615  96 GDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC-------KEHMVEGVTT 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  491 KkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ 542
Cdd:cd05615 169 R-------------TFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLaGQ 208
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
336-539 2.86e-17

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: 82.74  E-value: 2.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDE--ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd07848   8 VVGEGAYGVVLKCRHKETKEIVAIKKFKDSEEneEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNML 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 kDFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKk 492
Cdd:cd07848  88 -ELLEEMPNGVPPEKVRsYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTEYVATR- 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  493 rtlrkndrkkrytvvgnpYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd07848 166 ------------------WYRSPELLLGAPYGKAVDMWSVGCILGEL 194
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
334-535 2.91e-17

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: 82.37  E-value: 2.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLT------EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd14194  10 GEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSredierEVSILKEIQHPNVITLHEVYENKTDVILILEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIkLDKTV-----VVADFGLSRliveerkr 482
Cdd:cd14194  90 VAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIML-LDRNVpkpriKIIDFGLAH-------- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  483 apmekattkkRTLRKNDRKkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14194 161 ----------KIDFGNEFK---NIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 200
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
323-597 3.29e-17

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: 82.42  E-value: 3.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  323 QQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCD-EETQKTFLTEVKV-MRSLDHPNVLKFIGVLYKDKK 400
Cdd:cd06618   9 KYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGnKEENKRILMDLDVvLKSHDCPYIVKCYGYFITDSD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  401 LNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYL---HSmcIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd06618  89 VFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLkekHG--VIHRDVKPSNILLDESGNVKLCDFGISGRLV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  478 EerkrapmEKATTKKrtlrkndrkkrytvVGNPYWMAPEML---NGKSYDETVDIFSFGIVLCEIIGQVYADPDClprTL 554
Cdd:cd06618 167 D-------SKAKTRS--------------AGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYRNC---KT 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  555 DFGLNVKLFWEKfvPTDCPPA------FFPLAAICCRLEPESRPAFSKL 597
Cdd:cd06618 223 EFEVLTKILNEE--PPSLPPNegfspdFCSFVDLCLTKDHRYRPKYREL 269
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
152-236 3.56e-17

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 76.55  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    152 LISMPATTEGRRGFSVSVESACSnyATTVQVKEVNRMhiSPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTL 231
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQG--DPGIFVSEVLPG--GAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKV 76

                  ....*
gi 5031869    232 QLLIE 236
Cdd:pfam00595  77 TLTIL 81
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
335-540 4.13e-17

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: 82.36  E-value: 4.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAI---KVTHKATGKVMVMKEL----IRCDEETQKTFLTEVKVmrsLDHPNVLKFIGVLY----KDKKLNL 403
Cdd:cd05613   6 KVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLkkatIVQKAKTAEHTRTERQV---LEHIRQSPFLVTLHyafqTDTKLHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSR-LIVEERKR 482
Cdd:cd05613  83 ILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKeFLLDENER 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  483 ApmekattkkrtlrkndrkkrYTVVGNPYWMAPEMLNG--KSYDETVDIFSFGIVLCEII 540
Cdd:cd05613 163 A--------------------YSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELL 202
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
376-535 4.33e-17

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: 81.55  E-value: 4.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLD-HPNVLKFIGVLYKDKKLNL--------LTEYIEGG-TLKDFLR-SMDPfpwqqkVRFAKGIASGMAYLHS 444
Cdd:cd13982  44 EVQLLRESDeHPNVIRYFCTEKDRQFLYIalelcaasLQDLVESPrESKLFLRpGLEP------VRLLRQIASGLAHLHS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  445 MCIIHRDLNSHNCLIKLDKT-----VVVADFGLSRliveerkrapmeKATTKKRTLRkndrkKRYTVVGNPYWMAPEMLN 519
Cdd:cd13982 118 LNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCK------------KLDVGRSSFS-----RRSGVAGTSGWIAPEMLS 180
                       170
                ....*....|....*....
gi 5031869  520 GKSYDET---VDIFSFGIV 535
Cdd:cd13982 181 GSTKRRQtraVDIFSLGCV 199
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
335-543 4.50e-17

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: 82.40  E-value: 4.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELI-RCDEETQKtfltEVKVMRSLD-HPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14179  13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSkRMEANTQR----EIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKlDKT----VVVADFGLSRLiveerkRAPmeka 488
Cdd:cd14179  89 LLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFT-DESdnseIKIIDFGFARL------KPP---- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  489 ttkkrtlrknDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV 543
Cdd:cd14179 158 ----------DNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLsGQV 203
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
337-575 4.57e-17

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: 81.26  E-value: 4.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKA-TGKVMVMKELIRCDEETQKTFLT-EVKVMRSLDHPNVLKfigvLYKDKKLN----LLTEYIEG 410
Cdd:cd14120   1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNLLGkEIKILKELSHENVVA----LLDCQETSssvyLVMEYCNG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPwQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIK---------LDKTVVVADFGLSRLIVEER 480
Cdd:cd14120  77 GDLADYLQAKGTLS-EDTIRvFLQQIAAAMKALHSKGIVHRDLKPQNILLShnsgrkpspNDIRLKIADFGFARFLQDGM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 KRApmekattkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVlceiigqVYadpDCLPRTLDFGLN- 559
Cdd:cd14120 156 MAA---------------------TLCGSPMYMAPEVIMSLQYDAKADLWSIGTI-------VY---QCLTGKAPFQAQt 204
                       250       260
                ....*....|....*....|....*
gi 5031869  560 ---VKLFWEKF------VPTDCPPA 575
Cdd:cd14120 205 pqeLKAFYEKNanlrpnIPSGTSPA 229
LIM1_LIMK1 cd09462
The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain ...
12-65 4.58e-17

The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188846 [Multi-domain]  Cd Length: 74  Bit Score: 76.08  E-value: 4.58e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   12 CPGCGDHIAPSQiWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYW 65
Cdd:cd09462  22 CASCGQSIYDGQ-YLQALNSDWHADCFRCCECGASLSHWYYEKDGRLFCKKDYW 74
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
383-539 4.85e-17

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: 82.10  E-value: 4.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  383 LDHPNVLKFIG----VLYKDKKLNLLTEYIEGGTLKDFLRSmDPFPWQQKVRFAKGIASGMAYLHS----MC----IIHR 450
Cdd:cd14142  56 LRHENILGFIAsdmtSRNSCTQLWLITHYHENGSLYDYLQR-TTLDHQEMLRLALSAASGLVHLHTeifgTQgkpaIAHR 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  451 DLNSHNCLIKLDKTVVVADFGLsrliveerkrAPMEKATTKKRTLRKNDRkkrytvVGNPYWMAPEML----NGKSYD-- 524
Cdd:cd14142 135 DLKSKNILVKSNGQCCIADLGL----------AVTHSQETNQLDVGNNPR------VGTKRYMAPEVLdetiNTDCFEsy 198
                       170
                ....*....|....*
gi 5031869  525 ETVDIFSFGIVLCEI 539
Cdd:cd14142 199 KRVDIYAFGLVLWEV 213
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
335-542 5.14e-17

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: 81.39  E-value: 5.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLykDKKLNLLTEYIEGGT 412
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIKcpPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEYMETGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSmDPFPWQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapMEKATt 490
Cdd:cd14025  80 LEKLLAS-EPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKW---------NGLSH- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  491 kkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKS--YDETVDIFSFGIVLCEIIGQ 542
Cdd:cd14025 149 -------SHDLSRDGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQ 195
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
337-549 5.15e-17

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: 81.69  E-value: 5.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI--RCDEETQKTFLTEVKVMRSLDHPNVLKFI----GVLYKDKKLNLLTEYIEG 410
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCELQdrKLTKAEQQRFKEEAEMLKGLQHPNIVRFYdsweSVLKGKKCIVLVTELMTS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIK-LDKTVVVADFGLSRLIveerkRAPMEK 487
Cdd:cd14031  98 GTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLM-----RTSFAK 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  488 attkkrtlrkndrkkryTVVGNPYWMAPEMLNgKSYDETVDIFSFGIVLCEIIGQVYADPDC 549
Cdd:cd14031 173 -----------------SVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSEC 216
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
336-543 5.68e-17

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: 82.35  E-value: 5.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKD-KKLNLLTEYIEG 410
Cdd:cd05616   7 VLGKGSFGKVMLAERKGTDELyavkILKKDVVIQDDDVECT-MVEKRVLALSGKPPFLTQLHSCFQTmDRLYFVMEYVNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKATT 490
Cdd:cd05616  86 GDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMC-------KENIWDGVTT 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  491 KkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV 543
Cdd:cd05616 159 K-------------TFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLaGQA 199
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
334-536 5.97e-17

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: 80.92  E-value: 5.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14074   8 EETLGRGHFAVVKLARHVFTGEKVAVKviDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI-KLDKTVVVADFGLSrliveeRKRAPMEKAT 489
Cdd:cd14074  88 DMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS------NKFQPGEKLE 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  490 TKkrtlrkndrkkrytvVGNPYWMAPEMLNGKSYDE-TVDIFSFGIVL 536
Cdd:cd14074 162 TS---------------CGSLAYSAPEILLGDEYDApAVDIWSLGVIL 194
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
336-540 6.04e-17

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: 82.06  E-value: 6.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQ----------------AIKVTHKATGKVmvmKELIRCDEEtqKTFLTEVKvmrsldHPNVLKFIGVLYKDK 399
Cdd:cd05582   2 VLGQGSFGKvflvrkitgpdagtlyAMKVLKKATLKV---RDRVRTKME--RDILADVN------HPFIVKLHYAFQTEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  400 KLNLLTEYIEGGTLkdFLR-SMDPFPWQQKVRFAKG-IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV 477
Cdd:cd05582  71 KLYLILDFLRGGDL--FTRlSKEVMFTEEDVKFYLAeLALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESI 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  478 EERKRApmekattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05582 149 DHEKKA--------------------YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 191
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
332-536 6.38e-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: 81.38  E-value: 6.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKAT----GKVMVMKELIRCD----EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNL 403
Cdd:cd14076   4 ILGRTLGEGEFGKVKLGWPLPKanhrSGVQVAIKLIRRDtqqeNCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkra 483
Cdd:cd14076  84 VLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHF---- 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  484 pmekattkkrtlrKNDRKKryTVVGNPYWMAPEMLNGKS-YDET-VDIFSFGIVL 536
Cdd:cd14076 160 -------------NGDLMS--TSCGSPCYAAPELVVSDSmYAGRkADIWSCGVIL 199
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
337-539 6.77e-17

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: 82.02  E-value: 6.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI---RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd06635  33 IGHGSFGAVYFARDVRTSEVVAIKKMSysgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSAS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrAPMEkattkkr 493
Cdd:cd06635 113 DLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA------SPAN------- 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  494 tlrkndrkkryTVVGNPYWMAPEM---LNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06635 180 -----------SFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIEL 217
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
337-539 8.32e-17

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: 81.15  E-value: 8.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAI--KVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14206   5 IGNGWFGKVIlgEIFSDYTPAQVVVKELrVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRS------MDP-FPWQQKV---RFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkra 483
Cdd:cd14206  85 KRYLRAqrkadgMTPdLPTRDLRtlqRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSH--------- 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  484 pmekattkkrtlrkNDRKKRYTVVGNPYWM-----APEML-----NGKSYDET--VDIFSFGIVLCEI 539
Cdd:cd14206 156 --------------NNYKEDYYLTPDRLWIplrwvAPELLdelhgNLIVVDQSkeSNVWSLGVTIWEL 209
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
334-555 9.48e-17

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: 80.29  E-value: 9.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKV----THKATGKVMVMKELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14186   6 LNLLGKGSFACVYRArslhTGLEVAIKMIDKKAMQKAGMVQRV-RNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSM-DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmeka 488
Cdd:cd14186  85 NGEMSRYLKNRkKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLA--------------- 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  489 ttkkrTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQVYADPDCLPRTLD 555
Cdd:cd14186 150 -----TQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTlLVGRPPFDTDTVKNTLN 212
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
335-539 1.03e-16

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: 81.30  E-value: 1.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQktFLTEVKVMRSLDH-PNVLKFIGVLYK------DKKLNLLTE 406
Cdd:cd06637  12 ELVGNGTYGQVYKGRHVKTGQLAAIKVMdVTGDEEEE--IKQEINMLKKYSHhRNIATYYGAFIKknppgmDDQLWLVME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSMDPFPWQQK--VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrAP 484
Cdd:cd06637  90 FCGAGSVTDLIKNTKGNTLKEEwiAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS---------AQ 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  485 MEKATtkkrtlrkndrKKRYTVVGNPYWMAPEMLN-----GKSYDETVDIFSFGIVLCEI 539
Cdd:cd06637 161 LDRTV-----------GRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEM 209
pknD PRK13184
serine/threonine-protein kinase PknD;
337-540 1.15e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 84.05  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   337 LGKGFFGQAIKVTHKATGKVMVMKElIRCD----EETQKTFLTEVKVMRSLDHPNVLKfIGVLYKDKKLNLLT-EYIEGG 411
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRVALKK-IREDlsenPLLKKRFLREAKIAADLIHPGIVP-VYSICSDGDPVYYTmPYIEGY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   412 TLKDFLRSMdpfpWQQKVR----------------FAKgIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRL 475
Cdd:PRK13184  88 TLKSLLKSV----WQKESLskelaektsvgaflsiFHK-ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIF 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   476 IVEERK-----RAPMEKATTKKRTlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:PRK13184 163 KKLEEEdlldiDVDERNICYSSMT-------IPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQML 225
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
337-592 1.18e-16

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: 80.85  E-value: 1.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI---RCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd08229  32 IGRGQFSEVYRATCLLDGVPVALKKVQifdLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 ----KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRApmekat 489
Cdd:cd08229 112 srmiKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAA------ 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYADPdclprtldfgLNVKLFWEK 566
Cdd:cd08229 186 --------------HSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAAlqsPFYGDK----------MNLYSLCKK 241
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031869  567 FVPTDCPP--------AFFPLAAICCRLEPESRP 592
Cdd:cd08229 242 IEQCDYPPlpsdhyseELRQLVNMCINPDPEKRP 275
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
336-536 1.19e-16

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: 80.63  E-value: 1.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLD-HPNVLKFIGVLYKDKKLN--------LLTE 406
Cdd:cd14036   7 VIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGKEESdqgqaeylLLTE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGtLKDFLRSMD---PFPWQQKVRFAKGIASGMAYLH--SMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerk 481
Cdd:cd14036  87 LCKGQ-LVDFVKKVEapgPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEA---- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  482 RAPMEKATTKKRTLRKNDRKKRYTvvgnPYWMAPEMLNGKS---YDETVDIFSFGIVL 536
Cdd:cd14036 162 HYPDYSWSAQKRSLVEDEITRNTT----PMYRTPEMIDLYSnypIGEKQDIWALGCIL 215
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
334-535 1.23e-16

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: 80.22  E-value: 1.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLT------EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd14105  10 GEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSredierEVSILRQVLHPNIITLHDVFENKTDVVLILEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIkLDKTV-----VVADFGLSRLIveerkr 482
Cdd:cd14105  90 VAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIML-LDKNVpipriKLIDFGLAHKI------ 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  483 apmekattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14105 163 ---------------EDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 200
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
335-536 1.27e-16

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: 80.48  E-value: 1.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVM-----KELIRCDEETQKTFLTEVKVMRSLD-HPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd14093   9 EILGRGVSSTVRRCIEKETGQefaVKIIditgeKSSENEAEELREATRREIEILRQVSgHPNIIELHDVFESPTFIFLVF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapm 485
Cdd:cd14093  89 ELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEK---- 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  486 ekattkkrtLRKndrkkrytVVGNPYWMAPEML------NGKSYDETVDIFSFGIVL 536
Cdd:cd14093 165 ---------LRE--------LCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIM 204
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
334-604 1.39e-16

