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Conserved domains on  [gi|578806145|ref|XP_005265227|]
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macrophage-stimulating protein receptor isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_RON cd11279
The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor ...
27-523 0e+00

The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a wide range of effects, including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. RON has been implicated in cancers of the breast, colon, pancreas and ovaries because both splice variants and receptor overexpression have been identified in these tumors. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as ligand recognition and binding model. RON is 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 tyrosine kinase domain. The Sema domain of RON may be necessary for receptor dimerization and activation.


:

Pssm-ID: 200540 [Multi-domain]  Cd Length: 493  Bit Score: 859.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   27 WQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDrneSAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAA 106
Cdd:cd11279     1 WQCPRIPYALTRNFSVKYVVPSFSAGSPIQNIVSYEDA---SAVFVATRNHLHVLNPELKLLQNLVTGPTGSPGCQICAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  107 CGPGPHGPPG-DTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTR 185
Cdd:cd11279    78 CPPGPPGPSPeDTDNKVLVLDPEEPWLYSCGSSLHGRCFLHELESRGSAVHIASTACLFSANANKPSDCPDCVASPLGTR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  186 VTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQ 265
Cdd:cd11279   158 VTVVEQSHTSYFYVASTLNSSVAASYSPRSVSIRRLKSDQDGFAPGFHSLTVLPKYLDSYPIHYVHSFTSGDFVYFLTVQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  266 PASVtdDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEG-GQPYPVLRVAHSAPVGAQLATELSIAEGQE 344
Cdd:cd11279   238 PESP--DSSAYHTRLVRLSAKEPELRDYRELVLDCRFEPKRRRRRRPAErEVPYNVLQAAHAAPVGSKLAVELGISEGQE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  345 VLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRH 424
Cdd:cd11279   316 VLFGVFAESQPGSPVPQKNSAVCAFPISLLNEAIDEGMEKCCSSSNSDRLFRGLDFFQPQSYCPHPPNLSAAVSNTSCWN 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  425 FPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDsGQPVQRDVSR 504
Cdd:cd11279   396 FPTLVSTSSFRVDLFNGHLSGVLLTSIYVTVLDNVTVAHLGTSDGRILQVVLQRSLNYLLYVSNFSLGD-GQPVQRDVSR 474
                         490
                  ....*....|....*....
gi 578806145  505 LGDHLLFASGDQVFQVPIQ 523
Cdd:cd11279   475 LGDSLLFASGNQVFKVNIT 493
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
1087-1348 0e+00

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: 547.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC 1166
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVVLPYMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHR 1246
Cdd:cd05058    81 HGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNHT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05058   161 GAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                         250       260
                  ....*....|....*....|..
gi 578806145 1327 ADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05058   241 PKPEMRPTFSELVSRISQIFST 262
IPT_plexin_repeat2 cd01179
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
684-768 9.91e-32

Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


:

Pssm-ID: 238584  Cd Length: 85  Bit Score: 119.25  E-value: 9.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWT 763
Cdd:cd01179     1 PSITSLSPSYGPQSGGTRLTITGKHLNAGSSVRVTVGGQPCKILSVSSSQIVCLTPPSASPGEAPVKVLIDGARRLAPLV 80

                  ....*
gi 578806145  764 FQYRE 768
Cdd:cd01179    81 FTYTE 85
IPT_plexin_repeat1 cd01180
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
569-683 8.68e-28

First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


:

Pssm-ID: 238585  Cd Length: 94  Bit Score: 108.17  E-value: 8.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  569 PKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSglvpEGTHQVTVGQSPCRPLPkdssklrpvPRKDFVEEFECELEPLGTQ 648
Cdd:cd01180     1 PVITEFFPLSGPLEGGTRLTICGSNLGLRKN----DVRHGVRVGGVPCNPEP---------PEYSSSEKIVCTTGPAGNP 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578806145  649 aVGPTNVSLTVTNMPpgkhfrvDGTSVLRGFSFME 683
Cdd:cd01180    68 -VFNGPVEVTVGHGS-------FRTESSEGFSFVD 94
IPT smart00429
ig-like, plexins, transcription factors;
769-860 4.03e-08

ig-like, plexins, transcription factors;


:

Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 52.04  E-value: 4.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    769 DPVVLSISPNCGYI--NSHITICGQHLTSAWHLVLSFHDGlraveSRQCERQL--PEQQLCRLPEYvvrdPQGWVAGNLS 844
Cdd:smart00429    1 DPVITRISPTSGPVsgGTEITLCGKNLKSISVVFVEVGVG-----EAPCTFSPssSTAIVCKTPPY----HNIPGSVPVR 71
                            90
                    ....*....|....*.
gi 578806145    845 ARGDGAAGFTLPGFRF 860
Cdd:smart00429   72 TVGLRNGGVPSSPQPF 87
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
526-568 1.48e-06

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 46.55  E-value: 1.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578806145   526 GCRHFLTCGRCLRAWhFMGCGWC--GNMCGQQKECPG------SWQQDH--CP 568
Cdd:pfam01437    1 RCSQYTSCSSCLAAR-DPYCGWCssEGRCVRRSACGApegnceEWEQASskCP 52
 
Name Accession Description Interval E-value
Sema_RON cd11279
The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor ...
27-523 0e+00

The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a wide range of effects, including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. RON has been implicated in cancers of the breast, colon, pancreas and ovaries because both splice variants and receptor overexpression have been identified in these tumors. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as ligand recognition and binding model. RON is 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 tyrosine kinase domain. The Sema domain of RON may be necessary for receptor dimerization and activation.


Pssm-ID: 200540 [Multi-domain]  Cd Length: 493  Bit Score: 859.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   27 WQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDrneSAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAA 106
Cdd:cd11279     1 WQCPRIPYALTRNFSVKYVVPSFSAGSPIQNIVSYEDA---SAVFVATRNHLHVLNPELKLLQNLVTGPTGSPGCQICAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  107 CGPGPHGPPG-DTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTR 185
Cdd:cd11279    78 CPPGPPGPSPeDTDNKVLVLDPEEPWLYSCGSSLHGRCFLHELESRGSAVHIASTACLFSANANKPSDCPDCVASPLGTR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  186 VTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQ 265
Cdd:cd11279   158 VTVVEQSHTSYFYVASTLNSSVAASYSPRSVSIRRLKSDQDGFAPGFHSLTVLPKYLDSYPIHYVHSFTSGDFVYFLTVQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  266 PASVtdDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEG-GQPYPVLRVAHSAPVGAQLATELSIAEGQE 344
Cdd:cd11279   238 PESP--DSSAYHTRLVRLSAKEPELRDYRELVLDCRFEPKRRRRRRPAErEVPYNVLQAAHAAPVGSKLAVELGISEGQE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  345 VLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRH 424
Cdd:cd11279   316 VLFGVFAESQPGSPVPQKNSAVCAFPISLLNEAIDEGMEKCCSSSNSDRLFRGLDFFQPQSYCPHPPNLSAAVSNTSCWN 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  425 FPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDsGQPVQRDVSR 504
Cdd:cd11279   396 FPTLVSTSSFRVDLFNGHLSGVLLTSIYVTVLDNVTVAHLGTSDGRILQVVLQRSLNYLLYVSNFSLGD-GQPVQRDVSR 474
                         490
                  ....*....|....*....
gi 578806145  505 LGDHLLFASGDQVFQVPIQ 523
Cdd:cd11279   475 LGDSLLFASGNQVFKVNIT 493
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
1087-1348 0e+00

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: 547.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC 1166
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVVLPYMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHR 1246
Cdd:cd05058    81 HGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNHT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05058   161 GAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                         250       260
                  ....*....|....*....|..
gi 578806145 1327 ADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05058   241 PKPEMRPTFSELVSRISQIFST 262
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1086-1339 6.52e-123

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 382.26  E-value: 6.52e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1086 DRVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:smart00219    4 GKKLGEGAFGEVYKGKLKGKGGKkKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPL-YIVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVqq 1244
Cdd:smart00219   83 MEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK-- 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1245 hRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:smart00219  161 -RGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQC 239
                           250
                    ....*....|....*
gi 578806145   1325 WEADPAVRPTFRVLV 1339
Cdd:smart00219  240 WAEDPEDRPTFSELV 254
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1086-1339 3.78e-122

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: 380.30  E-value: 3.78e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1086 DRVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglPH-VLLP 1163
Cdd:pfam07714    4 GEKLGEGAFGEVYKGTLKGEGENtKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGE--PLyIVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1164 YMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYsvQ 1243
Cdd:pfam07714   82 YMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYY--R 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1244 QHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQ 1323
Cdd:pfam07714  160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQ 239
                          250
                   ....*....|....*.
gi 578806145  1324 CWEADPAVRPTFRVLV 1339
Cdd:pfam07714  240 CWAYDPEDRPTFSELV 255
Sema smart00630
semaphorin domain;
64-499 4.85e-79

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 266.54  E-value: 4.85e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145     64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPgcQTCAACGPGPHGPPGDTDTKVLVL-DPALPALVSCGS-SLQG 141
Cdd:smart00630    7 DEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSS--PDCEECVSKGKDPPTDCVNYIRLLlDYNEDRLLVCGTnAFQP 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    142 RCFLHDLEpqgtavhlaapaclfsahhnrpddcpdcvasplgtrvtvveqgqasYFYVASSLDAAVAASFSPRSVSIRRL 221
Cdd:smart00630   85 VCRLRNLG----------------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRL 118
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    222 KADAsgfapGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTD-DPSALHTRLARL--------SATEPELGD 292
Cdd:smart00630  119 KGTS-----GVSLRTVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVckndvggpRSLDKKWTS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    293 YRELVLDCRFapkrrrrgAPEGGQPYPVLRVAHSAPVGaqlatelsiAEGQEVLFGVFVTgkdgGPGVGPNSVVCAFPID 372
Cdd:smart00630  194 FLKARLECSV--------PGEDPFYFNELQAAFLLPPG---------SESDDVLYGVFST----SSNPIPGSAVCAFSLS 252
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    373 LLDTLIDEGVERCCESPV-HPGLRRGLDFFQSPSFCPNPPGLEALSP----NTSCRHF-PLLVSSSFSRVDLFNGLLGPV 446
Cdd:smart00630  253 DINAVFNGPFKECETSTSqWLPYSRGKVPYPRPGTCPNKPPSSKDLPdetlNFIKSHPlMDEVVQPLTGRPLFVKTDSNY 332
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145    447 QVTALYVTRLD---NVTVAHMGTMDGRILQVELVRSLNY--LLYVSNFSLGDSGQPVQ 499
Cdd:smart00630  333 LLTSIAVDRVAtdgNYTVLFLGTSDGRILKVVLSESSSSseSVVLEEISVFPDGSPIS 390
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1087-1333 4.26e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 132.06  E-value: 4.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRiQCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGImLPPEGLPHVLLPY 1164
Cdd:COG0515    13 RLLGRGGMGVVYLAR--DLRLGR-PVALKVLrpELAADPEARERFRREARALARLNHPNIVRVYDV-GEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRnPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysVQQ 1244
Cdd:COG0515    89 VEGESLADLLRRRGP-LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGAT---LTQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPD---SLYQVM 1321
Cdd:COG0515   165 TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSELRPDlppALDAIV 243
                         250
                  ....*....|..
gi 578806145 1322 QQCWEADPAVRP 1333
Cdd:COG0515   244 LRALAKDPEERY 255
IPT_plexin_repeat2 cd01179
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
684-768 9.91e-32

Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238584  Cd Length: 85  Bit Score: 119.25  E-value: 9.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWT 763
Cdd:cd01179     1 PSITSLSPSYGPQSGGTRLTITGKHLNAGSSVRVTVGGQPCKILSVSSSQIVCLTPPSASPGEAPVKVLIDGARRLAPLV 80

                  ....*
gi 578806145  764 FQYRE 768
Cdd:cd01179    81 FTYTE 85
IPT_plexin_repeat1 cd01180
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
569-683 8.68e-28

First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238585  Cd Length: 94  Bit Score: 108.17  E-value: 8.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  569 PKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSglvpEGTHQVTVGQSPCRPLPkdssklrpvPRKDFVEEFECELEPLGTQ 648
Cdd:cd01180     1 PVITEFFPLSGPLEGGTRLTICGSNLGLRKN----DVRHGVRVGGVPCNPEP---------PEYSSSEKIVCTTGPAGNP 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578806145  649 aVGPTNVSLTVTNMPpgkhfrvDGTSVLRGFSFME 683
Cdd:cd01180    68 -VFNGPVEVTVGHGS-------FRTESSEGFSFVD 94
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
321-502 1.67e-26