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: 80.40  E-value: 1.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKvtHKATGKVMVmkELIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14152   5 GELIGQGRWGKVHR--GRWHGEVAI--RLLEIDGNNQdhlKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKtVVVADFGL---SRLIVEERkrapme 486
Cdd:cd14152  81 RTLYSFVRDPKTSLDINKTRqIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK-VVITDFGLfgiSGVVQEGR------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  487 kattkkrtlRKNDRKKRYTVVgnpYWMAPE----MLNGKSYD-----ETVDIFSFGIVLCEIigQVYADP------DCLP 551
Cdd:cd14152 154 ---------RENELKLPHDWL---CYLAPEivreMTPGKDEDclpfsKAADVYAFGTIWYEL--QARDWPlknqpaEALI 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  552 RTLDFGLNVKlfwEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14152 220 WQIGSGEGMK---QVLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
309-597 1.39e-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: 80.33  E-value: 1.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  309 ISRSESLRCS----SSYSQQIFRPCDLIHGEVLgkgffgqAIKVTHKATgkvmvmKELIRCdeetqktFLTEVKVMRSLD 384
Cdd:cd14042   1 SLSSSSYGSLmtaaSFDQSQIFTKTGYYKGNLV-------AIKKVNKKR------IDLTRE-------VLKELKHMRDLQ 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  385 HPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRS----MDpfpWQQKVRFAKGIASGMAYLHSMCII-HRDLNSHNCLI 459
Cdd:cd14042  61 HDNLTRFIGACVDPPNICILTEYCPKGSLQDILENedikLD---WMFRYSLIHDIVKGMHYLHDSEIKsHGNLKSSNCVV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  460 klDKTVV--VADFGLSRLIVEERKRAPMEKATTKKrtlrkndrkkrytvvgnpYWMAPEML--NGKSYDETV--DIFSFG 533
Cdd:cd14042 138 --DSRFVlkITDFGLHSFRSGQEPPDDSHAYYAKL------------------LWTAPELLrdPNPPPPGTQkgDVYSFG 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  534 IVLCEIIGqvyadpdclpRTLDFGLNVKLF-----WEKFVPTDCPPAFFP-LAAICCRLE------------PESRPAFS 595
Cdd:cd14042 198 IILQEIAT----------RQGPFYEEGPDLspkeiIKKKVRNGEKPPFRPsLDELECPDEvlslmqrcwaedPEERPDFS 267

                ..
gi 5031869  596 KL 597
Cdd:cd14042 268 TL 269
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
355-605 1.44e-16

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: 80.31  E-value: 1.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  355 KVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFP------WQQK 428
Cdd:cd14044  32 KVVILKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKISYPdgtfmdWEFK 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  429 VRFAKGIASGMAYLH-SMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrapmekattkkrtlrkndrkkrytvv 507
Cdd:cd14044 112 ISVMYDIAKGMSYLHsSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPSKD-------------------------- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  508 gnpYWMAPEMLNGKSYDETVDIFSFGIVLCEII--GQVYADPDCLPRtldfglNVKLFWEKFVPTDCPpaFFP------- 578
Cdd:cd14044 166 ---LWTAPEHLRQAGTSQKGDVYSYGIIAQEIIlrKETFYTAACSDR------KEKIYRVQNPKGMKP--FRPdlnlesa 234
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  579 ---------LAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:cd14044 235 gererevygLVKNCWEEDPEKRPDFKKIENTLAKIF 270
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
335-540 2.07e-16

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: 79.66  E-value: 2.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd14191   8 ERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN--CLIKLDKTVVVADFGLSRliveerkraPMEKATTK 491
Cdd:cd14191  88 ERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTKIKLIDFGLAR---------RLENAGSL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  492 KrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGiVLCEII 540
Cdd:cd14191 159 K------------VLFGTPEFVAPEVINYEPIGYATDMWSIG-VICYIL 194
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
337-540 2.66e-16

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: 79.49  E-value: 2.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRC---DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKrikKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliVEERkrapmEKATTK 491
Cdd:cd05577  81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLA---VEFK-----GGKKIK 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 KRtlrkndrkkrytvVGNPYWMAPEML-NGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05577 153 GR-------------VGTHGYMAPEVLqKEVAYDFSVDWFALGCMLYEMI 189
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
337-473 2.75e-16

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: 79.55  E-value: 2.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAI--KVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05042   3 IGNGWFGKVLlgEIYSGTSVAQVVVKELkASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDL 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  414 KDFLRS------MDPFPWQQKvRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS 473
Cdd:cd05042  83 KAYLRSereherGDSDTRTLQ-RMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLA 147
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
335-566 2.77e-16

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: 79.28  E-value: 2.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTH-KATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14201  12 DLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKT---------VVVADFGLSRLIveerkRA 483
Cdd:cd14201  92 LADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIADFGFARYL-----QS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  484 PMEKATtkkrtlrkndrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEiigqvyadpdCLPRTLDFGLN---- 559
Cdd:cd14201 167 NMMAAT----------------LCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQ----------CLVGKPPFQANspqd 220

                ....*..
gi 5031869  560 VKLFWEK 566
Cdd:cd14201 221 LRMFYEK 227
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
337-536 3.22e-16

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: 79.26  E-value: 3.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKElIRC-DEETQKTFLTEVKVMRSLDHPNVLK-----FIGVLYKDKKLNLLTEYIEG 410
Cdd:cd13986   8 LGEGGFSFVYLVEDLSTGRLYALKK-ILChSKEDVKEAMREIENYRLFNHPNILRlldsqIVKEAGGKKEVYLLLPYYKR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSM----DPFPWQQKVRFAKGIASGMAYLHSMCII---HRDLNSHNCLIKLDKTVVVADFG---LSRLIVEER 480
Cdd:cd13986  87 GSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGsmnPARIEIEGR 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  481 KRAPMEKATTKKRtlrkndrkkrytvvGNPYWMAPEMLNGKSY---DETVDIFSFGIVL 536
Cdd:cd13986 167 REALALQDWAAEH--------------CTMPYRAPELFDVKSHctiDEKTDIWSLGCTL 211
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
334-592 4.39e-16

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: 78.71  E-value: 4.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATG-KVMVM---KELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14070   7 GRKLGEGSFAKVREGLHAVTGeKVAIKvidKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMekat 489
Cdd:cd14070  87 GGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDPF---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIgqvyadPDCLPRTLDfGLNVKLFWEKFV- 568
Cdd:cd14070 163 --------------STQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAML------TGTLPFTVE-PFSLRALHQKMVd 221
                       250       260       270
                ....*....|....*....|....*....|
gi 5031869  569 ------PTDCPPAFFPLAAICCRLEPESRP 592
Cdd:cd14070 222 kemnplPTDLSPGAISFLRSLLEPDPLKRP 251
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
334-535 4.64e-16

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: 78.50  E-value: 4.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14183  11 GRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIqNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI----KLDKTVVVADFGLSRLIveerkRAPMeka 488
Cdd:cd14183  91 LFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVV-----DGPL--- 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  489 ttkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14183 163 ---------------YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVI 194
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
335-540 5.21e-16

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: 78.55  E-value: 5.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIR-------CDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd13993   6 SPIGEGAYGVVYLAVDLRTGRKYAIKCLYKsgpnskdGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSMDPFPWQQKV--RFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK-TVVVADFGLsrliveerkra 483
Cdd:cd13993  86 YCPNGDLFEAITENRIYVGKTELikNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGL----------- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  484 pmekATTKKRTLRKNdrkkrytvVGNPYWMAPEML-----NGKSYD-ETVDIFSFGIVLCEII 540
Cdd:cd13993 155 ----ATTEKISMDFG--------VGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLT 205
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
337-574 5.21e-16

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 78.85  E-value: 5.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQK-TFLTEVKVMRSL---DHPNVLKFIGVLY-----KDKKLNLLTE 406
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKSVrVQTNEDGLPlSTVREVALLKRLeafDHPNIVRLMDVCAtsrtdRETKVTLVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGgTLKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAP 484
Cdd:cd07863  88 HVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMALTP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  485 mekattkkrtlrkndrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-------GQVYADPDC-------L 550
Cdd:cd07863 167 ---------------------VVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFrrkplfcGNSEADQLGkifdligL 225
                       250       260       270
                ....*....|....*....|....*....|
gi 5031869  551 PRTLDFGLNVKLFWEKFVP------TDCPP 574
Cdd:cd07863 226 PPEDDWPRDVTLPRGAFSPrgprpvQSVVP 255
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
337-539 6.07e-16

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: 78.91  E-value: 6.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTF---LTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgTL 413
Cdd:cd06634  23 IGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWqdiIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLG-SA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLR-SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrAPMEkattkk 492
Cdd:cd06634 102 SDLLEvHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIM------APAN------ 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  493 rtlrkndrkkryTVVGNPYWMAPEM---LNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd06634 170 ------------SFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIEL 207
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
373-594 6.91e-16

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: 77.91  E-value: 6.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  373 FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPF--PWQQKVRFAKGIASGMAYLHSM--CII 448
Cdd:cd14057  39 FNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGTGVvvDQSQAVKFALDIARGMAFLHTLepLIP 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  449 HRDLNSHNCLIKLDKTvvvadfglsrliveerkrAPMEKATTKkrtLRKNDRKKRYtvvgNPYWMAPEMLNGKSYD---E 525
Cdd:cd14057 119 RHHLNSKHVMIDEDMT------------------ARINMADVK---FSFQEPGKMY----NPAWMAPEALQKKPEDinrR 173
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  526 TVDIFSFGIVLCEIIGQVYADPDCLPrtLDFGLNVKLfwEKFVPTdCPPAFFP----LAAICCRLEPESRPAF 594
Cdd:cd14057 174 SADMWSFAILLWELVTREVPFADLSN--MEIGMKIAL--EGLRVT-IPPGISPhmckLMKICMNEDPGKRPKF 241
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
334-536 7.11e-16

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: 77.74  E-value: 7.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14188   6 GKVLGKGGFAKCYEMTDLTTNKVYAAKIIphSRVSKPHQREKIdKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveeRKRAPMEkatt 490
Cdd:cd14188  86 RSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLA------ARLEPLE---- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  491 kkrtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14188 156 ----------HRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVM 191
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
364-540 7.56e-16

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: 78.60  E-value: 7.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  364 RCDEETQKTF---LT-EVKVMRSLDHPNVLKFIGVL-YKDKKLNLLTEYIeGGTLKDFLR-----SMDPFPWQQKVRFAK 433
Cdd:cd14001  39 KCDKGQRSLYqerLKeEAKILKSLNHPNIVGFRAFTkSEDGSLCLAMEYG-GKSLNDLIEeryeaGLGPFPAATILKVAL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  434 GIASGMAYLHS-MCIIHRDLNSHNCLIKLD-KTVVVADFGLSRLIVEErkrapMEKATtkkrtlrknDRKKRYtvVGNPY 511
Cdd:cd14001 118 SIARALEYLHNeKKILHGDIKSGNVLIKGDfESVKLCDFGVSLPLTEN-----LEVDS---------DPKAQY--VGTEP 181
                       170       180       190
                ....*....|....*....|....*....|
gi 5031869  512 WMAPEMLN-GKSYDETVDIFSFGIVLCEII 540
Cdd:cd14001 182 WKAKEALEeGGVITDKADIFAYGLVLWEMM 211
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
335-537 8.33e-16

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 78.01  E-value: 8.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14169   9 EKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVeNEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL---DKTVVVADFGLSRLiveerkrapmekatt 490
Cdd:cd14169  89 FDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSKI--------------- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  491 kkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFG----IVLC 537
Cdd:cd14169 154 -------EAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGvisyILLC 197
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
335-539 9.01e-16

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: 78.74  E-value: 9.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKV-THKaTGKVMVMKeLIRCDEETQKTFLTEVKVMRSL------DHPNVLKFIGVLYKDKKLNLLTEy 407
Cdd:cd14210  19 SVLGKGSFGQVVKClDHK-TGQLVAIK-IIRNKKRFHQQALVEVKILKHLndndpdDKHNIVRYKDSFIFRGHLCIVFE- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL-DKTVV-VADFGLSRLIVEerkra 483
Cdd:cd14210  96 LLSINLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQpSKSSIkVIDFGSSCFEGE----- 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  484 pmekattkkrtlrkndrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd14210 171 ------------------KVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAEL 208
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
337-540 9.63e-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: 78.08  E-value: 9.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKElirCDEE----TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN------LLTE 406
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQ---CRQElspkNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLApndlplLAME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKDFLRSMDPFPWQQK---VRFAKGIASGMAYLHSMCIIHRDLNSHNclikldktvVVADFGLSRLIveeRKRA 483
Cdd:cd14038  79 YCQGGDLRKYLNQFENCCGLREgaiLTLLSDISSALRYLHENRIIHRDLKPEN---------IVLQQGEQRLI---HKII 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  484 PMEKAttkkrtlRKNDRKKRYT-VVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14038 147 DLGYA-------KELDQGSLCTsFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECI 197
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
370-549 1.32e-15

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: 77.42  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  370 QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKK----LNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSM 445
Cdd:cd14032  44 RQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTR 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  446 C--IIHRDLNSHNCLIK-LDKTVVVADFGLSRLiveerKRAPMEKattkkrtlrkndrkkryTVVGNPYWMAPEMLNgKS 522
Cdd:cd14032 124 TppIIHRDLKCDNIFITgPTGSVKIGDLGLATL-----KRASFAK-----------------SVIGTPEFMAPEMYE-EH 180
                       170       180
                ....*....|....*....|....*..
gi 5031869  523 YDETVDIFSFGIVLCEIIGQVYADPDC 549
Cdd:cd14032 181 YDESVDVYAFGMCMLEMATSEYPYSEC 207
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
334-536 1.43e-15

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: 77.37  E-value: 1.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCD-EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14088   6 GQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDgRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGRE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCL----IKLDKtVVVADFGLSRLiveerkrapmEKA 488
Cdd:cd14088  86 VFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyynrLKNSK-IVISDFHLAKL----------ENG 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  489 TTKKRtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14088 155 LIKEP-------------CGTPEYLAPEVVGRQRYGRPVDCWAIGVIM 189
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
337-547 1.53e-15

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: 78.17  E-value: 1.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLIMARKLIhLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQ 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVRFAKGIASGMAYLHSM-CIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRapmekattkkrt 494
Cdd:cd06649  93 VLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN------------ 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  495 lrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADP 547
Cdd:cd06649 161 ----------SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIP 203
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
335-536 1.53e-15

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 77.73  E-value: 1.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKelI---RCDeeTQKtfltEVKVMRSLD-HPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14092  12 EALGDGSFSVCRKCVHKKTGQEFAVK--IvsrRLD--TSR----EVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCL---IKLDKTVVVADFGLSRLIVEerkrapMEK 487
Cdd:cd14092  84 GELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLftdEDDDAEIKIVDFGFARLKPE------NQP 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  488 ATTKKRTLrkndrkkrytvvgnPYwMAPEMLNGKS----YDETVDIFSFGIVL 536
Cdd:cd14092 158 LKTPCFTL--------------PY-AAPEVLKQALstqgYDESCDLWSLGVIL 195
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
334-604 1.66e-15

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: 76.97  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQaikVTH-KATGKVMV-MKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14153   5 GELIGKGRFGQ---VYHgRWHGEVAIrLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKtVVVADFGLSRLiveerkrAPMEKATT 490
Cdd:cd14153  82 TLYSVVRDAKVVLDVNKTRqIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK-VVITDFGLFTI-------SGVLQAGR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 KKRTLRKNDrkkrytvvGNPYWMAPEMLNGKS---------YDETVDIFSFGIVLCEIIGQVYADPDCLPRTldfglnvk 561
Cdd:cd14153 154 REDKLRIQS--------GWLCHLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAREWPFKTQPAEA-------- 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  562 LFWEkfVPTDCPPAFFPLAA---------ICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14153 218 IIWQ--VGSGMKPNLSQIGMgkeisdillFCWAYEQEERPTFSKLMEMLEKL 267
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
337-536 1.71e-15

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 77.48  E-value: 1.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTH-KATGKVMVMKELIRCD---EETQKT----FLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14096   9 IGEGAFSNVYKAVPlRNTGKPVAIKVVRKADlssDNLKGSsranILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI--------------------KLDK----- 463
Cdd:cd14096  89 DGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkadddetKVDEgefip 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  464 --------TVVVADFGLSRLIVEERKRAPmekattkkrtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14096 169 gvggggigIVKLADFGLSKQVWDSNTKTP----------------------CGTVGYTAPEVVKDERYSKKVDMWALGCV 226

                .
gi 5031869  536 L 536
Cdd:cd14096 227 L 227
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
335-536 2.20e-15

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 76.68  E-value: 2.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVM-KELIRCDEETQktFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14082   9 EVLGSGQFGIVYGGKHRKTGRdvaIKVIdKLRFPTKQESQ--LRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK---TVVVADFGLSRLIVEerkrapme 486
Cdd:cd14082  87 DMLEMILSSEKGRLPERITKFlVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGE-------- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  487 kattkkRTLRKndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14082 159 ------KSFRR-------SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 195
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
337-540 2.53e-15

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: 76.72  E-value: 2.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeliRCDEETQKT------FLTEVKVMRSLDHPNVLKFIGV-----LYKDKKLNLLT 405
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIK---KCRQELSPSdknrerWCLEVQIMKKLNHPNVVSARDVppeleKLSPNDLPLLA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 -EYIEGGTLKDFLRSMDPFPW--QQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKL--DKTVV-VADFGLSRLIve 478
Cdd:cd13989  78 mEYCSGGDLRKVLNQPENCCGlkESEVRtLLSDISSAISYLHENRIIHRDLKPENIVLQQggGRVIYkLIDLGYAKEL-- 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  479 erkrapmekattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd13989 156 -------------------DQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECI 198
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
332-543 2.61e-15

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: 77.22  E-value: 2.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKELI-RCDEETQKtfltEVKVMRSLD-HPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14180   9 LEEPALGEGSFSVCRKCRHRQSGQEYAVKIISrRMEANTQR----EVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD---KTVVVADFGLSRLiveerKRAPME 486
Cdd:cd14180  85 GGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsdgAVLKVIDFGFARL-----RPQGSR 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  487 KATTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQV 543
Cdd:cd14180 160 PLQTPCFTLQ---------------YAAPELFSNQGYDESCDLWSLGVILYTMLsGQV 202
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
334-536 2.68e-15

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: 76.18  E-value: 2.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFG---QAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYK-DKKLNLLTEYIE 409
Cdd:cd14163   5 GKTIGEGTYSkvkEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESaDGKIYLVMELAE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKlDKTVVVADFGLSRLiveerkrapmekat 489
Cdd:cd14163  85 DGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQ-GFTLKLTDFGFAKQ-------------- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  490 tkkrtLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETV-DIFSFGIVL 536
Cdd:cd14163 150 -----LPKGGRELSQTFCGSTAYAAPEVLQGVPHDSRKgDIWSMGVVL 192
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
372-592 2.74e-15

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: 76.50  E-value: 2.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  372 TFLTEVKVMRSLDHPNVLKFIGVLYKdkKLNLLTEYIEGGTLKDFL----RSMDPFPWQQKVRFAKGIASGMAYLHSMCI 447
Cdd:cd14000  56 LLRQELTVLSHLHHPSIVYLLGIGIH--PLMLVLELAPLGSLDHLLqqdsRSFASLGRTLQQRIALQVADGLRYLHSAMI 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  448 IHRDLNSHNCLI-KLDKT----VVVADFGLSRliveerKRAPMEKATTKkrtlrkndrkkrytvvGNPYWMAPEMLNGKS 522
Cdd:cd14000 134 IYRDLKSHNVLVwTLYPNsaiiIKIADYGISR------QCCRMGAKGSE----------------GTPGFRAPEIARGNV 191
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  523 -YDETVDIFSFGIVLCEII--GQVYADPDCLPRTLDF--GLNVKLFWEKFVPtdcPPAFFPLAAICCRLEPESRP 592
Cdd:cd14000 192 iYNEKVDVFSFGMLLYEILsgGAPMVGHLKFPNEFDIhgGLRPPLKQYECAP---WPEVEVLMKKCWKENPQQRP 263
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
376-545 2.76e-15

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: 76.62  E-value: 2.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVLYK----DKKLNLLTEYIEGGTLKDFLRSmDPFPWQQKVRFAKGIASGMAYLHS------- 444
Cdd:cd14141  39 EIYSLPGMKHENILQFIGAEKRgtnlDVDLWLITAFHEKGSLTDYLKA-NVVSWNELCHIAQTMARGLAYLHEdipglkd 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  445 ---MCIIHRDLNSHNCLIKLDKTVVVADFGLSrLIVEERKRApmekattkkrtlrkndrKKRYTVVGNPYWMAPEMLNG- 520
Cdd:cd14141 118 ghkPAIAHRDIKSKNVLLKNNLTACIADFGLA-LKFEAGKSA-----------------GDTHGQVGTRRYMAPEVLEGa 179
                       170       180
                ....*....|....*....|....*....
gi 5031869  521 ----KSYDETVDIFSFGIVLCEIIGQVYA 545
Cdd:cd14141 180 infqRDAFLRIDMYAMGLVLWELASRCTA 208
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
335-597 3.05e-15

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: 76.60  E-value: 3.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIK-----VTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRS-LDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd05091  12 EELGEDRFGKVYKghlfgTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSrLQHPNIVCLLGVVTKEQPMSMIFSYC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDP----------------FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL 472
Cdd:cd05091  92 SHGDLHEFLVMRSPhsdvgstdddktvkstLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  473 SRLIVEerkrapmekattkkrtlrkndrKKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEIIGqvYA-DP 547
Cdd:cd05091 172 FREVYA----------------------ADYYKLMGNSLlpirWMSPEAIMYGKFSIDSDIWSYGVVLWEVFS--YGlQP 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  548 DCLPRTLDFglnVKLFWEKFV---PTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05091 228 YCGYSNQDV---IEMIRNRQVlpcPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
337-591 3.14e-15

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: 75.82  E-value: 3.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLT-EYIEGGTLK 414
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALK-FVPKPSTKLKDFLREYNISLELsVHPHIIKTYDVAFETEDYYVFAqEYAPYGDLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIkLDKT---VVVADFGLSRliveerkrapmEKATTK 491
Cdd:cd13987  80 SIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLL-FDKDcrrVKLCDFGLTR-----------RVGSTV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  492 KRtlrkndrkKRYTvvgNPYwMAPEMLNGK-----SYDETVDIFSFGIVL-CEIIGQV---YADPDClPRTLDFglnvkL 562
Cdd:cd13987 148 KR--------VSGT---IPY-TAPEVCEAKknegfVVDPSIDVWAFGVLLfCCLTGNFpweKADSDD-QFYEEF-----V 209
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031869  563 FWEKFVPTDCPPA---FFPLAAICCR----LEPESR 591
Cdd:cd13987 210 RWQKRKNTAVPSQwrrFTPKALRMFKkllaPEPERR 245
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
337-540 3.70e-15

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: 76.20  E-value: 3.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgTLKD 415
Cdd:cd07871  13 LGEGTYATVFKGRSKLTENLVALKEIrLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDS-DLKQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPMEKATTKKRT 494
Cdd:cd07871  92 YLDNCGNLMSMHNVKiFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLAR-----AKSVPTKTYSNEVVT 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  495 LrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd07871 167 L---------------WYRPPDVLLGSTeYSTPIDMWGVGCILYEMA 198
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
331-535 3.71e-15

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 75.85  E-value: 3.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIR------CDEEtqktFLTEVKV-MRSLDHPNVLKFIGVLYKDKKLNL 403
Cdd:cd14106  10 TVESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrrgqdCRNE----ILHEIAVlELCKDCPRVVNLHEVYETRSELIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKT---VVVADFGLSRLIveer 480
Cdd:cd14106  86 ILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVI---- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  481 krapmekattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14106 162 -----------------GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVL 199
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
336-540 3.77e-15

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: 75.91  E-value: 3.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd06624  15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSmdpfPW------QQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVV-VADFGlsrliveerkrapmek 487
Cdd:cd06624  95 LLRS----KWgplkdnENTIGYyTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVkISDFG---------------- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  488 atTKKRTLRKNDRKKRYTvvGNPYWMAPEMLNG--KSYDETVDIFSFGivlCEII 540
Cdd:cd06624 155 --TSKRLAGINPCTETFT--GTLQYMAPEVIDKgqRGYGPPADIWSLG---CTII 202
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
336-542 3.84e-15

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 76.66  E-value: 3.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL----IRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDK-KLNLLTEYIEG 410
Cdd:cd05587   3 VLGKGSFGKVMLAERKGTDELYAIKILkkdvIIQDDDVECT-MVEKRVLALSGKPPFLTQLHSCFQTMdRLYFVMEYVNG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKATT 490
Cdd:cd05587  82 GDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC-------KEGIFGGKTT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  491 KkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ 542
Cdd:cd05587 155 R-------------TFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLaGQ 194
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
335-540 4.02e-15

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 77.41  E-value: 4.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCD--EETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05627   8 KVIGRGAFGEVRLVQKKDTGHIYAMKILRKADmlEKEQVAHIrAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKAT-- 489
Cdd:cd05627  88 DMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLThn 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031869  490 -------------TKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05627 168 ppsdfsfqnmnskRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 231
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
337-540 4.18e-15

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 76.16  E-value: 4.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI-RCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLY--KDKKLNLLTEYIEGgT 412
Cdd:cd07831   7 IGEGTFSEVLKAQSRKTGKYYAIKCMKkHFKSLEQVNNLREIQALRRLsPHPNILRLIEVLFdrKTGRLALVFELMDM-N 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRS-MDPFPwQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKlDKTVVVADFGLSRLIveerkrapmekatt 490
Cdd:cd07831  86 LYELIKGrKRPLP-EKRVKnYMYQLLKSLDHMHRNGIFHRDIKPENILIK-DDILKLADFGSCRGI-------------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  491 kkrtlrknDRKKRYTVVGNPYWM-APE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07831 150 --------YSKPPYTEYISTRWYrAPEcLLTDGYYGPKMDIWAVGCVFFEIL 193
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
335-535 4.59e-15

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: 76.24  E-value: 4.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14168  16 EVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIeNEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSRLiveERKRAPMEkatt 490
Cdd:cd14168  96 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKM---EGKGDVMS---- 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031869  491 kkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14168 169 --------------TACGTPGYVAPEVLAQKPYSKAVDCWSIGVI 199
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
337-540 4.82e-15

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 76.94  E-value: 4.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   337 LGKGFFGQAIKVTHKATG-KVMVMKELIRCDEETQKTF---LTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:PTZ00426  38 LGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKQVdhvFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlIVEERKrapmekattkk 492
Cdd:PTZ00426 118 FFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK-VVDTRT----------- 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 5031869   493 rtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:PTZ00426 186 -----------YTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEIL 222
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
336-533 5.09e-15

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: 76.67  E-value: 5.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFG---QAIKVTHKATGKVMVMKEL-----IRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd05584   3 VLGKGGYGkvfQVRKTTGSDKGKIFAMKVLkkasiVRNQKDTAHT-KAERNILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmek 487
Cdd:cd05584  82 LSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIH--------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  488 attkkrtlrknDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFG 533
Cdd:cd05584 153 -----------DGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLG 187
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
335-587 5.87e-15

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 76.97  E-value: 5.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELiRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05626   7 KTLGIGAFGEVCLACKVDTHALYAMKTL-RKKDVLNRNQVAHVKAERDIlaeaDNEWVVKLYYSFQDKDNLYFVMDYIPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS---RLIVEER------- 480
Cdd:cd05626  86 GDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCtgfRWTHNSKyyqkgsh 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 -KRAPMEKA----------------TTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQ 542
Cdd:cd05626 166 iRQDSMEPSdlwddvsncrcgdrlkTLEQRATKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEmLVGQ 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  543 vyaDPDCLPRTLDFGLNVkLFWEK--FVPTD---CPPAFFPLAAICCRLE 587
Cdd:cd05626 246 ---PPFLAPTPTETQLKV-INWENtlHIPPQvklSPEAVDLITKLCCSAE 291
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
370-549 6.07e-15

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: 75.86  E-value: 6.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  370 QKTFLTEVKVMRSLDHPNVLKFI----GVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSM 445
Cdd:cd14030  68 RQRFKEEAGMLKGLQHPNIVRFYdsweSTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTR 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  446 C--IIHRDLNSHNCLIK-LDKTVVVADFGLSRLiveerKRAPMEKAttkkrtlrkndrkkrytVVGNPYWMAPEMLNGKs 522
Cdd:cd14030 148 TppIIHRDLKCDNIFITgPTGSVKIGDLGLATL-----KRASFAKS-----------------VIGTPEFMAPEMYEEK- 204
                       170       180
                ....*....|....*....|....*..
gi 5031869  523 YDETVDIFSFGIVLCEIIGQVYADPDC 549
Cdd:cd14030 205 YDESVDVYAFGMCMLEMATSEYPYSEC 231
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
335-540 6.25e-15

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 75.64  E-value: 6.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQKTFLTEVKVMRSLDH-PNVLKFIGVLYKDKK----LNLLTEY 407
Cdd:cd07837   7 EKIGEGTYGKVYKARDKNTGKLVALKKtrLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLDVEHVEENgkplLYLVFEY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGgTLKDFLRSM-----DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVV-VADFGLSRLIVeerk 481
Cdd:cd07837  87 LDT-DLKKFIDSYgrgphNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLkIADLGLGRAFT---- 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  482 rAPMEKATTKKRTLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd07837 162 -IPIKSYTHEIVTL---------------WYRAPEVLLGSThYSTPVDMWSVGCIFAEMS 205
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
348-551 6.30e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.84  E-value: 6.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   348 VTHKATGKVMVMKELIRCDEETQK-----TFLTEVKVMRSLDHPNVLKFIGVL-YKDKKLNLLTEYieGGTLKDFL-RSM 420
Cdd:PHA03209  74 LTPGSEGRVFVATKPGQPDPVVLKigqkgTTLIEAMLLQNVNHPSVIRMKDTLvSGAITCMVLPHY--SSDLYTYLtKRS 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   421 DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrAPMEkattkkrtlrkndr 500
Cdd:PHA03209 152 RPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVV----APAF-------------- 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   501 kkrYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYADPDCLP 551
Cdd:PHA03209 214 ---LGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAypsTIFEDPPSTP 264
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
336-540 7.17e-15

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: 76.07  E-value: 7.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL----IRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIrkahIVSRSEVTHT-LAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapmekattk 491
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKL---------------- 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  492 krTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05585 144 --NMKDDDKTN--TFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEML 188
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
12-68 8.14e-15

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 68.90  E-value: 8.14e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869     12 CPGCGDHIAPSQIwYRTVNETWHGSCFRCSECQDSLTNW-YYEKDGKLYCPKDYWGKF 68
Cdd:pfam00412   1 CAGCNRPIYDREL-VRALGKVWHPECFRCAVCGKPLTTGdFYEKDGKLYCKHDYYKLF 57
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
337-541 8.89e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 75.48  E-value: 8.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLyKDKKLN---LLTEYIEG 410
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKK-VRMDNERDGipiSSLREITLLLNLRHPNIVELKEVV-VGKHLDsifLVMEYCEQ 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 gTLKDFLRSM-DPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKlDKTVV-VADFGLSRLIveERKRAPMeka 488
Cdd:cd07845  93 -DLASLLDNMpTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLT-DKGCLkIADFGLARTY--GLPAKPM--- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  489 TTKKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEIIG 541
Cdd:cd07845 166 TPKVVTL---------------WYRAPELLLGcTTYTTAIDMWAVGCILAELLA 204
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
334-535 9.24e-15

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 74.99  E-value: 9.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLT------EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY 407
Cdd:cd14196  10 GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSreeierEVSILRQVLHPNIITLHDVYENRTDVVLILEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIkLDKTVVVA-----DFGLSRLIveerkr 482
Cdd:cd14196  90 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIPIPhikliDFGLAHEI------ 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  483 apmekattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14196 163 ---------------EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 200
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
334-536 1.07e-14

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: 74.58  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQK-TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14189   6 GRLLGKGGFARCYEMTDLATNKTYAVKVIphSRVAKPHQReKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRS----MDPfpwqqKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrAPM 485
Cdd:cd14189  86 KSLAHIWKArhtlLEP-----EVRyYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLA---------ARL 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  486 EKATTKKRtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14189 152 EPPEQRKK-----------TICGTPNYLAPEVLLRQGHGPESDVWSLGCVM 191
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
340-540 1.07e-14

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 74.95  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  340 GFFGQAIKVTHKATGKVMVMKElIRCDEETQK---TFLTEVKVMRSLDHPNVL--KFIGVLYKDKKLNLLTEYIEGgTLK 414
Cdd:cd07843  16 GTYGVVYRARDKKTGEIVALKK-LKMEKEKEGfpiTSLREINILLKLQHPNIVtvKEVVVGSNLDKIYMVMEYVEH-DLK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPMEKATTKKR 493
Cdd:cd07843  94 SLMETMKQPFLQSEVKcLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAR-----EYGSPLKPYTQLVV 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  494 TLrkndrkkrytvvgnpYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07843 169 TL---------------WYRAPELLLGaKEYSTAIDMWSVGCIFAELL 201
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
334-597 1.27e-14