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 107.74  E-value: 1.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   321 LRVAHSAPVGAQLATElsiaegqEVLFGVFVTGKDGGPGvgpNSVVCAFPIDLLDTLIdEGVERCCESPVHPGLRR-GLD 399
Cdd:pfam01403    1 LQDVFVLKPGAGDALD-------TVLYGVFTTQWSNSIG---GSAVCAFSLSDINAVF-EGPFKEQEKSDSKWLPYtGKV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   400 FFQSPSFCPNPPGLEALSPNTSC--RHFPLLVSS--SFSRVDLFNGLLgpVQVTALYVTRLD----NVTVAHMGTMDGRI 471
Cdd:pfam01403   70 PYPRPGTCINDPLRLDLPDSVLNfvKDHPLMDEAvqPVGGRPLLVRTG--VRLTSIAVDRVQaldgNYTVLFLGTDDGRL 147
                          170       180       190
                   ....*....|....*....|....*....|.
gi 578806145   472 LQVELVRSlNYLLYVSNFSLGDSGQPVQRDV 502
Cdd:pfam01403  148 HKVVLVGS-EESHIIEEIQVFPEPQPVLNLL 177
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1089-1305 7.06e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 83.71  E-value: 7.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVY------HGEYIdqaqnriqcAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALI-GIMlpPEGLPH 1159
Cdd:PTZ00263   26 LGTGSFGRVRiakhkgTGEYY---------AIKCLKKreILKMKQVQHVAQEKSILMELSHPFIVNMMcSFQ--DENRVY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRSPQRNPTvkDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE 1238
Cdd:PTZ00263   95 FLLEFVVGGELFTHLRKAGRFPN--DVAKFyHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRT 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1239 YYSVQQhrharlPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR 1305
Cdd:PTZ00263  173 FTLCGT------P-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPFFDDTPFRIYEKILAGR 231
IPT smart00429
ig-like, plexins, transcription factors;
683-767 6.04e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 65.90  E-value: 6.04e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    683 EPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN--GTECLLARVSEGQLLCATPPGAT-VASVPLS-LQVGGAQV 758
Cdd:smart00429    1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGvgEAPCTFSPSSSTAIVCKTPPYHNiPGSVPVRtVGLRNGGV 80
                            90
                    ....*....|
gi 578806145    759 PGS-WTFQYR 767
Cdd:smart00429   81 PSSpQPFTYV 90
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1086-1289 8.14e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.82  E-value: 8.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEyiDQAQNRIQcAIKSLSriTEMQQ----VEAFLREGLLMRGLNHPNVLAligimlppeglphVL 1161
Cdd:NF033483   12 GERIGRGGMAEVYLAK--DTRLDRDV-AVKVLR--PDLARdpefVARFRREAQSAASLSHPNIVS-------------VY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 -------LPYMC----HG-DLLQFIRSpqRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADF 1228
Cdd:NF033483   74 dvgedggIPYIVmeyvDGrTLKDYIRE--HGPlSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1229 GLAR-----------DILDreyySVQ-----QHRHArlpvkwMAleslqtyrfTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:NF033483  152 GIARalssttmtqtnSVLG----TVHylspeQARGG------TV---------DARSDIYSLGIVLYEMLT-GRPPF 208
IPT smart00429
ig-like, plexins, transcription factors;
568-627 5.62e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 60.13  E-value: 5.62e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    568 PPKLTEFHPHSGPLRGSTRLTLCGSNFylhpsGLVPEGTHQVTVGQSPCRPLPKDSSKLR 627
Cdd:smart00429    1 DPVITRISPTSGPVSGGTEITLCGKNL-----KSISVVFVEVGVGEAPCTFSPSSSTAIV 55
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
684-766 1.75e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 58.61  E-value: 1.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRA-VLVNGTECLLARVSEGQLLCATPPGATvASVPLSLQVGGAQ-VPGS 761
Cdd:pfam01833    1 PVITSISPSSGPASGGTTITITGSNFGTDSSDLkVTIGGTPCTVISVSSTTIVCTTPPGTS-GLVNVSVTVGGGGiSSSP 79

                   ....*
gi 578806145   762 WTFQY 766
Cdd:pfam01833   80 LTFTY 84
IPT smart00429
ig-like, plexins, transcription factors;
769-860 4.03e-08

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 52.04  E-value: 4.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    769 DPVVLSISPNCGYI--NSHITICGQHLTSAWHLVLSFHDGlraveSRQCERQL--PEQQLCRLPEYvvrdPQGWVAGNLS 844
Cdd:smart00429    1 DPVITRISPTSGPVsgGTEITLCGKNLKSISVVFVEVGVG-----EAPCTFSPssSTAIVCKTPPY----HNIPGSVPVR 71
                            90
                    ....*....|....*.
gi 578806145    845 ARGDGAAGFTLPGFRF 860
Cdd:smart00429   72 TVGLRNGGVPSSPQPF 87
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
526-568 1.48e-06

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 46.55  E-value: 1.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578806145   526 GCRHFLTCGRCLRAWhFMGCGWC--GNMCGQQKECPG------SWQQDH--CP 568
Cdd:pfam01437    1 RCSQYTSCSSCLAAR-DPYCGWCssEGRCVRRSACGApegnceEWEQASskCP 52
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
526-568 2.30e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 45.61  E-value: 2.30e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578806145    526 GCRHFLTCGRCLRAWHFmGCGWC--GNMCGQQKECPGS---WQQDHCP 568
Cdd:smart00423    1 RCSKYTSCSECLLARDP-YCAWCssQGRCTSGERCDSRrqnWLSGGCP 47
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
770-862 9.44e-05

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 42.45  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  770 PVVLSISPNCGYIN--SHITICGQHLTSAWHLVLSFHDGLRAVESRQCERQLpeqqLCRLPEYvvrDPQGWVAGNLSARG 847
Cdd:cd00102     1 PVITSISPSSGPVSggTEVTITGSNFGSGSNLRVTFGGGVPCSVLSVSSTAI----VCTTPPY---ANPGPGPVEVTVDR 73
                          90
                  ....*....|....*.
gi 578806145  848 DGAAGFTLP-GFRFLP 862
Cdd:cd00102    74 GNGGITSSPlTFTYVP 89
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
569-661 1.29e-04

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 42.05  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   569 PKLTEFHPHSGPLRGSTRLTLCGSNFylhpsGLVPEGThQVTVGQSPCRPLPKDSSKLRpvprkdfveefeCELEPLgtq 648
Cdd:pfam01833    1 PVITSISPSSGPASGGTTITITGSNF-----GTDSSDL-KVTIGGTPCTVISVSSTTIV------------CTTPPG--- 59
                           90
                   ....*....|...
gi 578806145   649 AVGPTNVSLTVTN 661
Cdd:pfam01833   60 TSGLVNVSVTVGG 72
 
Name Accession Description Interval E-value
Sema_RON cd11279
The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor ...
27-523 0e+00

The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a wide range of effects, including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. RON has been implicated in cancers of the breast, colon, pancreas and ovaries because both splice variants and receptor overexpression have been identified in these tumors. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as ligand recognition and binding model. RON is 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 tyrosine kinase domain. The Sema domain of RON may be necessary for receptor dimerization and activation.


Pssm-ID: 200540 [Multi-domain]  Cd Length: 493  Bit Score: 859.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   27 WQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDrneSAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAA 106
Cdd:cd11279     1 WQCPRIPYALTRNFSVKYVVPSFSAGSPIQNIVSYEDA---SAVFVATRNHLHVLNPELKLLQNLVTGPTGSPGCQICAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  107 CGPGPHGPPG-DTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTR 185
Cdd:cd11279    78 CPPGPPGPSPeDTDNKVLVLDPEEPWLYSCGSSLHGRCFLHELESRGSAVHIASTACLFSANANKPSDCPDCVASPLGTR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  186 VTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQ 265
Cdd:cd11279   158 VTVVEQSHTSYFYVASTLNSSVAASYSPRSVSIRRLKSDQDGFAPGFHSLTVLPKYLDSYPIHYVHSFTSGDFVYFLTVQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  266 PASVtdDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEG-GQPYPVLRVAHSAPVGAQLATELSIAEGQE 344
Cdd:cd11279   238 PESP--DSSAYHTRLVRLSAKEPELRDYRELVLDCRFEPKRRRRRRPAErEVPYNVLQAAHAAPVGSKLAVELGISEGQE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  345 VLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRH 424
Cdd:cd11279   316 VLFGVFAESQPGSPVPQKNSAVCAFPISLLNEAIDEGMEKCCSSSNSDRLFRGLDFFQPQSYCPHPPNLSAAVSNTSCWN 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  425 FPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDsGQPVQRDVSR 504
Cdd:cd11279   396 FPTLVSTSSFRVDLFNGHLSGVLLTSIYVTVLDNVTVAHLGTSDGRILQVVLQRSLNYLLYVSNFSLGD-GQPVQRDVSR 474
                         490
                  ....*....|....*....
gi 578806145  505 LGDHLLFASGDQVFQVPIQ 523
Cdd:cd11279   475 LGDSLLFASGNQVFKVNIT 493
Sema_MET_like cd11248
The Sema domain, a protein interacting module, of MET and RON receptor tyrosine kinases; This ...
46-523 0e+00

The Sema domain, a protein interacting module, of MET and RON receptor tyrosine kinases; This family includes MET and RON receptor tyrosine kinases. MET is encoded by the c-met protooncogene. MET is the receptor for hepatocyte growth factor/scatter factor (HGF/SF). HGF/SF and MET regulates multiple cellular events and are essential for the development of several tissues and organs, including the placenta, liver, and several groups of skeletal muscles. RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a variety of effects including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. MET and RON receptors have been implicated in cancer development and migration. They are composed of alpha-beta heterodimers. 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 tyrosine kinase domain. The Sema domain is necessary for receptor dimerization and activation.


Pssm-ID: 200509 [Multi-domain]  Cd Length: 467  Bit Score: 575.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   46 VPSFSAGGLVQAMVTYEGdrnESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHG-PPGDTDTKVLV 124
Cdd:cd11248     1 LPFFTADTPIQNIVLNEG---STEVYVAAQNVIYALNPDLQKVWEYKTGPVGSPDCQTCQDCSSGADPgVPKDTDNMVLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  125 LDPAL-PALVSCGSSLQGRCFLHDLEPqgTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSL 203
Cdd:cd11248    78 LETYYdDYLYSCGSTQNGVCYRHVLED--GADIQSEVHCLFSKKNNSPSYCPDCVASPLGTKVTNVESGRTIYFFVANSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  204 DAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARL 283
Cdd:cd11248   156 NSSLAGSFPPHSISVRRLKEDGFGFLSDQSYLDVLPSLRDSYPIKYVYSFHSGPFVYFLTVQRESLTKPSSAFHTRLVRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  284 SATEPELGDYRELVLDCRFAPKRRRRGAPEgGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPN 363
Cdd:cd11248   236 CSSDSEIWRYREMPLECIFTPKRRRRSTEE-DVVYNVLQAAHVSKVGADLADELGASEGDDILFGVFARSKPDSGEPMPN 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  364 SVVCAFPIDLLDTLIDEGVERCCESPVHPgLRRGLDFFQspsFCPNPPGlEALSPNTSCRHFPLLVSSSFSRVDLFNGLL 443
Cdd:cd11248   315 SALCAFPIKYVNDAIEKGVEKCCTSGLEH-FSGSLCHFQ---PCPTCPG-ESSSCEATCKEYRTEVTKPYQRVDLFNGQM 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  444 GPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNylLYVSNFSLGdsGQPVQRDVSRLG--DHLLFASGDQVFQVP 521
Cdd:cd11248   390 SNVLLTSILVTTIGNHTVAHLGTSDGRVLQVVLSRSGP--IPHVNFSLD--SQPVSREVAVLSsnGSLLFVTGDKITKVP 465

                  ..
gi 578806145  522 IQ 523
Cdd:cd11248   466 LI 467
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
1087-1348 0e+00

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: 547.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC 1166
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVVLPYMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHR 1246
Cdd:cd05058    81 HGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNHT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05058   161 GAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                         250       260
                  ....*....|....*....|..
gi 578806145 1327 ADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05058   241 PKPEMRPTFSELVSRISQIFST 262
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1086-1339 6.52e-123

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 382.26  E-value: 6.52e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1086 DRVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:smart00219    4 GKKLGEGAFGEVYKGKLKGKGGKkKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPL-YIVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVqq 1244
Cdd:smart00219   83 MEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK-- 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1245 hRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:smart00219  161 -RGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQC 239
                           250
                    ....*....|....*
gi 578806145   1325 WEADPAVRPTFRVLV 1339
Cdd:smart00219  240 WAEDPEDRPTFSELV 254
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1086-1339 3.78e-122

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: 380.30  E-value: 3.78e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1086 DRVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglPH-VLLP 1163
Cdd:pfam07714    4 GEKLGEGAFGEVYKGTLKGEGENtKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGE--PLyIVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1164 YMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYsvQ 1243
Cdd:pfam07714   82 YMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYY--R 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1244 QHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQ 1323
Cdd:pfam07714  160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQ 239
                          250
                   ....*....|....*.
gi 578806145  1324 CWEADPAVRPTFRVLV 1339
Cdd:pfam07714  240 CWAYDPEDRPTFSELV 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1086-1339 7.72e-122

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 379.59  E-value: 7.72e-122
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1086 DRVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:smart00221    4 GKKLGEGAFGEVYKGTLKGKGDGkEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPL-MIVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1165 MCHGDLLQFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVq 1243
Cdd:smart00221   83 MPGGDLLDYLRKNRPKElSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKV- 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1244 qhRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQ 1323
Cdd:smart00221  162 --KGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQ 239
                           250
                    ....*....|....*.
gi 578806145   1324 CWEADPAVRPTFRVLV 1339
Cdd:smart00221  240 CWAEDPEDRPTFSELV 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1087-1339 2.51e-115

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: 362.24  E-value: 2.51e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPL-YLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQR--------NPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE 1238
Cdd:cd00192    80 GGDLLDFLRKSRPvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLY 1318
Cdd:cd00192   160 YY--RKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELY 237
                         250       260
                  ....*....|....*....|.
gi 578806145 1319 QVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd00192   238 ELMLSCWQLDPEDRPTFSELV 258
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1087-1346 3.94e-83

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: 273.64  E-value: 3.94e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLS-RITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGL-----PHV 1160
Cdd:cd05035     5 KILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKvDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppsPMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSPQ-----RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL 1235
Cdd:cd05035    85 ILPFMKHGDLHSYLLYSRlgglpEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 DREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPD 1315
Cdd:cd05035   165 SGDYY--RQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRLKQPEDCLD 242
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578806145 1316 SLYQVMQQCWEADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd05035   243 EVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
Sema smart00630
semaphorin domain;
64-499 4.85e-79

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 266.54  E-value: 4.85e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145     64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPgcQTCAACGPGPHGPPGDTDTKVLVL-DPALPALVSCGS-SLQG 141
Cdd:smart00630    7 DEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSS--PDCEECVSKGKDPPTDCVNYIRLLlDYNEDRLLVCGTnAFQP 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    142 RCFLHDLEpqgtavhlaapaclfsahhnrpddcpdcvasplgtrvtvveqgqasYFYVASSLDAAVAASFSPRSVSIRRL 221
Cdd:smart00630   85 VCRLRNLG----------------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRL 118
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    222 KADAsgfapGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTD-DPSALHTRLARL--------SATEPELGD 292
Cdd:smart00630  119 KGTS-----GVSLRTVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVckndvggpRSLDKKWTS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    293 YRELVLDCRFapkrrrrgAPEGGQPYPVLRVAHSAPVGaqlatelsiAEGQEVLFGVFVTgkdgGPGVGPNSVVCAFPID 372
Cdd:smart00630  194 FLKARLECSV--------PGEDPFYFNELQAAFLLPPG---------SESDDVLYGVFST----SSNPIPGSAVCAFSLS 252
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    373 LLDTLIDEGVERCCESPV-HPGLRRGLDFFQSPSFCPNPPGLEALSP----NTSCRHF-PLLVSSSFSRVDLFNGLLGPV 446
Cdd:smart00630  253 DINAVFNGPFKECETSTSqWLPYSRGKVPYPRPGTCPNKPPSSKDLPdetlNFIKSHPlMDEVVQPLTGRPLFVKTDSNY 332
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145    447 QVTALYVTRLD---NVTVAHMGTMDGRILQVELVRSLNY--LLYVSNFSLGDSGQPVQ 499
Cdd:smart00630  333 LLTSIAVDRVAtdgNYTVLFLGTSDGRILKVVLSESSSSseSVVLEEISVFPDGSPIS 390
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
1071-1345 1.61e-77