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 75.42  E-value: 1.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIK-----VTHKATGKVMVMKELIRCDEETQ-KTFLTEVKVMRSLDHP-NVLKFIGVLYKDK-KLNLLT 405
Cdd:cd14207  12 GKSLGRGAFGKVVQasafgIKKSPTCRVVAVKMLKEGATASEyKALMTELKILIHIGHHlNVVNLLGACTKSGgPLMVIV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRS---------------------MDPFPWQQK------------------------------------ 428
Cdd:cd14207  92 EYCKYGNLSNYLKSkrdffvtnkdtslqeelikekKEAEPTGGKkkrlesvtssesfassgfqedkslsdveeeeedsgd 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  429 -----------VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekattKKRTLRK 497
Cdd:cd14207 172 fykrpltmedlISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYK------------NPDYVRK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  498 NDRKKRYTvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIG-------QVYADPDCLPRtLDFGLNVKlfwekfVPT 570
Cdd:cd14207 240 GDARLPLK------WMAPESIFDKIYSTKSDVWSYGVLLWEIFSlgaspypGVQIDEDFCSK-LKEGIRMR------APE 306
                       330       340
                ....*....|....*....|....*..
gi 5031869  571 DCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd14207 307 FATSEIYQIMLDCWQGDPNERPRFSEL 333
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
348-604 1.40e-14

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: 76.22  E-value: 1.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  348 VTHKATGKVMVMKELircdEETQKTFLTEVK-------VMRSL-DHPnvlkfigVLYKDKKL----NLLTE-YIEGGTLK 414
Cdd:cd05105 169 LSFENKGDYMDMKQA----DTTQYVPMLEIKeaskysdIQRSNyDRP-------ASYKGSNDsevkNLLSDdGSEGLTTL 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRsmdpFPWQqkvrfakgIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrapmekattkkrt 494
Cdd:cd05105 238 DLLS----FTYQ--------VARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHD--------------- 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lrkndrkKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEII---GQVYadPDCLPRTlDFGLNVKLFWEKF 567
Cdd:cd05105 291 -------SNYVSKGSTFlpvkWMAPESIFDNLYTTLSDVWSYGILLWEIFslgGTPY--PGMIVDS-TFYNKIKSGYRMA 360
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031869  568 VPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEAL 604
Cdd:cd05105 361 KPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
383-545 1.40e-14

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: 74.68  E-value: 1.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  383 LDHPNVLKFIGVLYKDKKLN----LLTEYIEGGTLKDFLRSmDPFPWQQKVRFAKGIASGMAYLHS---MC--------I 447
Cdd:cd14140  46 MKHENLLQFIAAEKRGSNLEmelwLITAFHDKGSLTDYLKG-NIVSWNELCHIAETMARGLSYLHEdvpRCkgeghkpaI 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  448 IHRDLNSHNCLIKLDKTVVVADFGLSrlIVEERKRAPMEKattkkrtlrkndrkkrYTVVGNPYWMAPEMLNG-----KS 522
Cdd:cd14140 125 AHRDFKSKNVLLKNDLTAVLADFGLA--VRFEPGKPPGDT----------------HGQVGTRRYMAPEVLEGainfqRD 186
                       170       180
                ....*....|....*....|...
gi 5031869  523 YDETVDIFSFGIVLCEIIGQVYA 545
Cdd:cd14140 187 SFLRIDMYAMGLVLWELVSRCKA 209
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
376-542 1.58e-14

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: 74.62  E-value: 1.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVL--YKDKKLNLLTEYIEGGTLKDfLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLN 453
Cdd:cd14199  75 EIAILKKLDHPNVVKLVEVLddPSEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVK 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  454 SHNCLIKLDKTVVVADFGLSrliveerkrapmekattkkRTLRKNDRKKRYTvVGNPYWMAPEMLNG--KSYD-ETVDIF 530
Cdd:cd14199 154 PSNLLVGEDGHIKIADFGVS-------------------NEFEGSDALLTNT-VGTPAFMAPETLSEtrKIFSgKALDVW 213
                       170
                ....*....|...
gi 5031869  531 SFGIVL-CEIIGQ 542
Cdd:cd14199 214 AMGVTLyCFVFGQ 226
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
328-597 1.83e-14

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: 75.02  E-value: 1.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  328 PCDLIH-GEVLGKGFFGQAIKVT----HKA----TGKVMVMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYK 397
Cdd:cd05102   5 PRDRLRlGKVLGHGAFGKVVEASafgiDKSssceTVAVKMLKEGATASE--HKALMSELKILIHIgNHLNVVNLLGACTK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  398 -DKKLNLLTEYIEGGTLKDFLRSMDPF--PWQQK----------------------------VRFAKG------------ 434
Cdd:cd05102  83 pNGPLMVIVEFCKYGNLSNFLRAKREGfsPYRERsprtrsqvrsmveavradrrsrqgsdrvASFTEStsstnqprqevd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  435 ------------------IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEE----RK---RAPMEkat 489
Cdd:cd05102 163 dlwqspltmedlicysfqVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpdyvRKgsaRLPLK--- 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  490 tkkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVP 569
Cdd:cd05102 240 ----------------------WMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLKDGTRMRAP 297
                       330       340
                ....*....|....*....|....*...
gi 5031869  570 TDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05102 298 EYATPEIYRIMLSCWHGDPKERPTFSDL 325
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
334-535 1.96e-14

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: 73.88  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIR----------CDEETQKtfltEVKVMRSLDHPNVLKFIGVLYKDKKLNL 403
Cdd:cd14195  10 GEELGSGQFAIVRKCREKGTGKEYAAKFIKKrrlsssrrgvSREEIER----EVNILREIQHPNIITLHDIFENKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIkLDKTV-----VVADFGLSRLIve 478
Cdd:cd14195  86 ILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIML-LDKNVpnpriKLIDFGIAHKI-- 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  479 erkrapmeKATTKKRtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14195 163 --------EAGNEFK-----------NIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 200
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
334-536 2.11e-14

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: 73.36  E-value: 2.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQA-IKVTHKATGKVMV-MKELIRCDEE-TQKTFLTEVKVMRSLDHPN-VLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14164   5 GTTIGEGSFSKVkLATSQKYCCKVAIkIVDRRRASPDfVQKFLPRELSILRRVNHPNiVQMFECIEVANGRLYIVMEAAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKgIASGMAYLHSMCIIHRDLNSHNCLIKLD-KTVVVADFGLSRLIveerkRAPMEKA 488
Cdd:cd14164  85 TDLLQKIQEVHHIPKDLARDMFAQ-MVGAVNYLHDMNIVHRDLKCENILLSADdRKIKIADFGFARFV-----EDYPELS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  489 TtkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVL 536
Cdd:cd14164 159 T---------------TFCGSRAYTPPEVILGTPYDpKKYDVWSLGVVL 192
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
336-539 2.24e-14

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: 74.07  E-value: 2.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLY---------KDKK-LN 402
Cdd:cd07864  14 IIGEGTYGQVYKAKDKDTGELVALKK-VRLDNEKEGfpiTAIREIKILRQLNHRSVVNLKEIVTdkqdaldfkKDKGaFY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  403 LLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKR 482
Cdd:cd07864  93 LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYNSEESR 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  483 ApmekATTKKRTLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEI 539
Cdd:cd07864 173 P----YTNKVITL---------------WYRPPELLLGEErYGPAIDVWSCGCILGEL 211
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
376-543 2.52e-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: 73.55  E-value: 2.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVL--YKDKKLNLLTEYIEGGTLKDfLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLN 453
Cdd:cd14118  64 EIAILKKLDHPNVVKLVEVLddPNEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIK 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  454 SHNCLIKLDKTVVVADFGLSrlivEERKRAPMEKATTkkrtlrkndrkkrytvVGNPYWMAPEML--NGKSYD-ETVDIF 530
Cdd:cd14118 143 PSNLLLGDDGHVKIADFGVS----NEFEGDDALLSST----------------AGTPAFMAPEALseSRKKFSgKALDIW 202
                       170
                ....*....|....
gi 5031869  531 SFGIVL-CEIIGQV 543
Cdd:cd14118 203 AMGVTLyCFVFGRC 216
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
336-540 2.74e-14

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: 74.26  E-value: 2.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCD----EETQkTFLTE---VKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd05589   6 VLGRGHFGKVLLAEYKPTGELFAIKALKKGDiiarDEVE-SLMCEkriFETVNSARHPFLVNLFACFQTPEHVCFVMEYA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSmDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmeka 488
Cdd:cd05589  85 AGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--------------- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  489 ttkKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05589 149 ---KEGMGFGDRTS--TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEML 195
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
330-597 3.39e-14

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 75.05  E-value: 3.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVT------HKATGKVMV--MKELIRCDEetQKTFLTEVKVMRSLD-HPNVLKFIGVLYKDKK 400
Cdd:cd05107  38 NLVLGRTLGSGAFGRVVEATahglshSQSTMKVAVkmLKSTARSSE--KQALMSELKIMSHLGpHLNIVNLLGACTKGGP 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  401 LNLLTEYIEGGTLKDFLRS--------------------------------------------MD--------------- 421
Cdd:cd05107 116 IYIITEYCRYGDLVDYLHRnkhtflqyyldknrddgslisggstplsqrkshvslgsesdggyMDmskdesadyvpmqdm 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  422 ------------PF--PWQQK-------------------------VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD 462
Cdd:cd05107 196 kgtvkyadiessNYesPYDQYlpsapertrrdtlinespalsymdlVGFSYQVANGMEFLASKNCVHRDLAARNVLICEG 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  463 KTVVVADFGLSRLIVeerkrapmekattkkrtlrkndRKKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCE 538
Cdd:cd05107 276 KLVKICDFGLARDIM----------------------RDSNYISKGSTFlplkWMAPESIFNNLYTTLSDVWSFGILLWE 333
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  539 II---GQVYADpdcLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05107 334 IFtlgGTPYPE---LPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQL 392
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
327-546 3.48e-14

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 74.65  E-value: 3.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  327 RPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMK-----ELIRcdEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKL 401
Cdd:cd05621  50 KAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKllskfEMIK--RSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  402 NLLTEYIEGGTLKDFLRSMD-PFPWQQkvRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrliveer 480
Cdd:cd05621 128 YMVMEYMPGGDLVNLMSNYDvPEKWAK--FYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFG--------- 196
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  481 krapmekattkkrTLRKNDRKKRY---TVVGNPYWMAPEMLNGKS----YDETVDIFSFGIVLCE-IIGQV--YAD 546
Cdd:cd05621 197 -------------TCMKMDETGMVhcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEmLVGDTpfYAD 259
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
337-540 3.66e-14

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: 74.13  E-value: 3.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEETQKTFlTEVKVMRSL-DHPNVLKFIGVLY--KDKKLNLLTEYIE- 409
Cdd:cd07852  15 LGKGAYGIVWKAIDKKTGEVVALKKIfdaFRNATDAQRTF-REIMFLQELnDHPNIIKLLNVIRaeNDKDIYLVFEYMEt 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 -------GGTLKDflrsmdpfpwqQKVRFakgIA----SGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVE 478
Cdd:cd07852  94 dlhavirANILED-----------IHKQY---IMyqllKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQ 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  479 ERKRAPMEKATtkkrtlrkndrkkRYtvVGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEII 540
Cdd:cd07852 160 LEEDDENPVLT-------------DY--VATRWYRAPEILLGsTRYTKGVDMWSVGCILGEML 207
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
11-63 4.26e-14

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 67.02  E-value: 4.26e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 5031869      11 RCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTN-WYYEKDGKLYCPKD 63
Cdd:smart00132   1 KCAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLSGdTFFEKDGKLYCKDC 54
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
335-540 4.41e-14

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: 73.79  E-value: 4.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTfLTEVKVMR-SLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLyavkVLKKDVILQDDDVECT-MTEKRILSlARNHPFLTQLYCCFQTPDRLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKAT 489
Cdd:cd05590  80 GGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC-------KEGIFNGKT 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  490 TKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05590 153 TS-------------TFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEML 190
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
335-540 4.51e-14

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: 73.87  E-value: 4.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRC--DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN------LLTE 406
Cdd:cd07851  21 SPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPfqSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLEdfqdvyLVTH 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIeGGTLKDFLRsmdpfpwQQK-----VRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveer 480
Cdd:cd07851 101 LM-GADLNNIVK-------CQKlsddhIQFlVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARH----- 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  481 krapmekaTTKKRTlrkndrkkryTVVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07851 168 --------TDDEMT----------GYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELL 210
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
338-593 5.11e-14

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: 72.55  E-value: 5.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  338 GKGFFGQAIKVTHKATGKvMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgtlKDFL 417
Cdd:cd14111  12 ARGRFGVIRRCRENATGK-NFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSG---KELL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  418 RSM-DPFPWQQK--VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapmekaTTKKRT 494
Cdd:cd14111  88 HSLiDRFRYSEDdvVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQ--------------SFNPLS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 LRKNDRKkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGiVLCEII--GQV-YADPDclPRTLDfglnVKLFWEKFVPTD 571
Cdd:cd14111 154 LRQLGRR-----TGTLEYMAPEMVKGEPVGPPADIWSIG-VLTYIMlsGRSpFEDQD--PQETE----AKILVAKFDAFK 221
                       250       260
                ....*....|....*....|....*.
gi 5031869  572 CPPAFFPLAAICCR----LEPESRPA 593
Cdd:cd14111 222 LYPNVSQSASLFLKkvlsSYPWSRPT 247
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
337-471 5.64e-14

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: 69.39  E-value: 5.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLD--HPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  415 DFL--RSMDPfpwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFG 471
Cdd:cd13968  81 AYTqeEELDE---KDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
334-597 6.65e-14

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: 73.73  E-value: 6.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGK--------VMVMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLL 404
Cdd:cd05106  43 GKTLGAGAFGKVVEATAFGLGKednvlrvaVKMLKASAHTDE--REALMSELKILSHLgQHKNIVNLLGACTHGGPVLVI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLR-------------------SMD-------------------------------------------- 421
Cdd:cd05106 121 TEYCCYGDLLNFLRkkaetflnfvmalpeisetSSDyknitlekkyirsdsgfssqgsdtyvemrpvsssssqssdskde 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  422 -------PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeerkrapmekattkkrt 494
Cdd:cd05106 201 edtedswPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIM----------------- 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 lrkNDrkKRYTVVGNPY----WMAPEMLNGKSYDETVDIFSFGIVLCEIIG---QVYadPDCLPRTLDFGLnVKLFWEKF 567
Cdd:cd05106 264 ---ND--SNYVVKGNARlpvkWMAPESIFDCVYTVQSDVWSYGILLWEIFSlgkSPY--PGILVNSKFYKM-VKRGYQMS 335
                       330       340       350
                ....*....|....*....|....*....|
gi 5031869  568 VPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05106 336 RPDFAPPEIYSIMKMCWNLEPTERPTFSQI 365
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
335-547 6.96e-14

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: 72.80  E-value: 6.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEE--TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEggt 412
Cdd:cd07869  11 EKLGEGSYATVYKGKSKVNGKLVALK-VIRLQEEegTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVH--- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 lKDFLRSMDPFP---WQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPMEKA 488
Cdd:cd07869  87 -TDLCQYMDKHPgglHPENVKlFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR-----AKSVPSHTY 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  489 TTKKRTLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEIIGQVYADP 547
Cdd:cd07869 161 SNEVVTL---------------WYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAFP 205
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
332-536 7.65e-14

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: 72.76  E-value: 7.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTevkvMRSLDHPNVLKFIGV---LYKDKK-LNLLTEY 407
Cdd:cd14170   5 VTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELH----WRASQCPHIVRIVDVyenLYAGRKcLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLkdFLRSMD----PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSrliveer 480
Cdd:cd14170  81 LDGGEL--FSRIQDrgdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYtskRPNAILKLTDFGFA------- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  481 krapmeKATTKKRTLRkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14170 152 ------KETTSHNSLT--------TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIM 193
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
367-605 7.98e-14

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: 72.05  E-value: 7.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  367 EETQKTFLTevkvMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMD-PFPWQQKVRFAKGIASGMAYLHSM 445
Cdd:cd14043  41 PSTKNVFSK----LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDmKLDWMFKSSLLLDLIKGMRYLHHR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  446 CIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveERKRAPMEKATTKKRtlrkndrkkrytvvgnpYWMAPEMLNGKSYDE 525
Cdd:cd14043 117 GIVHGRLKSRNCVVDGRFVLKITDYGYNEIL--EAQNLPLPEPAPEEL-----------------LWTAPELLRDPRLER 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  526 TV----DIFSFGIVLCEIIgqVYADPDCLprtldFGLNVKLFWEKFV--PTDCPPAF----FPLAAI-----CCRLEPES 590
Cdd:cd14043 178 RGtfpgDVFSFAIIMQEVI--VRGAPYCM-----LGLSPEEIIEKVRspPPLCRPSVsmdqAPLECIqlmkqCWSEAPER 250
                       250
                ....*....|....*
gi 5031869  591 RPAFSKLEDSFEALS 605
Cdd:cd14043 251 RPTFDQIFDQFKSIN 265
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
334-536 9.32e-14

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: 72.06  E-value: 9.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14090   7 GELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLhQCQGHPNILQLIEYFEDDERFYLVFEKMRGGP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI-KLDKT--VVVADFGLSRLIVEERKRapMEKAT 489
Cdd:cd14090  87 LLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCeSMDKVspVKICDFDLGSGIKLSSTS--MTPVT 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 TKKRTlrkndrkkryTVVGNPYWMAPEMLN-----GKSYDETVDIFSFGIVL 536
Cdd:cd14090 165 TPELL----------TPVGSAEYMAPEVVDafvgeALSYDKRCDLWSLGVIL 206
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
335-539 1.00e-13

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: 72.33  E-value: 1.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK--TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgT 412
Cdd:cd07872  12 EKLGEGTYATVFKGRSKLTENLVALKE-IRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDK-D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPMEKATTK 491
Cdd:cd07872  90 LKQYMDDCGNIMSMHNVKiFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR-----AKSVPTKTYSNE 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  492 KRTLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEI 539
Cdd:cd07872 165 VVTL---------------WYRPPDVLLGSSeYSTQIDMWGVGCIFFEM 198
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
335-546 1.03e-13

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 73.50  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05622  79 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEmikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMD-PFPWqqkVRFAKG-IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGlsrliveerkrapmekaT 489
Cdd:cd05622 159 DLVNLMSNYDvPEKW---ARFYTAeVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-----------------T 218
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031869  490 TKKrtLRKNDRKKRYTVVGNPYWMAPEMLNGKS----YDETVDIFSFGIVLCE-IIGQV--YAD 546
Cdd:cd05622 219 CMK--MNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEmLVGDTpfYAD 280
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
376-542 1.09e-13

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: 71.90  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVL--YKDKKLNLLTEYIEGGTLKDfLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLN 453
Cdd:cd14200  73 EIAILKKLDHVNIVKLIEVLddPAEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIK 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  454 SHNCLIKLDKTVVVADFGLSrliveerkrapmekattkkRTLRKNDRKKRYTvVGNPYWMAPEML--NGKSYD-ETVDIF 530
Cdd:cd14200 152 PSNLLLGDDGHVKIADFGVS-------------------NQFEGNDALLSST-AGTPAFMAPETLsdSGQSFSgKALDVW 211
                       170
                ....*....|...
gi 5031869  531 SFGIVL-CEIIGQ 542
Cdd:cd14200 212 AMGVTLyCFVYGK 224
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
313-541 1.40e-13

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: 72.76  E-value: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  313 ESLRCSSSYSQQIFrpcDLIhgEVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTFLTEVKVMRSLDHPNV 388
Cdd:cd05618   9 ESGKASSSLGLQDF---DLL--RVIGRGSYAKVLLVRLKKTERIYAMKvvkkELVNDDEDIDWVQTEKHVFEQASNHPFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  389 LKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVA 468
Cdd:cd05618  84 VGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLT 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  469 DFGLSrliveerkrapmekattkKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIG 541
Cdd:cd05618 164 DYGMC------------------KEGLRPGDTTS--TFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMA 216
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
336-605 1.56e-13

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 74.11  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETqktfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:PLN00113 697 VISRGKKGASYKGKSIKNGMQFVVKEINDVNSIP----SSEIADMGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSE 772
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   416 FLRSMDpfpWQQKVRFAKGIASGMAYLHSMCiihrdlnshncliklDKTVVVADFGLSRLIVEERKRAPMEKATTkkrTL 495
Cdd:PLN00113 773 VLRNLS---WERRRKIAIGIAKALRFLHCRC---------------SPAVVVGNLSPEKIIIDGKDEPHLRLSLP---GL 831
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   496 RKNDRKKRYTVVgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQVYADPdclprtlDFGLNVKLF-WEKFVPTDC- 572
Cdd:PLN00113 832 LCTDTKCFISSA----YVAPETRETKDITEKSDIYGFGLILIELLtGKSPADA-------EFGVHGSIVeWARYCYSDCh 900
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5031869   573 -----PPAFFP--------------LAAICCRLEPESRPAFSKLEDSFEALS 605
Cdd:PLN00113 901 ldmwiDPSIRGdvsvnqneivevmnLALHCTATDPTARPCANDVLKTLESAS 952
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
337-479 2.07e-13

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: 70.79  E-value: 2.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAI--KVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05087   5 IGHGWFGKVFlgEVNSGLSSTQVVVKELkASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGDL 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  414 KDFLRS------MDPFPWQQKvRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEE 479
Cdd:cd05087  85 KGYLRScraaesMAPDPLTLQ-RMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKE 155
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
335-540 2.14e-13

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 72.38  E-value: 2.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd05628   7 KVIGRGAFGEVRLVQKKDTGHVYAMKILRKADmleKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRA-------- 483
Cdd:cd05628  87 DMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEfyrnlnhs 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031869  484 -PME------KATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05628 167 lPSDftfqnmNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 230
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
335-539 2.26e-13

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 70.37  E-value: 2.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELircdeETQKTF----LTEVKVMRSL------DHPNVLKFIGVLYKDKKLNLL 404
Cdd:cd14133   5 EVLGKGTFGQVVKCYDLLTGEEVALKII-----KNNKDYldqsLDEIRLLELLnkkdkaDKYHIVRLKDVFYFKNHLCIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIeGGTLKDFLR--SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIK--LDKTVVVADFGLSrliVEER 480
Cdd:cd14133  80 FELL-SQNLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKIIDFGSS---CFLT 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  481 KRapmekattkkrtlrkndrkkRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd14133 156 QR--------------------LYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAEL 194
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
335-536 2.34e-13

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: 70.79  E-value: 2.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQktfltEVKV-MRSLDHPNVLKFIGV---LYKDKK-LNLLTEYIE 409
Cdd:cd14172  10 QVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARR-----EVEHhWRASGGPHIVHILDVyenMHHGKRcLLIIMECME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFL--RSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI--KLDKTVV-VADFGLSrliveerkrap 484
Cdd:cd14172  85 GGELFSRIqeRGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtsKEKDAVLkLTDFGFA----------- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  485 meKATTKKRTLRkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14172 154 --KETTVQNALQ--------TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIM 195
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
337-542 2.48e-13

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: 70.72  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHkATGKVMVMKELIRCD----EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd14026   5 LSRGAFGTVSRARH-ADWRVTVAIKCLKLDspvgDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFP---WQQKVRFAKGIASGMAYLHSMC--IIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapmek 487
Cdd:cd14026  84 LNELLHEKDIYPdvaWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKW------------ 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  488 attKKRTLRKNDRKKRYTVVGNPYWMAPEMLN-GKSYDETV--DIFSFGIVLCEIIGQ 542
Cdd:cd14026 152 ---RQLSISQSRSSKSAPEGGTIIYMPPEEYEpSQKRRASVkhDIYSYAIIMWEVLSR 206
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
335-540 2.80e-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: 70.11  E-value: 2.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQ----KTFLTEVKVMRSLD---HPNVLKFIGVLYKDKKLNL 403
Cdd:cd14004   6 KEMGEGAYGQVNLAIYKSKGKEvvikFIFKERILVDTWVRdrklGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDEFYYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTE-YIEGGTLKDFLR---SMDPFpwQQKVRFaKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIvee 479
Cdd:cd14004  86 VMEkHGSGMDLFDFIErkpNMDEK--EAKYIF-RQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYI--- 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  480 rKRAPMekattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYD-ETVDIFSFGIVLCEII 540
Cdd:cd14004 160 -KSGPF------------------DTFVGTIDYAAPEVLRGNPYGgKEQDIWALGVLLYTLV 202
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
335-536 2.96e-13

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 70.74  E-value: 2.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGK---VMVMKELIR-CDEETQKtfltevkVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14091   6 EEIGKGSYSVCKRCIHKATGKeyaVKIIDKSKRdPSEEIEI-------LLRYGQHPNIITLRDVYDDGNSVYLVTELLRG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK----TVVVADFGLSRLIveerkRAP-- 484
Cdd:cd14091  79 GELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESgdpeSLRICDFGFAKQL-----RAEng 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  485 --MEKATTKKrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14091 154 llMTPCYTAN-------------------FVAPEVLKKQGYDAACDIWSLGVLL 188
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
337-539 3.07e-13

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: 70.83  E-value: 3.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLT---EVKVMRSLD---HPNVLKFIGVLY-----KDKKLNLLT 405
Cdd:cd07862   9 IGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLStirEVAVLRHLEtfeHPNVVRLFDVCTvsrtdRETKLTLVF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkraP 484
Cdd:cd07862  89 EHVDQDLTTYLDKVPEPgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIY-------S 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  485 MEKATTkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd07862 162 FQMALT--------------SVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEM 202
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
354-540 4.38e-13

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 70.25  E-value: 4.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  354 GKVMVMKELIR--CDE--ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSM---DPFPWQ 426
Cdd:cd14157  16 GKQYVIKRLKEteCESpkSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDRLQQQggsHPLPWE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  427 QKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLsRLIVEERKRapmEKATTKKRTLRkndrkkrytv 506
Cdd:cd14157  96 QRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGL-RLCPVDKKS---VYTMMKTKVLQ---------- 161
                       170       180       190
                ....*....|....*....|....*....|....
gi 5031869  507 VGNPYWMAPEMLNGKsYDETVDIFSFGIVLCEII 540
Cdd:cd14157 162 ISLAYLPEDFVRHGQ-LTEKVDIFSCGVVLAEIL 194
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
336-540 4.42e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 71.97  E-value: 4.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFL-TEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL- 413
Cdd:PTZ00267  74 LVGRNPTTAAFVATRGSDPKEKVVAKFVMLNDERQAAYArSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLn 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   414 ---KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivEERKRAPMEKATt 490
Cdd:PTZ00267 154 kqiKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSK---QYSDSVSLDVAS- 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 5031869   491 kkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:PTZ00267 230 --------------SFCGTPYYLAPELWERKRYSKKADMWSLGVILYELL 265
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
335-536 4.46e-13

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: 70.14  E-value: 4.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATG-----KVMVMKELIRCDEETQKTfltEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14086   7 EELGKGAFSVVRRCVQKSTGqefaaKIINTKKLSARDHQKLER---EARICRLLKHPNIVRLHDSISEEGFHYLVFDLVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSrLIVEerkrapme 486
Cdd:cd14086  84 GGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLA-IEVQ-------- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  487 kattkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14086 155 -----------GDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVIL 193
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
332-540 6.28e-13

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 70.01  E-value: 6.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVlGKGFFGQAIKVTHKA--TGKVMVMKElIRCDEETQKTF----LTEVKVMRSLDHPNVLKFIGVL--YKDKKLNL 403
Cdd:cd07842   4 IEGCI-GRGTYGRVYKAKRKNgkDGKEYAIKK-FKGDKEQYTGIsqsaCREIALLRELKHENVVSLVEVFleHADKSVYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIE-------------------GGTLKDFLrsmdpfpWQqkvrfakgIASGMAYLHSMCIIHRDLNSHNCLI----K 460
Cdd:cd07842  82 LFDYAEhdlwqiikfhrqakrvsipPSMVKSLL-------WQ--------ILNGIHYLHSNWVLHRDLKPANILVmgegP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  461 LDKTVVVADFGLSRLIveerkRAPMekattkkRTLRKNDRkkrytVVGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEI 539
Cdd:cd07842 147 ERGVVKIGDLGLARLF-----NAPL-------KPLADLDP-----VVVTIWYRAPELLLGaRHYTKAIDIWAIGCIFAEL 209

                .
gi 5031869  540 I 540
Cdd:cd07842 210 L 210
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
376-542 6.71e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 71.26  E-value: 6.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   376 EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTE----------YIEGGTLKDflrsmDPFPWQQKvRFAKGIASGMAYLHSM 445
Cdd:PHA03210 213 EILALGRLNHENILKIEEILRSEANTYMITQkydfdlysfmYDEAFDWKD-----RPLLKQTR-AIMKQLLCAVEYIHDK 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   446 CIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveERKRAPMEkattkkrtlrkndrkkrYTVVGNPYWMAPEMLNGKSYDE 525
Cdd:PHA03210 287 KLIHRDIKLENIFLNCDGKIVLGDFGTAMPF--EKEREAFD-----------------YGWVGTVATNSPEILAGDGYCE 347
                        170
                 ....*....|....*..
gi 5031869   526 TVDIFSFGIVLCEIIGQ 542
Cdd:PHA03210 348 ITDIWSCGLILLDMLSH 364
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
337-546 6.82e-13

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: 69.51  E-value: 6.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAI--KVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd05086   5 IGNGWFGKVLlgEIYTGTSVARVVVKELkASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDpfpWQQK--------VRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGL--SR-----LIVE 478
Cdd:cd05086  85 KTYLANQQ---EKLRgdsqimllQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRykedyIETD 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  479 ERKRAPMEkattkkrtlrkndrkkrytvvgnpyWMAPEMLNGK-----SYDET--VDIFSFGIVLCEII---GQVYAD 546
Cdd:cd05086 162 DKKYAPLR-------------------------WTAPELVTSFqdgllAAEQTkySNIWSLGVTLWELFenaAQPYSD 214
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
337-540 7.28e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 69.56  E-value: 7.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGV------LYKDKKLnLLTEYIE 409
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCrLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVpeemnfLVNDVPL-LAMEYCS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDP---FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD--KTV-VVADFGLSRLIveerkra 483
Cdd:cd14039  80 GGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEIngKIVhKIIDLGYAKDL------- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  484 pmekattkkrtlrknDRKKRYT-VVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14039 153 ---------------DQGSLCTsFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECI 195
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
334-597 9.11e-13

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: 70.01  E-value: 9.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  334 GEVLGKGFFGQAIK-----VTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHP-NVLKFIGVLYK-DKKLNLLT 405
Cdd:cd05103  12 GKPLGRGAFGQVIEadafgIDKTATCRTVAVKMLkEGATHSEHRALMSELKILIHIGHHlNVVNLLGACTKpGGPLMVIV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSM--DPFPWQQK-VRFAKG------------------------------------------------ 434
Cdd:cd05103  92 EFCKFGNLSAYLRSKrsEFVPYKTKgARFRQGkdyvgdisvdlkrrldsitssqssassgfveekslsdveeeeagqedl 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  435 ----------------IASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkrapmekattkKRTLRKN 498
Cdd:cd05103 172 ykdfltledlicysfqVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKD------------PDYVRKG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  499 DRKKRYTvvgnpyWMAPEMLNGKSYDETVDIFSFGIVLCEIIG-------QVYADPD-ClpRTLDFGLNVKlfwekfVPT 570
Cdd:cd05103 240 DARLPLK------WMAPETIFDRVYTIQSDVWSFGVLLWEIFSlgaspypGVKIDEEfC--RRLKEGTRMR------APD 305
                       330       340
                ....*....|....*....|....*..
gi 5031869  571 DCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd05103 306 YTTPEMYQTMLDCWHGEPSQRPTFSEL 332
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
336-540 9.36e-13

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: 69.16  E-value: 9.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRC---DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd05607   9 VLGKGGFGEVCAVQVKNTGQMYACKKLDKKrlkKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliVEerkrAPMEKATT 490
Cdd:cd05607  89 LKYHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLA---VE----VKEGKPIT 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 KKrtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05607 162 QR--------------AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMV 197
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
337-539 9.37e-13