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: 257.92  E-value: 1.61e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1071 VKDVLIPhERVVTHSdRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSL-SRITEMQQVEAFLREGLLMRGLNHPNVLALIG 1149
Cdd:cd05074     1 LKDVLIQ-EQQFTLG-RMLGKGEFGSVREAQLKSEDGSFQKVAVKMLkADIFSSSDIEEFLREAACMKEFDHPNVIKLIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1150 IML--PPEG---LPHVLLPYMCHGDLLQFIRSPQ--RNP---TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDE 1219
Cdd:cd05074    79 VSLrsRAKGrlpIPMVILPFMKHGDLHTFLLMSRigEEPftlPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1220 SFTVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTH 1299
Cdd:cd05074   159 NMTVCVADFGLSKKIYSGDYY--RQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYN 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1300 FLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05074   237 YLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1076-1350 1.71e-77

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: 257.66  E-value: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVvtHSDRVIGKGHFGVVYHG--EYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLP 1153
Cdd:cd05032     3 LPREKI--TLIRELGQGSFGMVYEGlaKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1154 pEGLPHVLLPYMCHGDLLQFIRS---------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVK 1224
Cdd:cd05032    81 -GQPTLVVMELMAKGDLKSYLRSrrpeaennpGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1225 VADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQG 1304
Cdd:cd05032   160 IGDFGMTRDIYETDYY--RKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDG 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1305 RRLPQPEYCPDSLYQVMQQCWEADPAVRPTFrvlvgevEQIVSALL 1350
Cdd:cd05032   238 GHLDLPENCPDKLLELMRMCWQYNPKMRPTF-------LEIVSSLK 276
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1087-1343 1.86e-77

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: 257.35  E-value: 1.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYID---QAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglPH-VLL 1162
Cdd:cd05044     1 KFLGSGAFGEVFEGTAKDilgDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDND--PQyIIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRS--PQRNP----TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDES----FTVKVADFGLAR 1232
Cdd:cd05044    79 ELMEGGDLLSYLRAarPTAFTppllTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKdyreRVVKIGDFGLAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1233 DILDREYYSVQQHRhaRLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEY 1312
Cdd:cd05044   159 DIYKNDYYRKEGEG--LLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDN 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578806145 1313 CPDSLYQVMQQCWEADPAVRPTFRVLVGEVE 1343
Cdd:cd05044   237 CPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
1088-1339 6.34e-77

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: 256.22  E-value: 6.34e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCH 1167
Cdd:cd05043    13 LLQEGTFGRIFHGILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDGEKPMVLYPYMNW 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNP-------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYY 1240
Cdd:cd05043    93 GNLKLFLQQCRLSEannpqalSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPMDYH 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SV--QQHRharlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLY 1318
Cdd:cd05043   173 CLgdNENR----PIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPINCPDELF 248
                         250       260
                  ....*....|....*....|.
gi 578806145 1319 QVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd05043   249 AVMACCWALDPEERPSFQQLV 269
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
1076-1347 1.05e-76

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: 256.19  E-value: 1.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVVThsDRVIGKGHFGVVYHGEYID---QAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALIGIm 1151
Cdd:cd05053     9 LPRDRLTL--GKPLGEGAFGQVVKAEAVGldnKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGA- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1152 LPPEGLPHVLLPYMCHGDLLQFIRS---------------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCM 1216
Cdd:cd05053    86 CTQDGPLYVVVEYASKGNLREFLRArrppgeeaspddprvPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1217 LDESFTVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFD 1296
Cdd:cd05053   166 VTEDNVMKIADFGLARDIHHIDYY--RKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1297 LTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVS 1347
Cdd:cd05053   244 LFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRILT 294
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1089-1335 2.19e-76

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: 253.81  E-value: 2.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIML-PPEGLPHVLLPymcH 1167
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKgEPLMLVMELAP---L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQQHr 1246
Cdd:cd05060    80 GPLLKYLKK-RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALgAGSDYYRATTA- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 hARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05060   158 -GRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSIMLSCWK 236

                  ....*....
gi 578806145 1327 ADPAVRPTF 1335
Cdd:cd05060   237 YRPEDRPTF 245
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
1087-1349 2.82e-76

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: 254.16  E-value: 2.82e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyIDQAQNRIQCAIKSLS-RITEMQQVEAFLREGLLMRGLNHPNVLALIGIML---PPEGLPH--V 1160
Cdd:cd05075     6 KTLGEGEFGSVMEGQ-LNQDDSVLKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLqntESEGYPSpvV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFI------RSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI 1234
Cdd:cd05075    85 ILPFMKHGDLHSFLlysrlgDCPVYLPT-QMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 LDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCP 1314
Cdd:cd05075   164 YNGDYY--RQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPPDCL 241
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578806145 1315 DSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd05075   242 DGLYELMSSCWLLNPKDRPSFETLRCELEKILKDL 276
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1087-1343 4.57e-76

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: 252.59  E-value: 4.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITeMQqVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05034     1 KKLGAGQFGEVWMGVW----NGTTKVAVKTLKPGT-MS-PEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPI-YIVTELMS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQ-RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSvqqH 1245
Cdd:cd05034    74 KGSLLDYLRTGEgRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTA---R 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd05034   151 EGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCW 230
                         250
                  ....*....|....*...
gi 578806145 1326 EADPAVRPTFRVLVGEVE 1343
Cdd:cd05034   231 KKEPEERPTFEYLQSFLE 248
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1089-1345 1.03e-73

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: 246.11  E-value: 1.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQQveAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd05039    14 IGKGEFGDVMLGDYRGQ-----KVAVKCLKDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLEGNGL-YIVTEYMAKG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDildreyySVQQHRH 1247
Cdd:cd05039    86 SLVDYLRSRGRAViTRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE-------ASSNQDG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 ARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd05039   159 GKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPEGCPPEVYKVMKNCWEL 238
                         250
                  ....*....|....*...
gi 578806145 1328 DPAVRPTFRVLVGEVEQI 1345
Cdd:cd05039   239 DPAKRPTFKQLREKLEHI 256
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
1073-1349 2.13e-73

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: 246.38  E-value: 2.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1073 DVLIphERVVTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQ-QVEAFLREGLLMRGLNHPNVLALIGIM 1151
Cdd:cd14204     1 DVMI--DRNLLSLGKVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKLDNFSQrEIEEFLSEAACMKDFNHPNVIRLLGVC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1152 LP--PEGLPH--VLLPYMCHGDLLQFIRS------PQRNPtVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF 1221
Cdd:cd14204    79 LEvgSQRIPKpmVILPFMKYGDLHSFLLRsrlgsgPQHVP-LQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1222 TVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFL 1301
Cdd:cd14204   158 TVCVADFGLSKKIYSGDYY--RQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1302 AQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd14204   236 LHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESL 283
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
1078-1346 4.17e-73

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: 245.37  E-value: 4.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1078 HERVVTHSdRVIGKGHFGVVYHGEY-IDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEG 1156
Cdd:cd05038     2 EERHLKFI-KQLGEGHFGSVELCRYdPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1157 LPHVL----LPYMCHGDLLQFIRSPQRNPTvkdLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR 1232
Cdd:cd05038    81 RSLRLimeyLPSGSLRDYLQRHRDQIDLKR---LLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1233 DI-LDREYYSVQQHRHarLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAP-------PYRHIDP-------FDL 1297
Cdd:cd05038   158 VLpEDKEYYYVKEPGE--SPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPsqsppalFLRMIGIaqgqmivTRL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1298 THFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd05038   236 LELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
1087-1341 1.66e-71

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: 240.78  E-value: 1.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYI-DQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglpHVLLP-Y 1164
Cdd:cd05057    13 KVLGSGAFGTVYKGVWIpEGEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQ---VQLITqL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREyysvQQ 1244
Cdd:cd05057    90 MPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAK-LLDVD----EK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHA---RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVM 1321
Cdd:cd05057   165 EYHAeggKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTIDVYMVL 244
                         250       260
                  ....*....|....*....|
gi 578806145 1322 QQCWEADPAVRPTFRVLVGE 1341
Cdd:cd05057   245 VKCWMIDAESRPTFKELANE 264
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
1086-1345 3.55e-69

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: 233.47  E-value: 3.55e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIML-PPEGLPHVLLPY 1164
Cdd:cd05056    11 GRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITeNPVWIVMELAPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 mchGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQ 1244
Cdd:cd05056    91 ---GELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 hrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05056   168 ---GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 244
                         250       260
                  ....*....|....*....|.
gi 578806145 1325 WEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05056   245 WAYDPSKRPRFTELKAQLSDI 265
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
1089-1339 3.89e-69

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: 232.43  E-value: 3.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaqNRIQCAIKSLSRIT-EMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPeglPHVLL--PYM 1165
Cdd:cd13999     1 IGSGSFGEVYKGKW-----RGTDVAIKKLKVEDdNDELLKEFRREVSILSKLRHPNIVQFIGACLSP---PPLCIvtEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyySVQQH 1245
Cdd:cd13999    73 PGGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIK------NSTTE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLP--VKWMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQ-GRRLPQPEYCPDSLYQVMQ 1322
Cdd:cd13999   147 KMTGVVgtPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTG-EVPFKELSPIQIAAAVVQkGLRPPIPPDCPPELSKLIK 225
                         250
                  ....*....|....*..
gi 578806145 1323 QCWEADPAVRPTFRVLV 1339
Cdd:cd13999   226 RCWNEDPEKRPSFSEIV 242
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
1089-1338 4.19e-69

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: 233.81  E-value: 4.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNR--IQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMC 1166
Cdd:cd05048    13 LGEGAFGKVYKGELLGPSSEEsaISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQC-MLFEYMA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFI--RSPQRNPTVK-------------DLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05048    92 HGDLHEFLvrHSPHSDVGVSsdddgtassldqsDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDILDREYYSVQQHRhaRLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05048   172 RDIYSSDYYRVQSKS--LLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMIRSRQLLPCPE 249
                         250       260
                  ....*....|....*....|....*..
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd05048   250 DCPARVYSLMVECWHEIPSRRPRFKEI 276
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1087-1343 1.23e-67

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: 229.22  E-value: 1.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05068    14 RKLGSGQFGEVWEGLW----NNTTPVAVKTLKPGT--MDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPI-YIITELMK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYsvQQHR 1246
Cdd:cd05068    87 HGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEY--EARE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05068   165 GAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQLYDIMLECWK 244
                         250
                  ....*....|....*..
gi 578806145 1327 ADPAVRPTFRVLVGEVE 1343
Cdd:cd05068   245 ADPMERPTFETLQWKLE 261
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
1089-1345 2.23e-67

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: 228.07  E-value: 2.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIqCAIKSLSRitEMQQVEAFLREGLLMRGLNHPNVLALIGIML--PPEglpHVLLPYMC 1166
Cdd:cd05052    14 LGGGQYGEVY--EGVWKKYNLT-VAVKTLKE--DTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTrePPF---YIITEFMP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQR---NPTVkdLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSvq 1243
Cdd:cd05052    86 YGNLLDYLRECNReelNAVV--LLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTA-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 qHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQ 1323
Cdd:cd05052   162 -HAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCPPKVYELMRA 240
                         250       260
                  ....*....|....*....|..
gi 578806145 1324 CWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05052   241 CWQWNPSDRPSFAEIHQALETM 262
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
1087-1339 3.40e-66

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: 225.34  E-value: 3.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEY--IDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLppEGLPH-VLLP 1163
Cdd:cd05036    12 RALGQGAFGEVYEGTVsgMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCF--QRLPRfILLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNP------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFT---VKVADFGLARDI 1234
Cdd:cd05036    90 LMAGGDLKSFLRENRPRPeqpsslTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvAKIGDFGMARDI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 LDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCP 1314
Cdd:cd05036   170 YRADYY--RKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRMDPPKNCP 247
                         250       260
                  ....*....|....*....|....*
gi 578806145 1315 DSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd05036   248 GPVYRIMTQCWQHIPEDRPNFSTIL 272
Sema_MET cd11278
The Sema domain, a protein interacting module, of MET (also called hepatocyte growth factor ...
28-522 1.19e-64

The Sema domain, a protein interacting module, of MET (also called hepatocyte growth factor receptor, HGFR); MET is encoded by the c-met protooncogene. MET is a receptor tyrosine kinase that binds its ligand, hepatocyte growth factor/scatter factor (HGF/SF). HGF/SF and MET are essential for the development of several tissues and organs, including the placenta, liver, and several groups of skeletal muscles. It also plays a major role in the abnormal migration of cancer cells as a result of overexpression or MET mutations. MET is 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 tyrosine kinase domain. The cytoplasmic C-terminal region acts as a docking site for multiple protein substrates, including Grb2, Gab1, STAT3, Shc, SHIP-1 and Src. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. The Sema domain of Met is necessary for receptor dimerization and activation.


Pssm-ID: 200539 [Multi-domain]  Cd Length: 492  Bit Score: 228.60  E-value: 1.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   28 QCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGdrnesAVFVAIRNRLHVLGPDLKSVQSLATGPA-GDPGCQTCAA 106
Cdd:cd11278     1 QCKEAAKKSEMNLNMKYQLPNFTAETPIQNVILHKH-----HIYVGAVNKIYVLNEDLQKVSEYKTGPVlEHPDCFPCQD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  107 CGPGPHGPPG---DTDTKVLVLDPALP-ALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAH-HNRPDDCPDCVASP 181
Cdd:cd11278    76 CSDKANLSNGvwkDNVNMALFVETYYDdQLISCGSVNRGTCQRHVFPHDHPADIQSEVHCIYSPQiEEEPDQCPDCVVST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  182 LGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFApgFVA----LSVLPKHLVSYSIEYVHSFHTGA 257
Cdd:cd11278   156 LGSKVLVTVKDRFVNFFVGNTINSSYFPDHPLHSISVRRLKETQDGFE--FLTdqsyIDVLPEFRDSYPIKYVHAFESNN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  258 FVYFLTVQPASVtdDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGapEGGQPYPVLRVAHSAPVGAQLATEL 337
Cdd:cd11278   234 FVYFLTVQRESL--DSQTFHTRIIRFCSIDSELRSYMEMPLECIFTEKRRKRS--TKKEVFNILQAAYVSKPGAQLAREM 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  338 SIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPI----DLLDTLIDEGVERCCESPVHPGLRRGLD--FFQSPSFCPNPP 411
Cdd:cd11278   310 GASLNDDILFGVFAQSKPDSAEPMNRSAVCAVSIktinEFFNKIVDKQNVKCLQHFYGKNHEHCFNrtFLRNASYCEARR 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  412 glealspntscRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVsNFSL 491
Cdd:cd11278   390 -----------DEYRVEVTTALQRVDLFMGQFSNVLLTSISVFTKGDLTIANLGTSEGRFMQVVVSRSGPSTPHV-NFLL 457
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 578806145  492 gDSgQPVQRDV-----SRLGDHLLFASGDQVFQVPI 522
Cdd:cd11278   458 -DS-HPVSPEVivehtLNQNGYTLVITGKKITKIPL 491
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
1087-1336 1.57e-64

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: 220.80  E-value: 1.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGE--YIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLL-P 1163
Cdd:cd05049    11 RELGEGAFGKVFLGEcyNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCT--EGDPLLMVfE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIR-------------SPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGL 1230
Cdd:cd05049    89 YMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 ARDILDREYYSVQQHRhaRLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQP 1310
Cdd:cd05049   169 SRDIYSTDYYRVGGHT--MLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECITQGRLLQRP 246
                         250       260
                  ....*....|....*....|....*.
gi 578806145 1311 EYCPDSLYQVMQQCWEADPAVRPTFR 1336
Cdd:cd05049   247 RTCPSEVYAVMLGCWKREPQQRLNIK 272
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
1089-1335 3.93e-64

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: 218.47  E-value: 3.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQaqnRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd05041     3 IGRGNFGDVYRGVLKPD---NTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPI-MIVMELVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyYSVQQHRhA 1248
Cdd:cd05041    79 SLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGE-YTVSDGL-K 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEAD 1328
Cdd:cd05041   157 QIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYD 236

                  ....*..
gi 578806145 1329 PAVRPTF 1335
Cdd:cd05041   237 PENRPSF 243
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1089-1338 4.46e-64

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: 218.47  E-value: 4.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIQCAIKSLsRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd05059    12 LGSGQFGVVHLGKW----RGKIDVAIKMI-KEGSMSE-DDFIEEAKVMMKLSHPKLVQLYGVCTKQRPI-FIVTEYMANG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrhA 1248
Cdd:cd05059    85 CLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSVG---T 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEAD 1328
Cdd:cd05059   162 KFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEK 241
                         250
                  ....*....|
gi 578806145 1329 PAVRPTFRVL 1338
Cdd:cd05059   242 PEERPTFKIL 251
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
1087-1345 1.26e-63

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: 217.30  E-value: 1.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITEMQQVEaFLREGLLMRGLNHPNVLALIGIMlpPEGLP-HVLLPYM 1165
Cdd:cd05148    12 RKLGSGYFGEVWEGLW----KNRVRVAIKILKSDDLLKQQD-FQKEVQALKRLRHKHLISLFAVC--SVGEPvYIITELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQ-RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREYYSVQQ 1244
Cdd:cd05148    85 EKGSLLAFLRSPEgQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLAR-LIKEDVYLSSD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HrhaRLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05148   164 K---KIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLEC 240
                         250       260
                  ....*....|....*....|.
gi 578806145 1325 WEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05148   241 WAAEPEDRPSFKALREELDNI 261
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
1089-1335 2.13e-63

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: 216.44  E-value: 2.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITeMQQVEA---FLREGLLMRGLNHPNVLALIGIMLPPeglPHVLLPYM 1165
Cdd:cd05040     3 LGDGSFGVVRRGEWTTPSGKVIQVAVKCLKSDV-LSQPNAmddFLKEVNAMHSLDHPNLIRLYGVVLSS---PLMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CH-GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQ 1243
Cdd:cd05040    79 APlGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALpQNEDHYVMQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRhaRLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFL-AQGRRLPQPEYCPDSLYQVMQ 1322
Cdd:cd05040   159 EHR--KVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIdKEGERLERPDDCPQDIYNVML 236
                         250
                  ....*....|...
gi 578806145 1323 QCWEADPAVRPTF 1335
Cdd:cd05040   237 QCWAHKPADRPTF 249
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
1087-1345 3.14e-63

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: 216.81  E-value: 3.14e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPE-GLPHVLLPY 1164
Cdd:cd05109    13 KVLGSGAFGTVYKGIWIPDGENvKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTvQLVTQLMPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MChgdLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--DILDREYYSv 1242
Cdd:cd05109    93 GC---LLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARllDIDETEYHA- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 qqhRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQ 1322
Cdd:cd05109   169 ---DGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMV 245
                         250       260
                  ....*....|....*....|...
gi 578806145 1323 QCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05109   246 KCWMIDSECRPRFRELVDEFSRM 268
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
1076-1339 3.52e-63

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: 217.14  E-value: 3.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVVTHsdRVIGKGHFGVVYHGEYID--QAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlp 1153
Cdd:cd05061     3 VSREKITLL--RELGQGSFGMVYEGNARDiiKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1154 PEGLPH-VLLPYMCHGDLLQFIRS--------PQR-NPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTV 1223
Cdd:cd05061    79 SKGQPTlVVMELMAHGDLKSYLRSlrpeaennPGRpPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1224 KVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQ 1303
Cdd:cd05061   159 KIGDFGMTRDIYETDYY--RKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMD 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578806145 1304 GRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd05061   237 GGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIV 272
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
1086-1346 9.38e-63

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: 215.98  E-value: 9.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGE--YIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLP 1163
Cdd:cd05045     5 GKTLGEGEFGKVVKATafRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYG-ACSQDGPLLLIVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQR------------------NP-----TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDES 1220
Cdd:cd05045    84 YAKYGSLRSFLRESRKvgpsylgsdgnrnssyldNPderalTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1221 FTVKVADFGLARDILDREYYsVQQHRhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHF 1300
Cdd:cd05045   164 RKMKISDFGLSRDVYEEDSY-VKRSK-GRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFNL 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1301 LAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd05045   242 LKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1086-1355 1.83e-62

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: 214.16  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSL-SRITEMQQVEaFLREGLLMRGLNHPNVLALIGIMLPPEglPHVLL-P 1163
Cdd:cd05033     9 EKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLkSGYSDKQRLD-FLTEASIMGQFDHPNVIRLEGVVTKSR--PVMIVtE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyySVQ 1243
Cdd:cd05033    86 YMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE--ATY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQ 1323
Cdd:cd05033   164 TTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQLMLD 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1324 CWEADPAVRPTFrvlvgevEQIVSALlgDHYV 1355
Cdd:cd05033   244 CWQKDRNERPTF-------SQIVSTL--DKMI 266
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
1086-1345 2.14e-62

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: 216.04  E-value: 2.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPE-GLPHVLLP 1163
Cdd:cd05108    12 IKVLGSGAFGTVYKGLWIPEGEKvKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTvQLITQLMP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMChgdLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL--DREYYS 1241
Cdd:cd05108    92 FGC---LLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGaeEKEYHA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 vqqhRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVM 1321
Cdd:cd05108   169 ----EGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIM 244
                         250       260
                  ....*....|....*....|....
gi 578806145 1322 QQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05108   245 VKCWMIDADSRPKFRELIIEFSKM 268
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
1088-1344 3.65e-62

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: 213.87  E-value: 3.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEY--IDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGimLPPEGLPH-VLLPY 1164
Cdd:cd05046    12 TLGRGEFGEVFLAKAkgIEEEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLG--LCREAEPHyMILEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIR---------SPQrNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL 1235
Cdd:cd05046    90 TDLGDLKQFLRatkskdeklKPP-PLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 DREYYsvqQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGR-RLPQPEYCP 1314
Cdd:cd05046   169 NSEYY---KLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGKlELPVPEGCP 245
                         250       260       270
                  ....*....|....*....|....*....|
gi 578806145 1315 DSLYQVMQQCWEADPAVRPTFRVLVGEVEQ 1344
Cdd:cd05046   246 SRLYKLMTRCWAVNPKDRPSFSELVSALGE 275
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
1089-1344 4.72e-62

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: 212.43  E-value: 4.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQ--AQNRIQCAIKSlsritemqqvEAFLREGLLMRGLNHPNVLALIGIMLPpEGLpHVLLPYMC 1166
Cdd:cd05083    14 IGEGEFGAVLQGEYMGQkvAVKNIKCDVTA----------QAFLEETAVMTKLQHKNLVRLLGVILH-NGL-YIVMELMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRN--PTVKdLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreyYSVQQ 1244
Cdd:cd05083    82 KGNLVNFLRSRGRAlvPVIQ-LLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK-------VGSMG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05083   154 VDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSC 233
                         250       260
                  ....*....|....*....|
gi 578806145 1325 WEADPAVRPTFRVLVGEVEQ 1344
Cdd:cd05083   234 WEAEPGKRPSFKKLREKLEK 253
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
1077-1367 2.33e-61

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: 212.90  E-value: 2.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1077 PHERVVThsDRVIGKGHFGVVYHGEYI----DQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLN-HPNVLALIGIm 1151
Cdd:cd05099    10 PRDRLVL--GKPLGEGCFGQVVRAEAYgidkSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIINLLGV- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1152 LPPEGLPHVLLPYMCHGDLLQFIR---------------SPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCM 1216
Cdd:cd05099    87 CTQEGPLYVIVEYAAKGNLREFLRarrppgpdytfditkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1217 LDESFTVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFD 1296
Cdd:cd05099   167 VTEDNVMKIADFGLARGVHDIDYY--KKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEE 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1297 LTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVgEVEQIVSALLGDHYVQLPATYMNLGPS 1367
Cdd:cd05099   245 LFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLV-EALDKVLAAVSEEYLDLSMPFEQYSPS 314
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
1127-1336 7.01e-61

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: 211.04  E-value: 7.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1127 EAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHGDLLQFIR-----------SPQRNPTVKDLISFGLQVAR 1195
Cdd:cd05051    64 EDFLKEVKIMSQLKDPNIVRLLGVCTRDEPL-CMIVEYMENGDLNQFLQkheaetqgasaTNSKTLSYGTLLYMATQIAS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1196 GMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrHARLPVKWMALESLQTYRFTTKSDVWSFG 1275
Cdd:cd05051   143 GMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLYSGDYYRIEG--RAVLPIRWMAWESILLGKFTTKSDVWAFG 220
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1276 VLLWELLTRG-APPYRHIDPF----DLTHFLA-QGRR--LPQPEYCPDSLYQVMQQCWEADPAVRPTFR 1336
Cdd:cd05051   221 VTLWEILTLCkEQPYEHLTDEqvieNAGEFFRdDGMEvyLSRPPNCPKEIYELMLECWRRDEEDRPTFR 289
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
1087-1339 2.33e-60

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: 209.65  E-value: 2.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEY--IDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALIGiMLPPEGLPHVLLP 1163
Cdd:cd05055    41 KTLGAGAFGKVVEATAygLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLG-ACTIGGPILVITE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRN-PTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd05055   120 YCCYGDLLNFLRRKRESfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQhrHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIdPFDLTHF--LAQGRRLPQPEYCPDSLYQV 1320
Cdd:cd05055   200 KG--NARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGM-PVDSKFYklIKEGYRMAQPEHAPAEIYDI 276
                         250
                  ....*....|....*....
gi 578806145 1321 MQQCWEADPAVRPTFRVLV 1339
Cdd:cd05055   277 MKTCWDADPLKRPTFKQIV 295
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
1089-1338 2.53e-60

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: 207.48  E-value: 2.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidQAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd05084     4 IGRGNFGEVFSGRL--RADNTP-VAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPI-YIVMELVQGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRha 1248
Cdd:cd05084    80 DFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAATGGMK-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEAD 1328
Cdd:cd05084   158 QIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWEYD 237
                         250
                  ....*....|
gi 578806145 1329 PAVRPTFRVL 1338
Cdd:cd05084   238 PRKRPSFSTV 247
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1087-1345 3.52e-60

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: 207.14  E-value: 3.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqaqNRIQCAIKSLSRITEMQqveAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC 1166
Cdd:cd05082    12 QTIGKGEFGDVMLGDY-----RGNKVAVKCIKNDATAQ---AFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKD-LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildrEYYSVQQH 1245
Cdd:cd05082    84 KGSLVDYLRSRGRSVLGGDcLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK-----EASSTQDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 rhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd05082   159 --GKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCW 236
                         250       260
                  ....*....|....*....|
gi 578806145 1326 EADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05082   237 HLDAAMRPSFLQLREQLEHI 256
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
1089-1367 3.97e-60

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: 210.26  E-value: 3.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYI----DQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALIGiMLPPEGLPHVLLP 1163
Cdd:cd05100    20 LGEGCFGQVVMAEAIgidkDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLG-ACTQDGPLYVLVE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRS---------------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADF 1228
Cdd:cd05100    99 YASKGNLREYLRArrppgmdysfdtcklPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1229 GLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLP 1308
Cdd:cd05100   179 GLARDVHNIDYY--KKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPS 1367
Cdd:cd05100   257 KPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSVPFEQYSPG 315
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
1064-1347 6.16e-60

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 208.72  E-value: 6.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1064 DSALLAEVKDVLIPHERVVTHS-DRV-----IGKGHFGVVYHGEYI----DQAQNRIQCAIKSLSRITEMQQVEAFLREG 1133
Cdd:cd05101     1 DAPMLAGVSEYELPEDPKWEFPrDKLtlgkpLGEGCFGQVVMAEAVgidkDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1134 LLMRGL-NHPNVLALIGiMLPPEGLPHVLLPYMCHGDLLQFIRS---------------PQRNPTVKDLISFGLQVARGM 1197
Cdd:cd05101    81 EMMKMIgKHKNIINLLG-ACTQDGPLYVIVEYASKGNLREYLRArrppgmeysydinrvPEEQMTFKDLVSCTYQLARGM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1198 EYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVL 1277
Cdd:cd05101   160 EYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYY--KKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVL 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1278 LWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVS 1347
Cdd:cd05101   238 MWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILT 307
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
1087-1341 1.46e-59