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 69.26  E-value: 9.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK--TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGgTLK 414
Cdd:cd07873  10 LGEGTYATVYKGRSKLTDNLVALKE-IRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDK-DLK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMDPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPMEKATTKKR 493
Cdd:cd07873  88 QYLDDCGNSINMHNVKlFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR-----AKSIPTKTYSNEVV 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  494 TLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEI 539
Cdd:cd07873 163 TL---------------WYRPPDILLGSTdYSTQIDMWGVGCIFYEM 194
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
371-604 1.00e-12

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


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 68.76  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  371 KTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMD---PFPWQQKVRFAKGIASGMAYLHSM-- 445
Cdd:cd14160  37 KRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLQCHGvtkPLSWHERINILIGIAKAIHYLHNSqp 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  446 -CIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveeRKRAPMEKATTKKRT-LRKNdrkkrytvvgnpYWMAPE--MLNGK 521
Cdd:cd14160 117 cTVICGNISSANILLDDQMQPKLTDFALAHF----RPHLEDQSCTINMTTaLHKH------------LWYMPEeyIRQGK 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  522 SYDETvDIFSFGIVLCEII-GQ--VYADPDCL-----------PRTLDFGLNvklFWEKFVPTdCPPAF----FPLAAIC 583
Cdd:cd14160 181 LSVKT-DVYSFGIVIMEVLtGCkvVLDDPKHLqlrdllhelmeKRGLDSCLS---FLDLKFPP-CPRNFsaklFRLAGRC 255
                       250       260
                ....*....|....*....|.
gi 5031869  584 CRLEPESRPAFSKLEDSFEAL 604
Cdd:cd14160 256 TATKAKLRPDMDEVLQRLEST 276
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
337-608 1.05e-12

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: 68.91  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIkvTHKATGKVMVMKELIRCDEET--QKTFLTEVKVMRsldHPNVLKFIGVLYKDK----KLNLLTEYIEG 410
Cdd:cd14220   3 IGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHEN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLR--SMDPfpwQQKVRFAKGIASGMAYLHSM--------CIIHRDLNSHNCLIKLDKTVVVADFGLsrliveer 480
Cdd:cd14220  78 GSLYDFLKctTLDT---RALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGL-------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 krAPMEKATTKKRTLRKNDRkkrytvVGNPYWMAPEMLngksyDETV-----------DIFSFGIVLCEIIgqvyadpdc 549
Cdd:cd14220 147 --AVKFNSDTNEVDVPLNTR------VGTKRYMAPEVL-----DESLnknhfqayimaDIYSFGLIIWEMA--------- 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  550 lPRTLDFGL--NVKLFWEKFVPTDcpPAFFPLAAICC--RLepesRPAFSKLEDSFEALSLYL 608
Cdd:cd14220 205 -RRCVTGGIveEYQLPYYDMVPSD--PSYEDMREVVCvkRL----RPTVSNRWNSDECLRAVL 260
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
336-540 1.07e-12

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: 68.92  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELircdEET-------QKTFLTEVKVMRSLDHPNVLKfIGVLYKDKK-LNLLTEY 407
Cdd:cd05605   7 VLGKGGFGEVCACQVRATGKMYACKKL----EKKrikkrkgEAMALNEKQILEKVNSRFVVS-LAYAYETKDaLCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGGTLKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkrapm 485
Cdd:cd05605  82 MNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGE----- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  486 ekaTTKKRtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05605 157 ---TIRGR-------------VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMI 195
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
337-539 1.33e-12

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 69.14  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELircdeeTQKTFLTEVKVMRSLDHPNVLK---------FIGVLYK---DKKLNLL 404
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVL------SKKVIVAKKEVAHTIGERNILVrtaldespfIVGLKFSfqtPTDLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrap 484
Cdd:cd05586  75 TDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS----------- 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  485 meKATTKkrtlrknDRKKRYTVVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05586 144 --KADLT-------DNKTTNTFCGTTEYLAPEvLLDEKGYTKMVDFWSLGVLVFEM 190
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
335-536 1.39e-12

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 68.46  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIgvlykDKKLN----------L 403
Cdd:cd14037   9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLsGHKNIVGYI-----DSSANrsgngvyevlL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFL--RSMDPFPWQQKVRFAKGIASGMAYLHSM--CIIHRDLNSHNCLIKLDKTVVVADFGlsrlivee 479
Cdd:cd14037  84 LMEYCKGGGVIDLMnqRLQTGLTESEILKIFCDVCEAVAAMHYLkpPLIHRDLKVENVLISDSGNYKLCDFG-------- 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  480 rkrapmeKATTKKRTLRKNDRK-------KRYTvvgNPYWMAPEMLN---GKSYDETVDIFSFGIVL 536
Cdd:cd14037 156 -------SATTKILPPQTKQGVtyveediKKYT---TLQYRAPEMIDlyrGKPITEKSDIWALGCLL 212
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
335-536 1.53e-12

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: 68.52  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGkvmvMKELIRCDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14175   7 ETIGVGSYSVCKRCVHKATN----MEYAVKVIDKSKRDPSEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIkLDKT-----VVVADFGLSRLIveerkRApmeka 488
Cdd:cd14175  83 LDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILY-VDESgnpesLRICDFGFAKQL-----RA----- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  489 ttkkrtlrknDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14175 152 ----------ENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILL 189
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
330-541 1.62e-12

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: 69.28  E-value: 1.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIhgEVLGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLT 405
Cdd:cd05617  18 DLI--RVIGRGSYAKVLLVRLKKNDQIYAMKvvkkELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapm 485
Cdd:cd05617  96 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC------------ 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  486 ekattkKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIG 541
Cdd:cd05617 164 ------KEGLGPGDTTS--TFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMA 211
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
376-536 1.78e-12

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 67.88  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVL-YKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNS 454
Cdd:cd14165  51 ELEILARLNHKSIIKTYEIFeTSDGKVYIVMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKC 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  455 HNCLIKLDKTVVVADFGLSRliveerkraPMEKATTKKRTLRKndrkkryTVVGNPYWMAPEMLNGKSYDETV-DIFSFG 533
Cdd:cd14165 131 ENLLLDKDFNIKLTDFGFSK---------RCLRDENGRIVLSK-------TFCGSAAYAAPEVLQGIPYDPRIyDIWSLG 194

                ...
gi 5031869  534 IVL 536
Cdd:cd14165 195 VIL 197
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
335-541 2.16e-12

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: 68.55  E-value: 2.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEE--TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLN------LLTE 406
Cdd:cd07855  11 ETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVvtTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYAdfkdvyVVLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGgTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIV---EERKRA 483
Cdd:cd07855  91 LMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLCtspEEHKYF 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  484 PMEKATTKkrtlrkndrkkrytvvgnPYwMAPE-MLNGKSYDETVDIFSFGIVLCEIIG 541
Cdd:cd07855 170 MTEYVATR------------------WY-RAPElMLSLPEYTQAIDMWSVGCIFAEMLG 209
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
373-540 2.26e-12

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: 67.68  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  373 FLTEVKVMRSLDHPNVLKFIGVlyKDKKLNLLTEYIEGGTLKDFLR------SMDPFPWQQKVRFAKGIASGMAYLHSMC 446
Cdd:cd14067  57 FRQEASMLHSLQHPCIVYLIGI--SIHPLCFALELAPLGSLNTVLEenhkgsSFMPLGHMLTFKIAYQIAAGLAYLHKKN 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  447 IIHRDLNSHNCLI-KLDK----TVVVADFGLSRLIVEERKRApmekattkkrtlrkndrkkrytVVGNPYWMAPEMLNGK 521
Cdd:cd14067 135 IIFCDLKSDNILVwSLDVqehiNIKLSDYGISRQSFHEGALG----------------------VEGTPGYQAPEIRPRI 192
                       170
                ....*....|....*....
gi 5031869  522 SYDETVDIFSFGIVLCEII 540
Cdd:cd14067 193 VYDEKVDMFSYGMVLYELL 211
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
337-540 2.72e-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: 68.37  E-value: 2.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKD----KKLNLLTEYIEGGT 412
Cdd:cd05610  12 ISRGAFGKVYLGRKKNNSKLYAVK-VVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSlqsaNNVYLVMEYLIGGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRL-------IVEERKRAPM 485
Cdd:cd05610  91 VKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVtlnrelnMMDILTTPSM 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  486 EKAT--------------------------TKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEI 539
Cdd:cd05610 171 AKPKndysrtpgqvlslisslgfntptpyrTPKSVRRGAARVEGERILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEF 250

                .
gi 5031869  540 I 540
Cdd:cd05610 251 L 251
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
330-536 3.25e-12

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 66.96  E-value: 3.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFltevkvmrslDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd13995  10 DFIPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACF----------RHENIAELYGALLWEETVHLFMEAGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVaDFGLSrliveerkrAPMEKAT 489
Cdd:cd13995  80 GGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLS---------VQMTEDV 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  490 TKKRTLRkndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd13995 150 YVPKDLR-----------GTEIYMSPEVILCRGHNTKADIYSLGATI 185
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
336-542 3.50e-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: 67.36  E-value: 3.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd05630   7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDP--FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkrapmekaTT 490
Cdd:cd05630  87 LKFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQ--------TI 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  491 KKRtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ 542
Cdd:cd05630 159 KGR-------------VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIaGQ 198
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
335-474 3.95e-12

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 67.41  E-value: 3.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKElIRCDEE--TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEggt 412
Cdd:cd07844   6 DKLGEGSYATVYKGRSKLTGQLVALKE-IRLEHEegAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD--- 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031869  413 lKDFLRSMDPFPW---QQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSR 474
Cdd:cd07844  82 -TDLKQYMDDCGGglsMHNVRlFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR 146
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
335-542 4.33e-12

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: 67.52  E-value: 4.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTfLTEVKVMR-SLDHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVyaikVLKKDVILQDDDVDCT-MTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerKRAPMEKA 488
Cdd:cd05591  80 GGDLMFQIQRARKFD-EPRARFyAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC-------KEGILNGK 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  489 TTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ 542
Cdd:cd05591 152 TTT-------------TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMaGQ 193
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
337-536 6.48e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 66.72  E-value: 6.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIrcdeeTQKTFLTEVKV-MRSLDHPNV----------LKFIGVLYKDKKLNLLT 405
Cdd:cd14171  14 LGTGISGPVRVCVKKSTGERFALKILL-----DRPKARTEVRLhMMCSGHPNIvqiydvyansVQFPGESSPRARLLIVM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIK---LDKTVVVADFGLSRLiveerkr 482
Cdd:cd14171  89 ELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKdnsEDAPIKLCDFGFAKV------- 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  483 apmekattkkrtlrknDRKKRYTVVGNPYWMAPEMLNGK-----------------SYDETVDIFSFGIVL 536
Cdd:cd14171 162 ----------------DQGDLMTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVII 216
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
333-542 6.50e-12

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: 66.55  E-value: 6.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  333 HGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQK---TFLTEVKVMRSLDHPNVLKfIGVLYKDKK-LNLLTEYI 408
Cdd:cd05631   4 HYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKRILEKVNSRFVVS-LAYAYETKDaLCLVLTIM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSM-DP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERkrapme 486
Cdd:cd05631  83 NGGDLKFHIYNMgNPgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGE------ 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  487 kaTTKKRtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ 542
Cdd:cd05631 157 --TVRGR-------------VGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIqGQ 198
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
406-536 6.64e-12

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: 67.20  E-value: 6.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPwQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVVVADFGLSRlIVEERKR 482
Cdd:cd13977 115 EFCDGGDMNEYLLSRRPDR-QTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILIshkRGEPILKVADFGLSK-VCSGSGL 192
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  483 APMEKATTKKRTLRkndrkkryTVVGNPYWMAPEMLNGKsYDETVDIFSFGIVL 536
Cdd:cd13977 193 NPEEPANVNKHFLS--------SACGSDFYMAPEVWEGH-YTAKADIFALGIII 237
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
337-543 7.16e-12

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: 66.96  E-value: 7.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELiRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd05598   9 IGVGAFGEVSLVRKKDTNALYAMKTL-RKKDVLKRNQVAHVKAERDIlaeaDNEWVVKLYYSFQDKENLYFVMDYIPGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSMDPFPwQQKVRFAkgIAS---GMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekat 489
Cdd:cd05598  88 LMSLLIKKGIFE-EDLARFY--IAElvcAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC---------------- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  490 tkkRTLRKNDRKKRYT---VVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQV 543
Cdd:cd05598 149 ---TGFRWTHDSKYYLahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEmLVGQP 203
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
332-535 7.57e-12

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: 66.00  E-value: 7.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKelIRCDEETqktFLTEVKVMRSLDHPNVLKFIGVLYKDKK-LNLLTEYIEG 410
Cdd:cd14109   7 IGEEDEKRAAQGAPFHVTERSTGRNFLAQ--LRYGDPF---LMREVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLAST 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTL--KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKtVVVADFGLSRLIVeerkrapmeka 488
Cdd:cd14109  82 IELvrDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDK-LKLADFGQSRRLL----------- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031869  489 ttkkrtlrkndRKKRYTVV-GNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14109 150 -----------RGKLTTLIyGSPEFVSPEIVNSYPVTLATDMWSVGVL 186
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
336-540 8.55e-12

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 66.68  E-value: 8.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMK----ELIRcDEETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05588   2 VIGRGSYAKVLMVELKKTKRIYAMKvikkELVN-DDEDIDWVQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekatt 490
Cdd:cd05588  81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMC----------------- 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031869  491 kKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd05588 144 -KEGLRPGDTTS--TFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEML 190
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
330-535 1.23e-11

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: 65.73  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELI--RCDEETQKTFLTEVKVMR-SLDHPNVLKFIGVLYKDKKLNLLTE 406
Cdd:cd14197  10 SLSPGRELGRGKFAVVRKCVEKDSGKEFAAKFMRkrRKGQDCRMEIIHEIAVLElAQANPWVINLHEVYETASEMILVLE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  407 YIEGGTLKD--FLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK---TVVVADFGLSRLIveerk 481
Cdd:cd14197  90 YAAGGEIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRIL----- 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  482 rapmekattkkrtlrKNDRKKRyTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14197 165 ---------------KNSEELR-EIMGTPEYVAPEILSYEPISTATDMWSIGVL 202
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
431-602 1.25e-11

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: 66.85  E-value: 1.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  431 FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrapmekattkkrtlrKNDrkKRYTVVGNP 510
Cdd:cd05104 219 FSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDI--------------------RND--SNYVVKGNA 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  511 Y----WMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRL 586
Cdd:cd05104 277 RlpvkWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVDSKFYKMIKEGYRMDSPEFAPSEMYDIMRSCWDA 356
                       170
                ....*....|....*.
gi 5031869  587 EPESRPAFSKLEDSFE 602
Cdd:cd05104 357 DPLKRPTFKQIVQLIE 372
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
337-540 1.35e-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: 66.22  E-value: 1.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDE---ETQKTFlTEVKVMRSLDHPNVLKFIGVLYKDKKLN-----LLTEYI 408
Cdd:cd07877  25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQsiiHAKRTY-RELRLLKHMKHENVIGLLDVFTPARSLEefndvYLVTHL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSmdpfpwqQK-----VRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKr 482
Cdd:cd07877 104 MGADLNNIVKC-------QKltddhVQFlIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMT- 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  483 apmekattkkrtlrkndrkkryTVVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07877 176 ----------------------GYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELL 212
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
425-592 1.44e-11

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: 65.20  E-value: 1.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  425 WQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerKRAPMEKattkkrtlrkndrkkry 504
Cdd:cd13975 101 LEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK------PEAMMSG----------------- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  505 TVVGNPYWMAPEMLNGKsYDETVDIFSFGIVLCEII-GQVYadpdcLPRTLDFGLNVKLFWeKFVPTDCPPAFFP----- 578
Cdd:cd13975 158 SIVGTPIHMAPELFSGK-YDNSVDVYAFGILFWYLCaGHVK-----LPEAFEQCASKDHLW-NNVRKGVRPERLPvfdee 230
                       170
                ....*....|....*..
gi 5031869  579 ---LAAICCRLEPESRP 592
Cdd:cd13975 231 cwnLMEACWSGDPSQRP 247
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
337-539 1.65e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 67.45  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    337 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLT-EVKVMRSLDHPNVLKFIGVLYK--DKKLNLLTEYIEGGT 412
Cdd:PTZ00266   21 IGNGRFGEVFLVKHKRTQEFFCWKAIsYRGLKEREKSQLViEVNVMRELKHKNIVRYIDRFLNkaNQKLYILMEFCDAGD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869    413 L-KDFLRSMDPFPWQQK---VRFAKGIASGMAYLHSMC-------IIHRDLNSHNCLIK-----LDKTVV---------- 466
Cdd:PTZ00266  101 LsRNIQKCYKMFGKIEEhaiVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLStgirhIGKITAqannlngrpi 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869    467 --VADFGLSRLIVEErkrapmekattkkrtlrkndrKKRYTVVGNPYWMAPEML--NGKSYDETVDIFSFGIVLCEI 539
Cdd:PTZ00266  181 akIGDFGLSKNIGIE---------------------SMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYEL 236
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
337-540 1.71e-11

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 65.64  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKG-----FFGqaIKVThkaTGKVMVMKEL--IRcdeetQKTFLTEVKVMRSL-DHPNVLKFIGVLyKDKKLN---LLT 405
Cdd:cd14132  26 IGRGkysevFEG--INIG---NNEKVVIKVLkpVK-----KKKIKREIKILQNLrGGPNIVKLLDVV-KDPQSKtpsLIF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  406 EYIEGGTLKDFLRSMDPFPwqqkVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK-TVVVADFGLSrliveERKRA 483
Cdd:cd14132  95 EYVNNTDFKTLYPTLTDYD----IRYyMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWGLA-----EFYHP 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  484 pmekattkkrtlrkndrKKRYTV-VGNPYWMAPEML-NGKSYDETVDIFSFGIVLCEII 540
Cdd:cd14132 166 -----------------GQEYNVrVASRYYKGPELLvDYQYYDYSLDMWSLGCMLASMI 207
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
337-540 1.71e-11

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: 66.06  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIR--CDEETQKTFLTEVKVMRSLDHPNVLK----FIGVLykdKKLNLLTEyIEG 410
Cdd:cd07856  18 VGMGAFGLVCSARDQLTGQNVAVKKIMKpfSTPVLAKRTYRELKLLKHLRHENIISlsdiFISPL---EDIYFVTE-LLG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSmDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapmekatt 490
Cdd:cd07856  94 TDLHRLLTS-RPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI--------------- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  491 kkrtlrKNDRKKRYtvVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07856 158 ------QDPQMTGY--VSTRYYRAPEiMLTWQKYDVEVDIWSAGCIFAEML 200
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
335-541 1.85e-11

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 65.71  E-value: 1.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCD--EETQktfLTEVKVMRSL----DHPNVLKfigvLY----KDKKLNLL 404
Cdd:cd05599   7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEmlEKEQ---VAHVRAERDIlaeaDNPWVVK----LYysfqDEENLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQkVRF-----AKGIASgmayLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRlivee 479
Cdd:cd05599  80 MEFLPGGDMMTLLMKKDTLTEEE-TRFyiaetVLAIES----IHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT----- 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031869  480 rkraPMEKAttkkrtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIG 541
Cdd:cd05599 150 ----GLKKS------------HLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEmLIG 196
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
337-535 2.34e-11

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: 64.56  E-value: 2.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELI--RCDEETQKTFLTEVKVMR-SLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14198  16 LGRGKFAVVRQCISKSTGQEYAAKFLKkrRRGQDCRAEILHEIAVLElAKSNPRVVNLHEVYETTSEIILILEYAAGGEI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRS--MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCL---IKLDKTVVVADFGLSRLIveerkrapmEKA 488
Cdd:cd14198  96 FNLCVPdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGDIKIVDFGMSRKI---------GHA 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  489 TtkkrTLRKndrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14198 167 C----ELRE--------IMGTPEYLAPEILNYDPITTATDMWNIGVI 201
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
337-604 2.83e-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: 2.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIkvTHKATGKVMVMKELIRCDEET--QKTFLTEVKVMRsldHPNVLKFIGVLYKDK----KLNLLTEYIEG 410
Cdd:cd14219  13 IGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHEN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDpFPWQQKVRFAKGIASGMAYLHSM--------CIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErkr 482
Cdd:cd14219  88 GSLYDYLKSTT-LDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISD--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  483 apmekatTKKRTLRKNDRkkrytvVGNPYWMAPEMLngksyDETV-----------DIFSFGIVLCEIIgqvyadpdclP 551
Cdd:cd14219 164 -------TNEVDIPPNTR------VGTKRYMPPEVL-----DESLnrnhfqsyimaDMYSFGLILWEVA----------R 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  552 RTLDFGL--NVKLFWEKFVPTDcpPAFFPLAAICCRlePESRPAFSKLEDSFEAL 604
Cdd:cd14219 216 RCVSGGIveEYQLPYHDLVPSD--PSYEDMREIVCI--KRLRPSFPNRWSSDECL 266
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
335-540 4.51e-11

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: 64.63  E-value: 4.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEET--QKTfLTEVKVMRSLDHPNVLKFIGVLYKD-----KKLNLLTEY 407
Cdd:cd07849  11 SYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTycLRT-LREIKILLRFKHENIIGILDIQRPPtfesfKDVYIVQEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  408 IEGgTLKDFLRSmdpfpwqQKVR------FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERK 481
Cdd:cd07849  90 MET-DLYKLIKT-------QHLSndhiqyFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHD 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  482 RAPM--EKATTKkrtlrkndrkkrytvvgnpYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07849 162 HTGFltEYVATR-------------------WYRAPEiMLNSKGYTKAIDIWSVGCILAEML 204
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
335-535 4.86e-11

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: 63.76  E-value: 4.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLK 414
Cdd:cd14114   8 EELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  415 DFLRSMD-PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHN--CLIKLDKTVVVADFGLSrliveeRKRAPME--KAT 489
Cdd:cd14114  88 ERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENimCTTKRSNEVKLIDFGLA------THLDPKEsvKVT 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031869  490 TkkrtlrkndrkkrytvvGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14114 162 T-----------------GTAEFAAPEIVEREPVGFYTDMWAVGVL 190
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
12-64 5.66e-11

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 58.10  E-value: 5.66e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869   12 CPGCGDHIAPsQIWYRTVNETWHGSCFRCSECQDSLTN-WYYEKDGKLYCPKDY 64
Cdd:cd08368   1 CAGCGKPIEG-RELLRALGKKWHPECFKCAECGKPLGGdSFYEKDGKPYCEKCY 53
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
337-535 6.84e-11

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: 63.06  E-value: 6.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDF 416
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVK-FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  417 LRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLdktvvvadfglsrliveeRKRAPMEKATTKKRTLR 496
Cdd:cd14115  80 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL------------------RIPVPRVKLIDLEDAVQ 141
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 5031869  497 KNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14115 142 ISGHRHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVL 180
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
330-535 8.63e-11

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: 63.07  E-value: 8.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  330 DLIHGEV--LGKGFFGQAIKVTHKATGKVM----VMKELIRCDEETQktfltEVKVMRSLDHPNVLKFIGVLYKDKKLNL 403
Cdd:cd14113   6 DSFYSEVaeLGRGRFSVVKKCDQRGTKRAVatkfVNKKLMKRDQVTH-----ELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  404 LTEYIEGGTLKDFLRSmdpfpW----QQKVRFAKG-IASGMAYLHSMCIIHRDLNSHNclikldktvvvadfglsrLIVE 478
Cdd:cd14113  81 VLEMADQGRLLDYVVR-----WgnltEEKIRFYLReILEALQYLHNCRIAHLDLKPEN------------------ILVD 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  479 ERKRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV 535
Cdd:cd14113 138 QSLSKPTIKLADFGDAVQLNTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVL 194
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
332-540 8.80e-11

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: 63.06  E-value: 8.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEg 410
Cdd:cd07870   3 LNLEKLGEGSYATVYKGISRINGQLVALKVIsMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 gtlKDFLRSMDPFP---WQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeRKRAPME 486
Cdd:cd07870  82 ---TDLAQYMIQHPgglHPYNVRlFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAR-----AKSIPSQ 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  487 KATTKKRTLrkndrkkrytvvgnpYWMAPEMLNGKS-YDETVDIFSFGIVLCEII 540
Cdd:cd07870 154 TYSSEVVTL---------------WYRPPDVLLGATdYSSALDIWGAGCIFIEML 193
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
335-536 9.21e-11

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 63.13  E-value: 9.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLD-HPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14174   8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGSI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKL-DKT--VVVADFGLSRLIVEERKRAPMekaTT 490
Cdd:cd14174  88 LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESpDKVspVKICDFDLGSGVKLNSACTPI---TT 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  491 KKRTlrkndrkkryTVVGNPYWMAPEML-----NGKSYDETVDIFSFGIVL 536
Cdd:cd14174 165 PELT----------TPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVIL 205
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
336-540 9.54e-11

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 63.48  E-value: 9.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKK-LNLLTEYIEGGT 412
Cdd:cd05601   8 VIGRGHFGEVQVVKEKATGDIYAMKVLKKSEtlAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSEnLYLVMEYHPGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFL-RSMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIklDKT--VVVADFGLSrliveerkrapmEKA 488
Cdd:cd05601  88 LLSLLsRYDDIFE-ESMARFyLAELVLAIHSLHSMGYVHRDIKPENILI--DRTghIKLADFGSA------------AKL 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  489 TTKKRTLRKndrkkryTVVGNPYWMAPEML---NGKS---YDETVDIFSFGIVLCEII 540
Cdd:cd05601 153 SSDKTVTSK-------MPVGTPDYIAPEVLtsmNGGSkgtYGVECDWWSLGIVAYEML 203
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
336-539 1.32e-10

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 63.04  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFfGQAIKVT---HKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd08227   5 VIGRGF-EDLMTVNlarYKPTGEYVTVRriNLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRS--MDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKA 488
Cdd:cd08227  84 GSAKDLICThfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRVVHD 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  489 TTKkrtlrkndrkkrYTVVGNPyWMAPEML--NGKSYDETVDIFSFGIVLCEI 539
Cdd:cd08227 164 FPK------------YSVKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACEL 203
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
335-536 1.35e-10

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: 62.68  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCD---------EETQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKKLNLL 404
Cdd:cd14181  16 EVIGRGVSSVVRRCVHRHTGQEFAVK-IIEVTaerlspeqlEEVRSSTLKEIHILRQVsGHPSIITLIDSYESSTFIFLV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveerkrAP 484
Cdd:cd14181  95 FDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHL------EP 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031869  485 MEKattkkrtLRKndrkkrytVVGNPYWMAPEMLNGkSYDET-------VDIFSFGIVL 536
Cdd:cd14181 169 GEK-------LRE--------LCGTPGYLAPEILKC-SMDEThpgygkeVDLWACGVIL 211
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
337-597 1.42e-10

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: 62.14  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATG-KVMVMKELIRCDEetqktfLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKD 415
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGfQCAVKKVRLEVFR------AEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD-KTVVVADFGLSrliveerkrAPMEKATTKKRT 494
Cdd:cd13991  88 LIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHA---------ECLDPDGLGKSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  495 LRKNDrkkrytVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL------CEIIGQVYADPDCL-----PRTLdfglnvklf 563
Cdd:cd13991 159 FTGDY------IPGTETHMAPEVVLGKPCDAKVDVWSSCCMMlhmlngCHPWTQYYSGPLCLkianePPPL--------- 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031869  564 WEkfVPTDCPPAFFPLAAICCRLEPESRPAFSKL 597
Cdd:cd13991 224 RE--IPPSCAPLTAQAIQAGLRKEPVHRASAAEL 255
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
337-541 1.86e-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: 63.22  E-value: 1.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRC--DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKD-----KKLNLLTEYIE 409
Cdd:cd07853   8 IGYGAFGVVWSVTDPRDGKRVALKKMPNVfqNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPhidpfEEIYVVTELMQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVrFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliVEErkrapmekat 489
Cdd:cd07853  88 SDLHKIIVSPQPLSSDHVKV-FLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR--VEE---------- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  490 tkkrtlrKNDRKKRYTVVGNPYWMAPEMLNG-KSYDETVDIFSFGIVLCEIIG 541
Cdd:cd07853 155 -------PDESKHMTQEVVTQYYRAPEILMGsRHYTSAVDIWSVGCIFAELLG 200
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
336-540 1.97e-10

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 62.78  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMK-----ELIRCDEETqkTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05596  33 VIGRGAFGEVQLVRHKSTKKVYAMKllskfEMIKRSDSA--FFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPG 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDpFPwQQKVRF--AKGIASGMAyLHSMCIIHRDLNSHNCLikLDKT--VVVADFGlsrliveerkrapme 486
Cdd:cd05596 111 GDLVNLMSNYD-VP-EKWARFytAEVVLALDA-IHSMGFVHRDVKPDNML--LDASghLKLADFG--------------- 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031869  487 kattkkrTLRKNDRKKRY---TVVGNPYWMAPEMLNGKS----YDETVDIFSFGIVLCEII 540
Cdd:cd05596 171 -------TCMKMDKDGLVrsdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEML 224
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
438-543 2.52e-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: 62.43  E-value: 2.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  438 GMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPmekattkkrtlrkndrkkrYTVvgNPYWMAPEM 517
Cdd:cd07850 114 GIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTP-------------------YVV--TRYYRAPEV 172
                        90       100
                ....*....|....*....|....*..
gi 5031869  518 LNGKSYDETVDIFSFGIVLCEII-GQV 543
Cdd:cd07850 173 ILGMGYKENVDIWSVGCIMGEMIrGTV 199
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
336-542 2.66e-10

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: 61.91  E-value: 2.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGT 412
Cdd:cd05632   9 VLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  413 LKDFLRSM-DP-FPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEerkrapmekatt 490
Cdd:cd05632  89 LKFHIYNMgNPgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPE------------ 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  491 kkrtlrKNDRKKRYTVVGnpyWMAPEMLNGKSYDETVDIFSFGIVLCEII-GQ 542
Cdd:cd05632 157 ------GESIRGRVGTVG---YMAPEVLNNQRYTLSPDYWGLGCLIYEMIeGQ 200
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
354-539 2.89e-10

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 61.48  E-value: 2.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  354 GKVMVMKELIRCDEETQKTFLTEVKVMRS----LDHPNVLKF----IGVLYKDKKLNLLTEYIEGGTLKDFL-------R 418
Cdd:cd14035  19 GVEVVWNELFFQDKKAFKAHEDKIKTMFEnltlVDHPNIVKFhkywLDVKDNHARVVFITEYVSSGSLKQFLkktkknhK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  419 SMDPFPWQqkvRFAKGIASGMAYLHSmC---IIHRDLNS------HNCLIKLDKTvvvadfgLSRLIVEErkrAPMEKAT 489
Cdd:cd14035  99 TMNARAWK---RWCTQILSALSYLHS-CeppIIHGNLTSdtifiqHNGLIKIGSV-------WHRLFVNV---LPEGGVR 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  490 TKKRTLRKNDRkkrytvvgNPYWMAPEMlnGKSYDET-VDIFSFGIVLCEI 539
Cdd:cd14035 165 GPLRQEREELR--------NLHFFPPEY--GSCEDGTaVDIFSFGMCALEM 205
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
336-540 3.18e-10

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 61.99  E-value: 3.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd14223   7 IIGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKLSFILDLMN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekat 489
Cdd:cd14223  87 GGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA---------------- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 tkkrtlRKNDRKKRYTVVGNPYWMAPEMLN-GKSYDETVDIFSFGIVLCEII 540
Cdd:cd14223 151 ------CDFSKKKPHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLL 196
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
337-541 3.35e-10

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: 62.00  E-value: 3.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEET--QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE----G 410
Cdd:cd07858  13 IGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRidAKRTLREIKLLRHLDHENVIAIKDIMPPPHREAFNDVYIVyelmD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveerkrapmekatt 490
Cdd:cd07858  93 TDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLART--------------- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  491 kkrTLRKNDRKKRYTVVgnPYWMAPE-MLNGKSYDETVDIFSFGIVLCEIIG 541
Cdd:cd07858 158 ---TSEKGDFMTEYVVT--RWYRAPElLLNCSEYTTAIDVWSVGCIFAELLG 204
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
336-540 3.58e-10

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 62.00  E-value: 3.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKKLNLLTEYIE 409
Cdd:cd05633  12 IIGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekat 489
Cdd:cd05633  92 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA---------------- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031869  490 tkkrtlRKNDRKKRYTVVGNPYWMAPEMLN-GKSYDETVDIFSFGIVLCEII 540
Cdd:cd05633 156 ------CDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLL 201
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
376-540 3.60e-10