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 206.34  E-value: 1.46e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLPHVLLPYM 1165
Cdd:cd05111    13 KVLGSGVFGTVHKGIWIPEGDSiKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGIC--PGASLQLVTQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArDIL---DREYYsv 1242
Cdd:cd05111    91 PLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVA-DLLypdDKKYF-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 qqHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQ 1322
Cdd:cd05111   168 --YSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTIDVYMVMV 245
                         250
                  ....*....|....*....
gi 578806145 1323 QCWEADPAVRPTFRVLVGE 1341
Cdd:cd05111   246 KCWMIDENIRPTFKELANE 264
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
1087-1353 1.69e-59

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: 206.05  E-value: 1.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05072    13 KKLGAGQFGEVWMGYY----NNSTKVAVKTLKPGT--MSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPI-YIITEYMA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTV-KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSvqqH 1245
Cdd:cd05072    86 KGSLLDFLKSDEGGKVLlPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTA---R 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd05072   163 EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDELYDIMKTCW 242
                         250       260
                  ....*....|....*....|....*...
gi 578806145 1326 EADPAVRPTFRVLVGEVEQIVSALLGDH 1353
Cdd:cd05072   243 KEKAEERPTFDYLQSVLDDFYTATEGQY 270
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
1076-1347 5.87e-59

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: 205.63  E-value: 5.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVVThsDRVIGKGHFGVVYHGEYI---DQAQNRI-QCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALIGi 1150
Cdd:cd05098    10 LPRDRLVL--GKPLGEGCFGQVVLAEAIgldKDKPNRVtKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLG- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1151 MLPPEGLPHVLLPYMCHGDLLQFIRS---------------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNC 1215
Cdd:cd05098    87 ACTQDGPLYVIVEYASKGNLREYLQArrppgmeycynpshnPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1216 MLDESFTVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPF 1295
Cdd:cd05098   167 LVTEDNVMKIADFGLARDIHHIDYY--KKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVE 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1296 DLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVS 1347
Cdd:cd05098   245 ELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVA 296
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
1089-1343 3.13e-58

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 201.65  E-value: 3.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIQCAIKSLsRITEMQQVEaFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd05113    12 LGTGQFGVVKYGKW----RGQYDVAIKMI-KEGSMSEDE-FIEEAKVMMNLSHEKLVQLYGVCTKQRPI-FIITEYMANG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrhA 1248
Cdd:cd05113    85 CLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVG---S 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEAD 1328
Cdd:cd05113   162 KFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHEK 241
                         250
                  ....*....|....*
gi 578806145 1329 PAVRPTFRVLVGEVE 1343
Cdd:cd05113   242 ADERPTFKILLSNIL 256
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
1087-1335 1.24e-57

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: 201.21  E-value: 1.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQC--AIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLL-P 1163
Cdd:cd05050    11 RDIGQGAFGRVFQARAPGLLPYEPFTmvAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCA--VGKPMCLLfE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIR--SPQRNP-------------------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFT 1222
Cdd:cd05050    89 YMAYGDLNEFLRhrSPRAQCslshstssarkcglnplplSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1223 VKVADFGLARDILDREYYSVQQHRHarLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLA 1302
Cdd:cd05050   169 VKIADFGLSRNIYSADYYKASENDA--IPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIYYVR 246
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578806145 1303 QGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd05050   247 DGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSF 279
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
1076-1344 1.59e-57

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: 200.64  E-value: 1.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVVThsDRVIGKGHFGVVYHG----EYIDQAQNRIqcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIM 1151
Cdd:cd05062     3 VAREKITM--SRELGQGSFGMVYEGiakgVVKDEPETRV--AIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1152 lpPEGLPH-VLLPYMCHGDLLQFIRS---------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF 1221
Cdd:cd05062    79 --SQGQPTlVIMELMTRGDLKSYLRSlrpemennpVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1222 TVKVADFGLARDILDREYYsvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFL 1301
Cdd:cd05062   157 TVKIGDFGMTRDIYETDYY--RKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFV 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1302 AQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQ 1344
Cdd:cd05062   235 MEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKE 277
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
1087-1339 2.30e-57

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 200.79  E-value: 2.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEY--IDQAQNRIQCAIKSLSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGIMLPPEGLPHVLLP 1163
Cdd:cd05054    13 KPLGRGAFGKVIQASAfgIDKSATCRTVAVKMLKEGATASEHKALMTElKILIHIGHHLNVVNLLGACTKPGGPLMVIVE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRS------PQRNP-------------------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLD 1218
Cdd:cd05054    93 FCKFGNLSNYLRSkreefvPYRDKgardveeeedddelykeplTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1219 ESFTVKVADFGLARDIL-DREYysVQQHrHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYR--HIDPf 1295
Cdd:cd05054   173 ENNVVKICDFGLARDIYkDPDY--VRKG-DARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPgvQMDE- 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1296 DLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd05054   249 EFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELV 292
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
1089-1342 4.31e-57

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: 198.25  E-value: 4.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIQCAIKSLsRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLppEGLP-HVLLPYMCH 1167
Cdd:cd05112    12 IGSGQFGLVHLGYW----LNKDKVAIKTI-REGAMSE-EDFIEEAEVMMKLSHPKLVQLYGVCL--EQAPiCLVFEFMEH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrh 1247
Cdd:cd05112    84 GCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTG--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 ARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd05112   161 TKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKE 240
                         250
                  ....*....|....*
gi 578806145 1328 DPAVRPTFRVLVGEV 1342
Cdd:cd05112   241 RPEDRPSFSLLLRQL 255
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
1087-1348 5.70e-57

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: 198.57  E-value: 5.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGImLPPEGLpHVLLPYMC 1166
Cdd:cd05067    13 ERLGAGQFGEVWMGYY----NGHTKVAIKSLKQGS--MSPDAFLAEANLMKQLQHQRLVRLYAV-VTQEPI-YIITEYME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQ-RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSvqqH 1245
Cdd:cd05067    85 NGSLVDFLKTPSgIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTA---R 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd05067   162 EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCW 241
                         250       260
                  ....*....|....*....|...
gi 578806145 1326 EADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05067   242 KERPEDRPTFEYLRSVLEDFFTA 264
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
1087-1359 4.74e-56

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: 197.21  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQN-RIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglPHVLLPYM 1165
Cdd:cd05110    13 KVLGSGAFGTVYKGIWVPEGETvKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT--IQLVTQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL-DREYYSVQQ 1244
Cdd:cd05110    91 PHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEgDEKEYNADG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 hrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05110   171 ---GKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKC 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578806145 1325 WEADPAVRPTFRVLVGEVEQIVS------ALLGDHYVQLPA 1359
Cdd:cd05110   248 WMIDADSRPKFKELAAEFSRMARdpqrylVIQGDDRMKLPS 288
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
1087-1346 6.48e-56

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 195.08  E-value: 6.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQaqnrIQCAIKSLsRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05114    10 KELGSGLFGVVRLGKWRAQ----YKVAIKAI-REGAMSE-EDFIEEAKVMMKLTHPKLVQLYGVCTQQKPI-YIVTEFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhr 1246
Cdd:cd05114    83 NGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSG-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 hARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05114   161 -AKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWH 239
                         250       260
                  ....*....|....*....|
gi 578806145 1327 ADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd05114   240 EKPEGRPTFADLLRTITEIA 259
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
1089-1332 9.63e-56

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: 195.57  E-value: 9.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEY--IDQAQNRIQCAIKSLSRITEMQQVEaFLREGLLMRGLNHPNVLALIGIMlpPEGLPHVLL-PYM 1165
Cdd:cd05092    13 LGEGAFGKVFLAEChnLLPEQDKMLVAVKALKEATESARQD-FQREAELLTVLQHQHIVRFYGVC--TEGEPLIMVfEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRS--------------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05092    90 RHGDLNRFLRShgpdakildggegqAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDILDREYYSVQQHrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05092   170 RDIYSTDYYRVGGR--TMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERPR 247
                         250       260
                  ....*....|....*....|.
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVR 1332
Cdd:cd05092   248 TCPPEVYAIMQGCWQREPQQR 268
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1089-1338 6.00e-55

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: 192.05  E-value: 6.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLPHVLLPYMCHG 1168
Cdd:cd14203     3 LGQGCFGEVWMGTW----NGTTKVAIKTLKPGT--MSPEAFLEEAQIMKKLRHDKLVQLYAVV--SEEPIYIVTEFMSKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQ-RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrh 1247
Cdd:cd14203    75 SLLDFLKDGEgKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQG--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 ARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd14203   152 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRK 231
                         250
                  ....*....|.
gi 578806145 1328 DPAVRPTFRVL 1338
Cdd:cd14203   232 DPEERPTFEYL 242
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
64-523 4.13e-54

The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine kinases; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestor of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signalling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. This family also includes the Met and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 194.86  E-value: 4.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-PGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGR 142
Cdd:cd11236     8 DNSTGRVYVGAVNRLYQLDSSLLLEAEVSTGPVLDsPLCLPPGCCSCDHPRSPTDNYNKILLIDYSSGRLITCGSLYQGV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  143 CFLHDL-----EPQGTAVHLAAPaclfsahhnrpddcpDCVASPLGTrVTVVEQGQASYFYVASSLDAAvaASFSPR-SV 216
Cdd:cd11236    88 CQLRNLsnisvVVERSSTPVAAN---------------DPNASTVGF-VGPGPYNNENVLYVGATYTNN--GYRDYRpAV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  217 SIRRLKADASGFAPGFV---ALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVtDDPSALHTRLARLSATEPELGDY 293
Cdd:cd11236   150 SSRSLPPDDDFNAGSLTggsAISIDDEYRDRYSIKYVYGFSSGGFSYFVTVQRKSV-DDESPYISRLVRVCQSDSNYYSY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  294 RELVLDCRFAPKRRrrgapeggqpYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPIDL 373
Cdd:cd11236   229 TEVPLQCTGGDGTN----------YNLLQAAYVGKAGSDLARSLGISTDDDVLFGVFSKSKGPSAEPSSKSALCVFSMKD 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  374 LDTLIDEgverccespvhpglrrgldffqspsFCPnppgLEALSPNTScrhfpllvsssfsrvdlfNGLLGPVQVTALYV 453
Cdd:cd11236   299 IEAAFND-------------------------NCP----LGGGVPITT------------------SAVLSDSLLTSVAV 331
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145  454 TRLDNVTVAHMGTMDGRILQVELVRSLNYLLYvSNFSLgDSGQPVQRD--VSRLGDHLLFASGDQVFQVPIQ 523
Cdd:cd11236   332 TTTRNHTVAFLGTSDGQLKKVVLESSSSATQY-ETLLV-DSGSPILPDmvFDPDGEHLYVMTPKKVTKVPVE 401
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1088-1335 4.56e-54

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: 190.25  E-value: 4.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGiMLPPEGLPHVLLPYMC 1166
Cdd:cd05047     2 VIGEGNFGQVLKAR-IKKDGLRMDAAIKRMKEYASKDDHRDFAGElEVLCKLGHHPNIINLLG-ACEHRGYLYLAIEYAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSP---QRNP------------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05047    80 HGNLLDFLRKSrvlETDPafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDildREYYSvqQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05047   160 RG---QEVYV--KKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 234
                         250       260
                  ....*....|....*....|....
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd05047   235 NCDDEVYDLMRQCWREKPYERPSF 258
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
1084-1349 4.57e-54

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 190.08  E-value: 4.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLP-HVLL 1162
Cdd:cd05066     7 KIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVV--TRSKPvMIVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREYYSV 1242
Cdd:cd05066    85 EYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSR-VLEDDPEAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQ 1322
Cdd:cd05066   164 YTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQLML 243
                         250       260
                  ....*....|....*....|....*..
gi 578806145 1323 QCWEADPAVRPTFrvlvgevEQIVSAL 1349
Cdd:cd05066   244 DCWQKDRNERPKF-------EQIVSIL 263
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1089-1336 6.50e-53

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: 187.53  E-value: 6.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEY----IDQAQnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPY 1164
Cdd:cd05090    13 LGECAFGKIYKGHLylpgMDHAQ---LVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVC-MLFEF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFI--RSPQ--------RNPTVK------DLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADF 1228
Cdd:cd05090    89 MNQGDLHEFLimRSPHsdvgcssdEDGTVKssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1229 GLARDILDREYYSVQQHrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLP 1308
Cdd:cd05090   169 GLSREIYSSDYYRVQNK--SLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 246
                         250       260
                  ....*....|....*....|....*...
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFR 1336
Cdd:cd05090   247 CSEDCPPRMYSLMTECWQEIPSRRPRFK 274
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
1088-1342 1.12e-52

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: 185.59  E-value: 1.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQqveaFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd05085     3 LLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIK----FLSEARILKQYDHPNIVKLIGVCTQRQPI-YIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHrh 1247
Cdd:cd05085    78 GDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLK-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 aRLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd05085   156 -QIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDY 234
                         250
                  ....*....|....*
gi 578806145 1328 DPAVRPTFRVLVGEV 1342
Cdd:cd05085   235 NPENRPKFSELQKEL 249
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
1076-1339 7.93e-52

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 186.34  E-value: 7.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVvtHSDRVIGKGHFGVVYHGEY--IDQAQNRIQCAIKSLSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGIML 1152
Cdd:cd05102     4 FPRDRL--RLGKVLGHGAFGKVVEASAfgIDKSSSCETVAVKMLKEGATASEHKALMSElKILIHIGNHLNVVNLLGACT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1153 PPEGLPHVLLPYMCHGDLLQFIR------------SP----------------------------------QRNP----- 1181
Cdd:cd05102    82 KPNGPLMVIVEFCKYGNLSNFLRakregfspyrerSPrtrsqvrsmveavradrrsrqgsdrvasftestsSTNQprqev 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1182 --------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL-DREYYsvqQHRHARLPV 1252
Cdd:cd05102   162 ddlwqsplTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYkDPDYV---RKGSARLPL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1253 KWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYR--HIDPfDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPA 1330
Cdd:cd05102   239 KWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPgvQINE-EFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPK 317

                  ....*....
gi 578806145 1331 VRPTFRVLV 1339
Cdd:cd05102   318 ERPTFSDLV 326
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1087-1336 1.37e-51

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 182.34  E-value: 1.37e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1087 RVIGKGHFGVVYHGEYIDqaqNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:smart00220    5 EKLGEGSFGKVYLARDKK---TGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1167 HGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD-REYYSVQQH 1245
Cdd:smart00220   81 GGDLFDLLKK-RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPgEKLTTFVGT 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   1246 RHarlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEY---CPDSLYQVMQ 1322
Cdd:smart00220  160 PE------YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIR 232
                           250
                    ....*....|....
gi 578806145   1323 QCWEADPAVRPTFR 1336
Cdd:smart00220  233 KLLVKDPEKRLTAE 246
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
1088-1348 1.54e-51

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: 184.05  E-value: 1.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGeYIDQAQNRIQCAIKSLSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGiMLPPEGLPHVLLPYMC 1166
Cdd:cd05089     9 VIGEGNFGQVIKA-MIKKDGLKMNAAIKMLKEFASENDHRDFAGElEVLCKLGHHPNIINLLG-ACENRGYLYIAIEYAP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSP---QRNP------------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05089    87 YGNLLDFLRKSrvlETDPafakehgtastlTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDildREYYSvqQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05089   167 RG---EEVYV--KKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKPR 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05089   242 NCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEA 278
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
1086-1349 2.43e-51

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 182.38  E-value: 2.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLP-HVLLPY 1164
Cdd:cd05065     9 EEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVV--TKSRPvMIITEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR----DILDREYY 1240
Cdd:cd05065    87 MENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfledDTSDPTYT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQhrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQV 1320
Cdd:cd05065   167 SSLG---GKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPTALHQL 243
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1321 MQQCWEADPAVRPTFrvlvgevEQIVSAL 1349
Cdd:cd05065   244 MLDCWQKDRNLRPKF-------GQIVNTL 265
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
1089-1338 3.32e-51

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: 181.70  E-value: 3.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIqCAIKSLSRITEMQQV-EAFLREGLLMRGLNHPNVLALIGIMlppEGLPHVLLPYMCH 1167
Cdd:cd05116     3 LGSGNFGTVKKGYYQMKKVVKT-VAVKILKNEANDPALkDELLREANVMQQLDNPYIVRMIGIC---EAESWMLVMEMAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 -GDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQQH 1245
Cdd:cd05116    79 lGPLNKFLQK-NRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALrADENYYKAQTH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 rhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd05116   158 --GKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCW 235
                         250
                  ....*....|...
gi 578806145 1326 EADPAVRPTFRVL 1338
Cdd:cd05116   236 TYDVDERPGFAAV 248
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
1087-1332 3.45e-51

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: 182.55  E-value: 3.45e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQA--QNRIQCAIKSLSRITEMQQVEaFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLL-P 1163
Cdd:cd05093    11 RELGEGAFGKVFLAECYNLCpeQDKILVAVKTLKDASDNARKD-FHREAELLTNLQHEHIVKFYGVCV--EGDPLIMVfE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRS------------PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05093    88 YMKHGDLNKFLRAhgpdavlmaegnRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDILDREYYSVQQHrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05093   168 RDVYSTDYYRVGGH--TMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 245
                         250       260
                  ....*....|....*....|.
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVR 1332
Cdd:cd05093   246 TCPKEVYDLMLGCWQREPHMR 266
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
1086-1343 4.11e-51

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: 181.76  E-value: 4.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglPHVLLPYM 1165
Cdd:cd05073    16 EKKLGAGQFGEVWMATY----NKHTKVAVKTMKPGS--MSVEAFLAEANVMKTLQHDKLVKLHAVVTKEP--IYIITEFM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPT-VKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQ 1244
Cdd:cd05073    88 AKGSLLDFLKSDEGSKQpLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 hrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05073   168 ---AKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRC 244
                         250
                  ....*....|....*....
gi 578806145 1325 WEADPAVRPTFRVLVGEVE 1343
Cdd:cd05073   245 WKNRPEERPTFEYIQSVLD 263
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
1086-1346 8.21e-51

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: 180.94  E-value: 8.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSR-ITEMQQVEaFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd05063    10 QKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLKPgYTEKQRQD-FLSEASIMGQFSHHNIIRLEGVVTKFKPA-MIITEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREYYSVQQ 1244
Cdd:cd05063    88 MENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSR-VLEDDPEGTYT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05063   167 TSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVYQLMLQC 246
                         250       260
                  ....*....|....*....|..
gi 578806145 1325 WEADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd05063   247 WQQDRARRPRFVDIVNLLDKLL 268
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
1089-1338 8.98e-51

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 181.71  E-value: 8.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYH------GEYIDQAQNR-----IQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGL 1157
Cdd:cd05097    13 LGEGQFGEVHLceaeglAEFLGEGAPEfdgqpVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1158 PhVLLPYMCHGDLLQFIRspQRN-----------PTV--KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVK 1224
Cdd:cd05097    93 C-MITEYMENGDLNQFLS--QREiestfthanniPSVsiANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1225 VADFGLARDILDREYYSVQQhrHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTR-GAPPYRHIDPFDLTH---- 1299
Cdd:cd05097   170 IADFGMSRNLYSGDYYRIQG--RAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSLLSDEQVIEntge 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578806145 1300 -FLAQGRR--LPQPEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd05097   248 fFRNQGRQiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
1089-1336 1.01e-50

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 181.73  E-value: 1.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGE------------YIDQAQNR-IQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPE 1155
Cdd:cd05095    13 LGEGQFGEVHLCEaegmekfmdkdfALEVSENQpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 GLPhVLLPYMCHGDLLQFIR-----SPQRNPTVKDLISF------GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVK 1224
Cdd:cd05095    93 PLC-MITEYMENGDLNQFLSrqqpeGQLALPSNALTVSYsdlrfmAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1225 VADFGLARDILDREYYSVQQhrHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTR-GAPPYRHIDPFDLTH---- 1299
Cdd:cd05095   172 IADFGMSRNLYSGDYYRIQG--RAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPYSQLSDEQVIEntge 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578806145 1300 -FLAQGRR--LPQPEYCPDSLYQVMQQCWEADPAVRPTFR 1336
Cdd:cd05095   250 fFRDQGRQtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQ 289
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
1182-1348 8.35e-50

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 180.56  E-value: 8.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1182 TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL-DREYYsvqQHRHARLPVKWMALESL 1260
Cdd:cd05103   177 TLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYkDPDYV---RKGDARLPLKWMAPETI 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1261 QTYRFTTKSDVWSFGVLLWELLTRGAPPYR--HIDPfDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd05103   254 FDRVYTIQSDVWSFGVLLWEIFSLGASPYPgvKIDE-EFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSEL 332
                         170
                  ....*....|
gi 578806145 1339 VGEVEQIVSA 1348
Cdd:cd05103   333 VEHLGNLLQA 342
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
1182-1339 1.13e-49

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: 180.20  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1182 TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSvqQHRHARLPVKWMALESLQ 1261
Cdd:cd14207   178 TMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYV--RKGDARLPLKWMAPESIF 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1262 TYRFTTKSDVWSFGVLLWELLTRGAPPYR--HIDPfDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd14207   256 DKIYSTKSDVWSYGVLLWEIFSLGASPYPgvQIDE-DFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELV 334
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
1089-1345 2.58e-49

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: 177.13  E-value: 2.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYiDQAQNRIQ--CAIKSLSRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPP--EGLpHVLLPY 1164
Cdd:cd14205    12 LGKGNFGSVEMCRY-DPLQDNTGevVAVKKLQHSTE-EHLRDFEREIEILKSLQHDNIVKYKGVCYSAgrRNL-RLIMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQ 1243
Cdd:cd14205    89 LPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLpQDKEYYKVK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHArlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLT----RGAPPYRHIDP-----------FDLTHFLAQGRRLP 1308
Cdd:cd14205   169 EPGES--PIFWYAPESLTESKFSVASDVWSFGVVLYELFTyiekSKSPPAEFMRMigndkqgqmivFHLIELLKNNGRLP 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14205   247 RPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
1087-1349 5.36e-49

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: 176.35  E-value: 5.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGE--YIDQAQNRIQCAIKSLSRITeMQQVEAFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLL-P 1163
Cdd:cd05094    11 RELGEGAFGKVFLAEcyNLSPTKDKMLVAVKTLKDPT-LAARKDFQREAELLTNLQHDHIVKFYGVCG--DGDPLIMVfE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTV---------------KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADF 1228
Cdd:cd05094    88 YMKHGDLNKFLRAHGPDAMIlvdgqprqakgelglSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1229 GLARDILDREYYSVQQHrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLP 1308
Cdd:cd05094   168 GMSRDVYSTDYYRVGGH--TMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLE 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFRvlvgEVEQIVSAL 1349
Cdd:cd05094   246 RPRVCPKEVYDIMLGCWQREPQQRLNIK----EIYKILHAL 282
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
1089-1348 1.30e-48

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: 174.87  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLPHVLLPYMCHG 1168
Cdd:cd05070    17 LGNGQFGEVWMGTW----NGNTKVAIKTLKPGT--MSPESFLEEAQIMKKLKHDKLVQLYAVV--SEEPIYIVTEYMSKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQ-RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrh 1247
Cdd:cd05070    89 SLLDFLKDGEgRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQG--- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 ARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd05070   166 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKK 245
                         250       260
                  ....*....|....*....|.
gi 578806145 1328 DPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05070   246 DPEERPTFEYLQGFLEDYFTA 266
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
1076-1348 1.35e-48

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: 174.87  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1076 IPHERVvtHSDRVIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITEMQqvEAFLREGLLMRGLNHPNVLALIGIMlpPE 1155
Cdd:cd05069     9 IPRESL--RLDVKLGQGCFGEVWMGTW----NGTTKVAIKTLKPGTMMP--EAFLQEAQIMKKLRHDKLVPLYAVV--SE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 GLPHVLLPYMCHGDLLQFIRSPQ-RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI 1234
Cdd:cd05069    79 EPIYIVTEFMGKGSLLDFLKEGDgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 LDREYYSVQQhrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCP 1314
Cdd:cd05069   159 EDNEYTARQG---AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCP 235
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578806145 1315 DSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd05069   236 ESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTA 269
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
1087-1346 2.69e-48

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: 173.96  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNR-IQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLP-HVLLPY 1164
Cdd:cd05079    10 RDLGEGHFGKVELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGiKLIMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQ 1243
Cdd:cd05079    90 LPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTDKEYYTVK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHArlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPF--------------DLTHFLAQGRRLPQ 1309
Cdd:cd05079   170 DDLDS--PVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPMTLFlkmigpthgqmtvtRLVRVLEEGKRLPR 247
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578806145 1310 PEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd05079   248 PPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
1087-1344 2.88e-48

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: 177.02  E-value: 2.88e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFG-VVYHGEY-IDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALIGiMLPPEGLPHVLLP 1163
Cdd:cd05104    41 KTLGAGAFGkVVEATAYgLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLgNHINIVNLLG-ACTVGGPTLVITE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSP-----------------------QRNPT-------------------------------------- 1182
Cdd:cd05104   120 YCCYGDLLNFLRRKrdsficpkfedlaeaalyrnllhQREMAcdslneymdmkpsvsyvvptkadkrrgvrsgsyvdqdv 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1183 -------------VKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrHAR 1249
Cdd:cd05104   200 tseileedelaldTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKG--NAR 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1250 LPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIdPFDLTHF--LAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd05104   278 LPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGM-PVDSKFYkmIKEGYRMDSPEFAPSEMYDIMRSCWDA 356
                         330
                  ....*....|....*..
gi 578806145 1328 DPAVRPTFRVLVGEVEQ 1344
Cdd:cd05104   357 DPLKRPTFKQIVQLIEQ 373
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
1087-1339 3.40e-48

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: 173.93  E-value: 3.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYiDQAQNRI--QCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGImLPPEGLPHVLL-- 1162
Cdd:cd05080    10 RDLGEGHFGKVSLYCY-DPTNDGTgeMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGC-CSEQGGKSLQLim 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIrsPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD-REYYS 1241
Cdd:cd05080    88 EYVPLGSLRDYL--PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEgHEYYR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHArlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTR----GAPPYRHIDPFD----------LTHFLAQGRRL 1307
Cdd:cd05080   166 VREDGDS--PVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHcdssQSPPTKFLEMIGiaqgqmtvvrLIELLERGERL 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1308 PQPEYCPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd05080   244 PCPDKCPQEVYHLMKNCWETEASFRPTFENLI 275
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
1088-1345 6.42e-48

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: 172.19  E-value: 6.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITE---MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPY 1164
Cdd:cd14061     1 VIGVGGFGKVYRGIWRGE-----EVAVKAARQDPDediSVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVM-EY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVkdLISFGLQVARGMEYLAEQKFV---HRDLAARNCMLDESF--------TVKVADFGLARD 1233
Cdd:cd14061    75 ARGGALNRVLAGRKIPPHV--LVDWAIQIARGMNYLHNEAPVpiiHRDLKSSNILILEAIenedlenkTLKITDFGLARE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1234 IldreyysvqqHRHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-RLP 1308
Cdd:cd14061   153 W----------HKTTRMSAagtyAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAVNKlTLP 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14061   222 IPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1089-1336 7.08e-48

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: 172.90  E-value: 7.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQA--QNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMC 1166
Cdd:cd05091    14 LGEDRFGKVYKGHLFGTApgEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMS-MIFSYCS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFI--RSPQRN-------PTVK------DLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05091    93 HGDLHEFLvmRSPHSDvgstdddKTVKstlepaDFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLF 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDILDREYYSVQQHrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05091   173 REVYAADYYKLMGN--SLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRQVLPCPD 250
                         250       260
                  ....*....|....*....|....*
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPTFR 1336
Cdd:cd05091   251 DCPAWVYTLMLECWNEFPSRRPRFK 275
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
1089-1343 1.19e-47

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: 172.18  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITemQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLPHVLLPYMCHG 1168
Cdd:cd05071    17 LGQGCFGEVWMGTW----NGTTRVAIKTLKPGT--MSPEAFLQEAQVMKKLRHEKLVQLYAVV--SEEPIYIVTEYMSKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSP-QRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrh 1247
Cdd:cd05071    89 SLLDFLKGEmGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQG--- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 ARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEA 1327
Cdd:cd05071   166 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRK 245
                         250
                  ....*....|....*.
gi 578806145 1328 DPAVRPTFRVLVGEVE 1343
Cdd:cd05071   246 EPEERPTFEYLQAFLE 261
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
1088-1335 1.86e-47