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: 61.97  E-value: 3.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVLYKDKKLN------LLTEYIEGGTLKDFLRSMDPfpwQQKVRFAKGIASGMAYLHSMCIIH 449
Cdd:cd07876  70 ELVLLKCVNHKNIISLLNVFTPQKSLEefqdvyLVMELMDANLCQVIHMELDH---ERMSYLLYQMLCGIKHLHSAGIIH 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  450 RDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmekattkkRTLRKNDRKKRYTVvgNPYWMAPEMLNGKSYDETVDI 529
Cdd:cd07876 147 RDLKPSNIVVKSDCTLKILDFGLA-------------------RTACTNFMMTPYVV--TRYYRAPEVILGMGYKENVDI 205
                       170
                ....*....|.
gi 5031869  530 FSFGIVLCEII 540
Cdd:cd07876 206 WSVGCIMGELV 216
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
337-541 3.96e-10

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 61.65  E-value: 3.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKAT---------------GKVMVMKELIRcdeetqktfltEVKVMRSL-DHPNVLKFIGV----LY 396
Cdd:cd07857   8 LGQGAYGIVCSARNAETseeetvaikkitnvfSKKILAKRALR-----------ELKLLRHFrGHKNITCLYDMdivfPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  397 KDKKLNLLTEYIEGgTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLI 476
Cdd:cd07857  77 NFNELYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGF 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031869  477 VEERKrapmekattkkrtlrKNDRK-KRYtvVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEIIG 541
Cdd:cd07857 156 SENPG---------------ENAGFmTEY--VATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLG 205
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
335-536 4.02e-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: 61.18  E-value: 4.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKtfltEVKVM-RSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14178   9 EDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSE----EIEILlRYGQHPNIITLKDVYDDGKFVYLVMELMRGGEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD----KTVVVADFGLSRLIveerkRAPMEKAT 489
Cdd:cd14178  85 LDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgnpESIRICDFGFAKQL-----RAENGLLM 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  490 TKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14178 160 TPCYTAN---------------FVAPEVLKRQGYDAACDIWSLGILL 191
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
334-540 4.16e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 62.36  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   334 GEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKtfltEVKVMRSLDHPNVLKFIGVLY-----KDKK---LNLLT 405
Cdd:PTZ00036  71 GNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNR----ELLIMKNLNHINIIFLKDYYYtecfkKNEKnifLNVVM 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   406 EYIEGGT---LKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK-TVVVADFGlsrliveerk 481
Cdd:PTZ00036 147 EFIPQTVhkyMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFG---------- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   482 rapmekattKKRTLRKNDRKKRYtvVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:PTZ00036 217 ---------SAKNLLAGQRSVSY--ICSRFYRAPElMLGATNYTTHIDLWSLGCIIAEMI 265
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
339-534 4.22e-10

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: 60.70  E-value: 4.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  339 KGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLR 418
Cdd:cd14110  13 RGRFSVVRQCEEKRSGQMLAAK-IIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  419 SMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEErKRAPMekattkkrtlrkn 498
Cdd:cd14110  92 ERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQG-KVLMT------------- 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 5031869  499 DRKKRYTVVgnpywMAPEMLNGKSYDETVDIFSFGI 534
Cdd:cd14110 158 DKKGDYVET-----MAPELLEGQGAGPQTDIWAIGV 188
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
335-536 4.27e-10

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 61.57  E-value: 4.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGkvmvMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14176  25 EDIGVGSYSVCKRCIHKATN----MEFAVKIIDKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLD----KTVVVADFGLSRLIVEERK--RAPMEK 487
Cdd:cd14176 101 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGllMTPCYT 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031869  488 ATtkkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14176 181 AN----------------------FVAPEVLERQGYDAACDIWSLGVLL 207
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
337-540 4.75e-10

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 61.51  E-value: 4.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRC--DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY-----IE 409
Cdd:cd07880  23 VGSGAYGTVCSALDRRTGAKVAIKKLYRPfqSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLDRFHDFylvmpFM 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  410 GGTLKDFLRsMDPFPwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSrliveerkrapmeka 488
Cdd:cd07880 103 GTDLGKLMK-HEKLS-EDRIQFlVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA--------------- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  489 ttkkrtlRKNDRKKRYTVVGNpYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07880 166 -------RQTDSEMTGYVVTR-WYRAPEvILNWMHYTQTVDIWSVGCIMAEML 210
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
335-536 5.34e-10

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 60.70  E-value: 5.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKEL------IRCDEETQK---TFLTEVKVMRSLD-HPNVLKFIGVLYKDKKLNLL 404
Cdd:cd14182   9 EILGRGVSSVVRRCIHKPTRQEYAVKIIditgggSFSPEEVQElreATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKrap 484
Cdd:cd14182  89 FDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEK--- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031869  485 mekattkkrtLRKndrkkrytVVGNPYWMAPEML------NGKSYDETVDIFSFGIVL 536
Cdd:cd14182 166 ----------LRE--------VCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIM 205
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
376-540 8.49e-10

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: 60.87  E-value: 8.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  376 EVKVMRSLDHPNVLKFIGVLYKDKKLN------LLTEYIEGGTLKDFLRSMDPfpwQQKVRFAKGIASGMAYLHSMCIIH 449
Cdd:cd07874  66 ELVLMKCVNHKNIISLLNVFTPQKSLEefqdvyLVMELMDANLCQVIQMELDH---ERMSYLLYQMLCGIKHLHSAGIIH 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  450 RDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPmekattkkrtlrkndrkkrYTVVgnPYWMAPEMLNGKSYDETVDI 529
Cdd:cd07874 143 RDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTP-------------------YVVT--RYYRAPEVILGMGYKENVDI 201
                       170
                ....*....|.
gi 5031869  530 FSFGIVLCEII 540
Cdd:cd07874 202 WSVGCIMGEMV 212
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
337-540 9.26e-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: 60.83  E-value: 9.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  337 LGKGFFGQAIKVTHKATGKVMVMKELIRCDE---ETQKTFlTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEY-----I 408
Cdd:cd07878  23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQsliHARRTY-RELRLLKHMKHENVIGLLDVFTPATSIENFNEVylvtnL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTLKDFLRSMDPFpwQQKVRF-AKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRliveerkrapmek 487
Cdd:cd07878 102 MGADLNNIVKCQKLS--DEHVQFlIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR------------- 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  488 attkkrtlRKNDRKKRYtvVGNPYWMAPE-MLNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07878 167 --------QADDEMTGY--VATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELL 210
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
335-536 1.28e-09

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: 59.64  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGkvmvMKELIRCDEETQKTFLTEVKV-MRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTL 413
Cdd:cd14177  10 EDIGVGSYSVCKRCIHRATN----MEFAVKIIDKSKRDPSEEIEIlMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  414 KDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDK----TVVVADFGLSRLIveerkrapmekat 489
Cdd:cd14177  86 LDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQL------------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031869  490 tkkrtlrKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14177 153 -------RGENGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLL 192
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
331-594 1.30e-09

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: 59.42  E-value: 1.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  331 LIHGEVLGKGFFGQAIKVTHKATG------KVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLnLL 404
Cdd:cd05037   1 ITFHEHLGQGTFTNIYDGILREVGdgrvqeVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADENI-MV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  405 TEYIEGGTLKDFLRSMDPFPWQQ-KVRFAKGIASGMAYLHSMCIIHRDLNSHNCLI---KLDKTVV---VADFGLSR--L 475
Cdd:cd05037  80 QEYVRYGPLDKYLRRMGNNVPLSwKLQVAKQLASALHYLEDKKLIHGNVRGRNILLareGLDGYPPfikLSDPGVPItvL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  476 IVEER-KRAPmekattkkrtlrkndrkkrytvvgnpyWMAPEMLNG--KSYDETVDIFSFGIVLCEIIGQVYADPDCLPR 552
Cdd:cd05037 160 SREERvDRIP---------------------------WIAPECLRNlqANLTIAADKWSFGTTLWEICSGGEEPLSALSS 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031869  553 TldfglNVKLFWEK--FVPT-DCPPaFFPLAAICCRLEPESRPAF 594
Cdd:cd05037 213 Q-----EKLQFYEDqhQLPApDCAE-LAELIMQCWTYEPTKRPSF 251
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
327-540 1.52e-09

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 60.18  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  327 RPCDLihgEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKF--------------I 392
Cdd:cd07854   6 RYMDL---RPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVyevlgpsgsdltedV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  393 GVLYKDKKLNLLTEYIEggtlKDFLRSMD--PFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVV-VAD 469
Cdd:cd07854  83 GSLTELNSVYIVQEYME----TDLANVLEqgPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVLkIGD 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031869  470 FGLSRLiveerkrapMEKATTKKRTLRKNDRKKRYTvvgnpywmAPEM-LNGKSYDETVDIFSFGIVLCEII 540
Cdd:cd07854 159 FGLARI---------VDPHYSHKGYLSEGLVTKWYR--------SPRLlLSPNNYTKAIDMWAAGCIFAEML 213
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
159-239 1.60e-09

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 55.08  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869     159 TEGRRGFSVSVESACSNYattVQVKEVnrMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHD 238
Cdd:smart00228  10 GGGGLGFSLVGGKDEGGG---VVVSSV--VPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRG 84

                   .
gi 5031869     239 P 239
Cdd:smart00228  85 G 85
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
12-64 1.63e-09

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 53.86  E-value: 1.63e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869   12 CPGCGDHIAPSQIWYrTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDY 64
Cdd:cd09329   1 CAGCGQEIKNGQALL-ALDKQWHVWCFKCKECGKVLTGEYMGKDGKPYCERDY 52
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
383-597 1.63e-09

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 59.09  E-value: 1.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  383 LDHPNVLKF----IGVLYKDKKLNLLTEYIEGGTLKDFL-------RSMDPFPWQqkvRFAKGIASGMAYLHSmC---II 448
Cdd:cd13984  52 LDHPNIVKFhrywTDVQEEKARVIFITEYMSSGSLKQFLkktkknhKTMNEKSWK---RWCTQILSALSYLHS-CdppII 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  449 HRDLN------SHNCLIKLDKTvvvadfglsrliveerkrAPmekattkkRTLRkNDRKKRYTVVGNPYWMAPEMLNGKS 522
Cdd:cd13984 128 HGNLTcdtifiQHNGLIKIGSV------------------AP--------DAIH-NHVKTCREEHRNLHFFAPEYGYLED 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  523 YDETVDIFSFGIVLCEII--------GQVYADPDCLPRTLdFGL---NVKLFWEKfvptdcppaffplaaiCCRLEPESR 591
Cdd:cd13984 181 VTTAVDIYSFGMCALEMAaleiqsngEKVSANEEAIIRAI-FSLedpLQKDFIRK----------------CLSVAPQDR 243

                ....*.
gi 5031869  592 PAFSKL 597
Cdd:cd13984 244 PSARDL 249
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
332-536 2.00e-09

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 59.27  E-value: 2.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd14173   5 LQEEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLyQCQGHRNVLELIEFFEEEDKFYLVFEKMRG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVV---VADFGLSRLIVEERKRAPMEK 487
Cdd:cd14173  85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSpvkICDFDLGSGIKLNSDCSPIST 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031869  488 AttkkrtlrkndrkKRYTVVGNPYWMAPEMLNGKS-----YDETVDIFSFGIVL 536
Cdd:cd14173 165 P-------------ELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVIL 205
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
336-540 3.14e-09

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: 58.04  E-value: 3.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  336 VLGKGFFGQAIKVTHKatGKVMVMKelIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLnlLTEYIEGGTLkD 415
Cdd:cd14068   1 LLGDGGFGSVYRAVYR--GEDVAVK--IFNKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKGSL-D 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  416 FLRSMDPFPWQQKV--RFAKGIASGMAYLHSMCIIHRDLNSHNCL---IKLDKTVV--VADFGLSRLIVeerkrapmeka 488
Cdd:cd14068  74 ALLQQDNASLTRTLqhRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIIakIADYGIAQYCC----------- 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031869  489 ttkkrtlrkndRKKRYTVVGNPYWMAPEMLNGK-SYDETVDIFSFGIVLCEII 540
Cdd:cd14068 143 -----------RMGIKTSEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDIL 184
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
332-537 3.27e-09

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 57.99  E-value: 3.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  332 IHGEVlGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGG 411
Cdd:cd14108   6 IHKEI-GRGAFSYLRRVKEKSSDLSFAAK-FIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  412 TLKDFLRSmdPFPWQQKVR-FAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKT--VVVADFGlsrlivEERKRAPMEKa 488
Cdd:cd14108  84 LLERITKR--PTVCESEVRsYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFG------NAQELTPNEP- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031869  489 ttkkrtlrkndrkkRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIV--LC 537
Cdd:cd14108 155 --------------QYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIayLC 191
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
335-542 3.30e-09

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 59.29  E-value: 3.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKELiRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKKLNLLTEYIEG 410
Cdd:cd05625   7 KTLGIGAFGEVCLARKVDTKALYATKTL-RKKDVLLRNQVAHVKAERDIlaeaDNEWVVRLYYSFQDKDNLYFVMDYIPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  411 GTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLS---RLIVEER------- 480
Cdd:cd05625  86 GDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKyyqsgdh 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  481 -KRAPMEKATT----------------KKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCE-IIGQ 542
Cdd:cd05625 166 lRQDSMDFSNEwgdpencrcgdrlkplERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEmLVGQ 245
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
375-622 3.51e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 59.24  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   375 TEVKVMRSLDHPNVLKFIGVL-YKDKKLNLLTEYieGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLN 453
Cdd:PHA03212 132 TEAHILRAINHPSIIQLKGTFtYNKFTCLILPRY--KTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIK 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   454 SHNCLIKLDKTVVVADFGLSRLIVEerkrapmekattkkrtLRKNdrkKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFG 533
Cdd:PHA03212 210 AENIFINHPGDVCLGDFGAACFPVD----------------INAN---KYYGWAGTIATNAPELLARDPYGPAVDIWSAG 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869   534 IVLCEI-IGQ-VYADPDCLPRTLDFGLNVKLFWEKfvpTDCPPAFFPLAA----------ICCRL--EPESRPAFSKLED 599
Cdd:PHA03212 271 IVLFEMaTCHdSLFEKDGLDGDCDSDRQIKLIIRR---SGTHPNEFPIDAqanldeiyigLAKKSsrKPGSRPLWTNLYE 347
                        250       260
                 ....*....|....*....|...
gi 5031869   600 sfealslylgelgipLPAELEEL 622
Cdd:PHA03212 348 ---------------LPIDLEYL 355
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
335-536 3.66e-09

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 58.32  E-value: 3.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  335 EVLGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLT------EVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYI 408
Cdd:cd14094   9 EVIGKGPFSVVRRCIHRETGQQFAVK-IVDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGMLYMVFEFM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031869  409 EGGTL--KDFLRSMDPFPWQQKV--RFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKT---VVVADFGLSrliveerK 481
Cdd:cd14094  88 DGADLcfEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA-------I 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869  482 RAPMEKATTKKRtlrkndrkkrytvVGNPYWMAPEMLNGKSYDETVDIFSFGIVL 536
Cdd:cd14094 161 QLGESGLVAGGR-------------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 202
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
72-125 8.15e-08

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 48.85  E-value: 8.15e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869   72 CHGCSLLMTGPFMV-AGEFKYHPECFACMSCKVIIEDGDAYalVQHATLYCGKCH 125
Cdd:cd08368   1 CAGCGKPIEGRELLrALGKKWHPECFKCAECGKPLGGDSFY--EKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
72-125 2.31e-07

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 47.71  E-value: 2.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869     72 CHGCSLLMTGPFMV-AGEFKYHPECFACMSCKVIIEDGDAYalVQHATLYCGKCH 125
Cdd:pfam00412   1 CAGCNRPIYDRELVrALGKVWHPECFRCAVCGKPLTTGDFY--EKDGKLYCKHDY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
72-124 2.33e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 45.07  E-value: 2.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 5031869      72 CHGCSLLMTG--PFMVAGEFKYHPECFACMSCKVIIEDGDAYalVQHATLYCGKC 124
Cdd:smart00132   2 CAGCGKPIYGteRVLRALGKVWHPECFKCATCGKPLSGDTFF--EKDGKLYCKDC 54
 
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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