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: 172.49  E-value: 1.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGiMLPPEGLPHVLLPYMC 1166
Cdd:cd05088    14 VIGEGNFGQVLKAR-IKKDGLRMDAAIKRMKEYASKDDHRDFAGElEVLCKLGHHPNIINLLG-ACEHRGYLYLAIEYAP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSP---QRNP------------TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05088    92 HGNLLDFLRKSrvlETDPafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDildREYYSvqQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPE 1311
Cdd:cd05088   172 RG---QEVYV--KKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 246
                         250       260
                  ....*....|....*....|....
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd05088   247 NCDDEVYDLMRQCWREKPYERPSF 270
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
1089-1336 5.16e-47

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: 167.83  E-value: 5.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDqaqNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd00180     1 LGKGSFGKVYKARDKE---TGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFL-YLVMEYCEGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHa 1248
Cdd:cd00180    77 SLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGT- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 rLPVKWMALESLQTYRFTTKSDVWSFGVLLWELltrgappyrhidpfdlthflaqgrrlpqpeycpDSLYQVMQQCWEAD 1328
Cdd:cd00180   156 -TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYD 201

                  ....*...
gi 578806145 1329 PAVRPTFR 1336
Cdd:cd00180   202 PKKRPSAK 209
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
1089-1335 2.00e-46

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: 168.20  E-value: 2.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYiDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPHVLLPYMCH- 1167
Cdd:cd05115    12 LGSGNFGCVKKGVY-KMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC---EAEALMLVMEMASg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQQHr 1246
Cdd:cd05115    88 GPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgADDSYYKARSA- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 hARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd05115   167 -GKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWI 245

                  ....*....
gi 578806145 1327 ADPAVRPTF 1335
Cdd:cd05115   246 YKWEDRPNF 254
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
1129-1335 1.28e-45

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: 167.03  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1129 FLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMCHGDLLQFIRS------------------PQRNPTVKDLISFG 1190
Cdd:cd05096    66 FLKEVKILSRLKDPNIIRLLGVCVDEDPLC-MITEYMENGDLNQFLSShhlddkeengndavppahCLPAISYSSLLHVA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1191 LQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrHARLPVKWMALESLQTYRFTTKSD 1270
Cdd:cd05096   145 LQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQG--RAVLPIRWMAWECILMGKFTTASD 222
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1271 VWSFGVLLWELLTR-GAPPYRHIDPFDLTH-----FLAQGRR--LPQPEYCPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd05096   223 VWAFGVTLWEILMLcKEQPYGELTDEQVIEnagefFRDQGRQvyLFRPPPCPQGLYELMLQCWSRDCRERPSF 295
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
1087-1351 7.90e-45

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: 166.94  E-value: 7.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFG-VVYHGEY-IDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALIGIMlpPEGLP-HVLL 1162
Cdd:cd05106    44 KTLGAGAFGkVVEATAFgLGKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLgQHKNIVNLLGAC--THGGPvLVIT 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRN--------PTV--------------------------------------------------- 1183
Cdd:cd05106   122 EYCCYGDLLNFLRKKAETflnfvmalPEIsetssdyknitlekkyirsdsgfssqgsdtyvemrpvsssssqssdskdee 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1184 ----------KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQhrHARLPVK 1253
Cdd:cd05106   202 dtedswpldlDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKG--NARLPVK 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1254 WMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHI---DPFdlTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPA 1330
Cdd:cd05106   280 WMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGIlvnSKF--YKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPT 357
                         330       340
                  ....*....|....*....|.
gi 578806145 1331 VRPTFRvlvgEVEQIVSALLG 1351
Cdd:cd05106   358 ERPTFS----QISQLIQRQLG 374
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
1086-1335 8.95e-44

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: 160.47  E-value: 8.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd05064    10 ERILGTGRFGELCRGCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTM-MIVTEYM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFG-LARDILDREYYSVQq 1244
Cdd:cd05064    89 SNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRrLQEDKSEAIYTTMS- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 hrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd05064   168 ---GKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAPRNCPNLLHQLMLDC 244
                         250
                  ....*....|.
gi 578806145 1325 WEADPAVRPTF 1335
Cdd:cd05064   245 WQKERGERPRF 255
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
1088-1345 1.19e-43

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: 160.83  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNRIQ-CAIKSLSRITeMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPeGLP--HVLLPY 1164
Cdd:cd05081    11 QLGKGNFGSVELCRYDPLGDNTGAlVAVKQLQHSG-PDQQRDFQREIQILKALHSDFIVKYRGVSYGP-GRRslRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-LDREYYSVQ 1243
Cdd:cd05081    89 LPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpLDKDYYVVR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHArlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRG----APP---YRHIDPFD-------LTHFLAQGRRLPQ 1309
Cdd:cd05081   169 EPGQS--PIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCdkscSPSaefLRMMGCERdvpalcrLLELLEEGQRLPA 246
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578806145 1310 PEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd05081   247 PPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
1182-1346 3.42e-43

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: 163.26  E-value: 3.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1182 TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL-DREYYSvqqHRHARLPVKWMALESL 1260
Cdd:cd05107   237 SYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMrDSNYIS---KGSTFLPLKWMAPESI 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1261 QTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIdPFDLTHF--LAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd05107   314 FNNLYTTLSDVWSFGILLWEIFTLGGTPYPEL-PMNEQFYnaIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQL 392

                  ....*...
gi 578806145 1339 VGEVEQIV 1346
Cdd:cd05107   393 VHLVGDLL 400
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
1182-1346 4.97e-43

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: 162.50  E-value: 4.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1182 TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL-DREYYSvqqHRHARLPVKWMALESL 1260
Cdd:cd05105   235 TTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMhDSNYVS---KGSTFLPVKWMAPESI 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1261 QTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIdPFDLTHF--LAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd05105   312 FDNLYTTLSDVWSYGILLWEIFSLGGTPYPGM-IVDSTFYnkIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHL 390

                  ....*...
gi 578806145 1339 VGEVEQIV 1346
Cdd:cd05105   391 SDIVESLL 398
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
1088-1345 8.24e-43

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: 157.46  E-value: 8.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQ---QVEAFLREGLLMRGLNHPNVLALIGIMLPPeglPHVLL-- 1162
Cdd:cd14148     1 IIGVGGFGKVYKGLWRGE-----EVAVKAARQDPDEDiavTAENVRQEARLFWMLQHPNIIALRGVCLNP---PHLCLvm 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVkdLISFGLQVARGMEYLAEQKFV---HRDLAARNCMLDE--------SFTVKVADFGLA 1231
Cdd:cd14148    73 EYARGGALNRALAGKKVPPHV--LVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEpienddlsGKTLKITDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RdildreyysvQQHRHARLPVK----WMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-R 1306
Cdd:cd14148   151 R----------EWHKTTKMSAAgtyaWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVAMNKlT 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578806145 1307 LPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14148   220 LPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
1088-1345 1.18e-42

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: 157.51  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQ---QVEAFLREGLLMRGLNHPNVLALIGIMLPPeglPHV--LL 1162
Cdd:cd14146     1 IIGVGGFGKVYRATWKGQ-----EVAVKAARQDPDEDikaTAESVRQEAKLFSMLRHPNIIKLEGVCLEE---PNLclVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKD--------LISFGLQVARGMEYLAEQKFV---HRDLAARNCMLDESF--------TV 1223
Cdd:cd14146    73 EFARGGTLNRALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIehddicnkTL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1224 KVADFGLARdildreyysvQQHRHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTH 1299
Cdd:cd14146   153 KITDFGLAR----------EWHRTTKMSAagtyAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAY 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1300 FLAQGR-RLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14146   222 GVAVNKlTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
1086-1345 9.56e-40

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 149.04  E-value: 9.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITE---MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLL 1162
Cdd:cd14145    11 EEIIGIGGFGKVYRAIWIGD-----EVAVKAARHDPDediSQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNL--CLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFV---HRDLAARNCMLDESF--------TVKVADFGLA 1231
Cdd:cd14145    84 MEFARGGPLNRVLSGKRIPP-DILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKVengdlsnkILKITDFGLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RdildreyysvQQHRHARLPVK----WMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-R 1306
Cdd:cd14145   163 R----------EWHRTTKMSAAgtyaWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVAYGVAMNKlS 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578806145 1307 LPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14145   232 LPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
1087-1334 6.34e-39

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: 146.13  E-value: 6.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKS--LSRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGE---LMAVKEveLSGDSE-EELEALEREIRILSSLKHPNIVRYLGTERTENTL-NIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRS--PQRNPTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd06606    81 VPGGSLASLLKKfgKLPEPVVR---KYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHARLPvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHI-DPFDLTHFLAQGRRLPQ-PEYCPDSLYQV 1320
Cdd:cd06606   158 TKSLRGTPY--WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELgNPVAALFKIGSSGEPPPiPEHLSEEAKDF 234
                         250
                  ....*....|....
gi 578806145 1321 MQQCWEADPAVRPT 1334
Cdd:cd06606   235 LRKCLQRDPKKRPT 248
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
1086-1334 1.58e-38

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: 145.04  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYhgEYIDQAQNRiQCAIK--SLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGImLPPEGLPHVLLP 1163
Cdd:cd14014     5 VRLLGRGGMGEVY--RARDTLLGR-PVAIKvlRPELAEDEEFRERFLREARALARLSHPNIVRVYDV-GEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRspQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyySV 1242
Cdd:cd14014    81 YVEGGSLADLLR--ERGPlPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD----SG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHARL--PVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEY---CPDSL 1317
Cdd:cd14014   155 LTQTGSVLgtPA-YMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPPSPLnpdVPPAL 232
                         250
                  ....*....|....*..
gi 578806145 1318 YQVMQQCWEADPAVRPT 1334
Cdd:cd14014   233 DAIILRALAKDPEERPQ 249
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
1089-1334 3.83e-38

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: 144.27  E-value: 3.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLLPYMCH- 1167
Cdd:cd05042     3 IGNGWFGKVLLGE-IYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCV--EAIPYLLVMEFCDl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQR----NPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQ 1243
Cdd:cd05042    80 GDLKAYLRSEREhergDSDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDYIETD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHarLPVKWMALE-------SLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGR--RLPQPEY-- 1312
Cdd:cd05042   160 DKLW--FPLRWTAPElvtefhdRLLVVDQTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVVREQdtKLPKPQLel 237
                         250       260
                  ....*....|....*....|...
gi 578806145 1313 -CPDSLYQVMQQCWEAdPAVRPT 1334
Cdd:cd05042   238 pYSDRWYEVLQFCWLS-PEQRPA 259
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
1086-1345 9.60e-38

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: 143.25  E-value: 9.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAqnriqCAIKSLSRITEMQ---QVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLL 1162
Cdd:cd14147     8 EEVIGIGGFGKVYRGSWRGEL-----VAVKAARQDPDEDisvTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLC-LVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVkdLISFGLQVARGMEYLAEQKFV---HRDLAARN----------CMldESFTVKVADFG 1229
Cdd:cd14147    82 EYAAGGPLSRALAGRRVPPHV--LVNWAVQIARGMHYLHCEALVpviHRDLKSNNilllqpiendDM--EHKTLKITDFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1230 LARdildrEYYSVQQHRHARlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-RLP 1308
Cdd:cd14147   158 LAR-----EWHKTTQMSAAG-TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAYGVAVNKlTLP 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14147   231 IPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
1089-1352 3.87e-37

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 141.04  E-value: 3.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMqqvEAFLREGLLMRGLNHPNVLALIGIMLPPEGlPHVLLPYMCHG 1168
Cdd:cd14058     1 VGRGSFGVVCKARWRNQ-----IVAVKIIESESEK---KAFEVEVRQLSRVDHPNIIKLYGACSNQKP-VCLVMEYAEGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNP--TVKDLISFGLQVARGMEYL---AEQKFVHRDLAARNCMLDESFTV-KVADFGLARDIldREYYSV 1242
Cdd:cd14058    72 SLYNVLHGKEPKPiyTAAHAMSWALQCAKGVAYLhsmKPKALIHRDLKPPNLLLTNGGTVlKICDFGTACDI--STHMTN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHArlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHID--PFDLTHFLAQGRRLPQPEYCPDSLYQV 1320
Cdd:cd14058   150 NKGSAA-----WMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIGgpAFRIMWAVHNGERPPLIKNCPKPIESL 223
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1321 MQQCWEADPAVRPTFRvlvgEVEQIVSALLGD 1352
Cdd:cd14058   224 MTRCWSKDPEKRPSMK----EIVKIMSHLMQF 251
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
1090-1345 4.27e-37

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: 140.48  E-value: 4.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1090 GKGHFGVVYHGEYIDQAQnriQCAIKSLSRITemqqveaflREGLLMRGLNHPNVLALIGIMLPPeglPH--VLLPYMCH 1167
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDK---EVAVKKLLKIE---------KEAEILSVLSHRNIIQFYGAILEA---PNygIVTEYASY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKD-LISFGLQVARGMEYLAEQ---KFVHRDLAARNCMLDESFTVKVADFGLARdildreYYSVQ 1243
Cdd:cd14060    67 GSLFDYLNSNESEEMDMDqIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASR------FHSHT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPpYRHIDPFDLTHFLAQ-GRRLPQPEYCPDSLYQVMQ 1322
Cdd:cd14060   141 THMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVP-FKGLEGLQVAWLVVEkNERPTIPSSCPRSFAELMR 219
                         250       260
                  ....*....|....*....|...
gi 578806145 1323 QCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14060   220 RCWEADVKERPSFKQIIGILESM 242
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
1089-1334 6.37e-37

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: 140.86  E-value: 6.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRiQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGimLPPEGLPHVLLPYMCH- 1167
Cdd:cd14206     5 IGNGWFGKVILGEIFSDYTPA-QVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLG--LCTETIPFLLIMEFCQl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpQRNPT-------VKDLISF---GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR 1237
Cdd:cd14206    82 GDLKRYLRA-QRKADgmtpdlpTRDLRTLqrmAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNNYKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 EYYSVQQhrhaRL--PVKWMALESLQTYRF-------TTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHF-------- 1300
Cdd:cd14206   161 DYYLTPD----RLwiPLRWVAPELLDELHGnlivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFvvreqqmk 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578806145 1301 LAQGR-RLPQPEYcpdsLYQVMQQCWEAdPAVRPT 1334
Cdd:cd14206   237 LAKPRlKLPYADY----WYEIMQSCWLP-PSQRPS 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
1089-1336 3.28e-35

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: 134.93  E-value: 3.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQqveafLREgllMRGLNHPNVLALIGI-MLPPegLPHVLLPYMCH 1167
Cdd:cd14059     1 LGSGAQGAVFLGKFRGE-----EVAVKKVRDEKETD-----IKH---LRKLNHPNIIKFKGVcTQAP--CYCILMEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyySVQQHRH 1247
Cdd:cd14059    66 GQLYEVLRA-GREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEK---STKMSFA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1248 ArlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-RLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd14059   142 G--TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVGSNSlQLPVPSTCPDGFKLLMKQCWN 218
                         250
                  ....*....|
gi 578806145 1327 ADPAVRPTFR 1336
Cdd:cd14059   219 SKPRNRPSFR 228
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
1127-1335 2.83e-33

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: 130.31  E-value: 2.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1127 EAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDliSFGLQVARGMEYLAEQKFV 1206
Cdd:cd14027    36 EALLEEGKMMNRLRHSRVVKLLGVILE-EGKYSLVMEYMEKGNLMHVLKKVSVPLSVKG--RIILEIIEGMAYLHGKGVI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1207 HRDLAARNCMLDESFTVKVADFGLA-----------RDILDREYYSVQQHRHARLpvKWMALESLQTY--RFTTKSDVWS 1273
Cdd:cd14027   113 HKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeEHNEQREVDGTAKKNAGTL--YYMAPEHLNDVnaKPTEKSDVYS 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1274 FGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRlPQ----PEYCPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd14027   191 FAIVLWAIFANKEPYENAINEDQIIMCIKSGNR-PDvddiTEYCPREIIDLMKLCWEANPEARPTF 255
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
1089-1334 4.37e-33

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: 129.72  E-value: 4.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlpPEGLPHVLLPYMCH- 1167
Cdd:cd05087     5 IGHGWFGKVFLGE-VNSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQC--AEVTPYLLVMEFCPl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRS----PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQ 1243
Cdd:cd05087    82 GDLKGYLRScraaESMAPDPLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHarLPVKWMALE-------SLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHI-DPFDLTHFL-AQGRRLPQPEY-- 1312
Cdd:cd05087   162 DQLW--VPLRWIAPElvdevhgNLLVVDQTKQSNVWSLGVTIWELFELGNQPYRHYsDRQVLTYTVrEQQLKLPKPQLkl 239
                         250       260
                  ....*....|....*....|...
gi 578806145 1313 -CPDSLYQVMQQCWeADPAVRPT 1334
Cdd:cd05087   240 sLAERWYEVMQFCW-LQPEQRPT 261
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
1089-1343 8.60e-33

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: 128.28  E-value: 8.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAqnriqcAIKSLSRITEM-QQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglpHVLLPYMCH 1167
Cdd:cd14062     1 IGSGSFGTVYKGRWHGDV------AVKKLNVTDPTpSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ---LAIVTQWCE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GD-LLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdILDREYYSVQQHR 1246
Cdd:cd14062    72 GSsLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLA--TVKTRWSGSQQFE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQTYR---FTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAqGRRLPQPEY------CPDSL 1317
Cdd:cd14062   150 QPTGSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQILFMV-GRGYLRPDLskvrsdTPKAL 227
                         250       260
                  ....*....|....*....|....*.
gi 578806145 1318 YQVMQQCWEADPAVRPTFRVLVGEVE 1343
Cdd:cd14062   228 RRLMEDCIKFQRDERPLFPQILASLE 253
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
1089-1335 1.41e-32

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: 127.95  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYID-QAQNRIQCAIKSLSRITEMqqvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPYMCH 1167
Cdd:cd13978     1 LGSGGFGTVSKARHVSwFGMVAIKCLHSSPNCIEER---KALLKEAEKMERARHSYVLPLLGVCVERRSLGLVM-EYMEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDL--LQFIRSPQRNPTVKdlISFGLQVARGMEYL--AEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreyYSVQ 1243
Cdd:cd13978    77 GSLksLLEREIQDVPWSLR--FRIIHEIALGMNFLhnMDPPLLHHDLKPENILLDNHFHVKISDFGLSK-------LGMK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPVK--------WMALESLQT--YRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRR------- 1306
Cdd:cd13978   148 SISANRRRGTenlggtpiYMAPEAFDDfnKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRpslddig 227
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1307 LPQPEYCPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd13978   228 RLKQIENVQELISLMIRCWDGNPDARPTF 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
1087-1334 1.63e-32

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 127.32  E-value: 1.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdqaQNRIQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05122     6 EKIGKGGFGVVYKARHK---KTGQIVAIKKIN-LESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDEL-WIVMEFCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSpqRNPTVKD-LISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyysvqQ 1244
Cdd:cd05122    81 GGSLKDLLKN--TNKTLTEqQIAYvCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDG------K 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPVK-WMALESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGR--RLPQPEYCPDSLYQVM 1321
Cdd:cd05122   153 TRNTFVGTPyWMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKPPYSELPPMKALFLIATNGppGLRNPKKWSKEFKDFL 231
                         250
                  ....*....|...
gi 578806145 1322 QQCWEADPAVRPT 1334
Cdd:cd05122   232 KKCLQKDPEKRPT 244
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
1089-1345 2.52e-32

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: 127.39  E-value: 2.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNriqcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPeGLPHVLLPYMCHG 1168
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVV----AVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLES-DEKLLVYEYMPNG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRspqRNPTVKDL-------ISFGlqVARGMEYLAEQKF---VHRDLAARNCMLDESFTVKVADFGLARDILDRE 1238
Cdd:cd14066    76 SLEDRLH---CHKGSPPLpwpqrlkIAKG--IARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYSVQQHRHARLPvkWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPF---DLTHFLAQGRR--------- 1306
Cdd:cd14066   151 SVSKTSAVKGTIG--YLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENAsrkDLVEWVESKGKeeledildk 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1307 -----LPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14066   229 rlvddDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
1089-1342 2.62e-32

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: 126.84  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIqcaIKSLSRITEMQqveAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYMCHG 1168
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMV---MKELKRFDEQR---SFLKEVKLMRRLSHPNILRFIGVCVK-DNKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDES---FTVKVADFGLARDILDreYYSVQQH 1245
Cdd:cd14065    74 TLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREAnrgRNAVVADFGLAREMPD--EKTKKPD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTR--GAPPY--RHIDpFDLThflAQGRRLPQPEYCPDSL 1317
Cdd:cd14065   152 RKKRLTVvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRvpADPDYlpRTMD-FGLD---VRAFRTLYVPDCPPSF 227
                         250       260
                  ....*....|....*....|....*
gi 578806145 1318 YQVMQQCWEADPAVRPTFRVLVGEV 1342
Cdd:cd14065   228 LPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
1089-1338 2.66e-32

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: 126.96  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRIqCAIK--SLSRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd06627     8 IGRGAFGSVYKG--LNLNTGEF-VAIKqiSLEKIPK-SDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSL-YIILEYVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPtvKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI--LDREYYSVQ 1243
Cdd:cd06627    83 NGSLASIIKKFGKFP--ESLVAVYIyQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLneVEKDENSVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QhrharlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQ 1323
Cdd:cd06627   161 G------TPYWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDDHPPLPENISPELRDFLLQ 233
                         250
                  ....*....|....*
gi 578806145 1324 CWEADPAVRPTFRVL 1338
Cdd:cd06627   234 CFQKDPTLRPSAKEL 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1087-1333 4.26e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 132.06  E-value: 4.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRiQCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGImLPPEGLPHVLLPY 1164
Cdd:COG0515    13 RLLGRGGMGVVYLAR--DLRLGR-PVALKVLrpELAADPEARERFRREARALARLNHPNIVRVYDV-GEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRnPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysVQQ 1244
Cdd:COG0515    89 VEGESLADLLRRRGP-LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGAT---LTQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPD---SLYQVM 1321
Cdd:COG0515   165 TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSELRPDlppALDAIV 243
                         250
                  ....*....|..
gi 578806145 1322 QQCWEADPAVRP 1333
Cdd:COG0515   244 LRALAKDPEERY 255
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
1089-1338 8.98e-32

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: 126.08  E-value: 8.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHgeyIDQAQNRIQCAIKSLSRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd14154     1 LGKGFFGQAIK---VTHRETGEVMVMKELIRFDEEAQ-RNFLKEVKVMRSLDHPNVLKFIGVLYKDKKL-NLITEYIPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD-----REYYSVQ 1243
Cdd:cd14154    76 TLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEerlpsGNMSPSE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPVK-----------WMALESLQTYRFTTKSDVWSFGVLLWELLTR--GAPPY--RHIDpFDLTHFLAQGRRLP 1308
Cdd:cd14154   156 TLRHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRveADPDYlpRTKD-FGLNVDSFREKFCA 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 578806145 1309 QpeyCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd14154   235 G---CPPPFFKLAFLCCDLDPEKRPPFETL 261
IPT_plexin_repeat2 cd01179
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
684-768 9.91e-32

Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238584  Cd Length: 85  Bit Score: 119.25  E-value: 9.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWT 763
Cdd:cd01179     1 PSITSLSPSYGPQSGGTRLTITGKHLNAGSSVRVTVGGQPCKILSVSSSQIVCLTPPSASPGEAPVKVLIDGARRLAPLV 80

                  ....*
gi 578806145  764 FQYRE 768
Cdd:cd01179    81 FTYTE 85
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
1089-1334 1.60e-31

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


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 125.36  E-value: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGE-YIDQAQNRIqcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLLPYMCH 1167
Cdd:cd05086     5 IGNGWFGKVLLGEiYTGTSVARV--VVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCV--EAIPYLLVFEFCD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 -GDLLQFIRSPQ----RNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd05086    81 lGDLKTYLANQQeklrGDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKEDYIET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHArlPVKWMALESLQTYR-------FTTKSDVWSFGVLLWELLTRGAPPYRHIDPFD-LTHFLAQGR-RLPQPEY- 1312
Cdd:cd05086   161 DDKKYA--PLRWTAPELVTSFQdgllaaeQTKYSNIWSLGVTLWELFENAAQPYSDLSDREvLNHVIKERQvKLFKPHLe 238
                         250       260
                  ....*....|....*....|....
gi 578806145 1313 --CPDSLYQVMQQCWeADPAVRPT 1334
Cdd:cd05086   239 qpYSDRWYEVLQFCW-LSPEKRPT 261
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
1089-1343 2.65e-31

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: 124.18  E-value: 2.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidqaQNRIqCAIKSLSRIT--EMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC 1166
Cdd:cd14064     1 IGSGSFGKVYKGRC----RNKI-VAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTQYVS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAE--QKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyYSVQQ 1244
Cdd:cd14064    76 GGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFL-----QSLDE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLP--VKWMALESL-QTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-RLPQPEYCPDSLYQV 1320
Cdd:cd14064   151 DNMTKQPgnLRWMAPEVFtQCTRYSIKADVFSYALCLWELLT-GEIPFAHLKPAAAAADMAYHHiRPPIGYSIPKPISSL 229
                         250       260
                  ....*....|....*....|...
gi 578806145 1321 MQQCWEADPAVRPTFRVLVGEVE 1343
Cdd:cd14064   230 LMRGWNAEPESRPSFVEIVALLE 252
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
65-563 7.18e-31

The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 128.90  E-value: 7.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   65 RNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-PGC------QTCAAcgpgpHGPPGDTDTKVLVLDPALPALVSCGS 137
Cdd:cd11272    20 QSTGAVYVGAINRVYKLSGNLTILVAHKTGPEEDnKSCypplivQPCSE-----VLTLTNNVNKLLIIDYSENRLLACGS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  138 SLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPddcpdcvasplGTR--VTVVEQGQASYFYVASSLDAAvaASFSPrS 215
Cdd:cd11272    95 LYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKT-----------GTMygVIVRSEGEDGKLFIGTAVDGK--QDYFP-T 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  216 VSIRRLKADA-----------SGFAPGFVALSVLPKHLVS-YSIEYVHSFHTGAFVYFLTVQPAS----VTDDPSALH-- 277
Cdd:cd11272   161 LSSRKLPRDPessamldyelhSDFVSSLIKIPSDTLALVShFDIFYIYGFASGNFVYFLTVQPETpegvSINSAGDLFyt 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  278 TRLARLSATEPELGDYRELVLDCrfapkrrrrgaPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGG 357
Cdd:cd11272   241 SRIVRLCKDDPKFHSYVSLPFGC-----------VRGGVEYRLLQAAYLSKPGEVLARSLNITAQEDVLFAIFSKGQKQY 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  358 PGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRgldffqspsfcpnppgleALSPNTSCRHFPLLVSSSFSRVD 437
Cdd:cd11272   310 HHPPDDSALCAFPIRAINAQIKERLQSCYQGEGNLELNW------------------LLGKDVQCTKAPVPIDDNFCGLD 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  438 LFNGLLG--PVQVTALYVTRLDNVT-----------VAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSR 504
Cdd:cd11272   372 INQPLGGstPVEGVTLYTSSRDRLTsvasyvyngysVVFVGTKSGKLKKIRADGPPHGGVQYEMVSVFKDGSPILRDMAF 451
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806145  505 LGDH--LLFASGDQVFQVPIQgpGCRHFLTCGRCLRAW--HfmgCGWCG--NMCGQQKECPGSWQ 563
Cdd:cd11272   452 SIDHkyLYVMSERQVSRVPVE--SCEQYTTCGECLSSGdpH---CGWCAlhNMCSRRDKCQRAWE 511
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
1089-1345 2.34e-30

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: 121.66  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAqnriqcAIKSLsRITE--MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglpHVLLPYMC 1166
Cdd:cd14150     8 IGTGSFGTVFRGKWHGDV------AVKIL-KVTEptPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN---FAIITQWC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGD-LLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdILDREYYSVQQH 1245
Cdd:cd14150    78 EGSsLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLA--TVKTRWSGSQQV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVKWMALESLQ---TYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAqGRRLPQPEY------CPDS 1316
Cdd:cd14150   156 EQPSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDQIIFMV-GRGYLSPDLsklssnCPKA 233
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1317 LYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14150   234 MKRLLIDCLKFKREERPLFPQILVSIELL 262
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
1089-1349 2.02e-29

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: 119.40  E-value: 2.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAqnriqcAIKSLSRITEM-QQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglpHVLLPYMCH 1167
Cdd:cd14151    16 IGSGSFGTVYKGKWHGDV------AVKMLNVTAPTpQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---LAIVTQWCE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GD-LLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdILDREYYSVQQHR 1246
Cdd:cd14151    87 GSsLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA--TVKSRWSGSHQFE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQ---TYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAqGRRLPQPEY------CPDSL 1317
Cdd:cd14151   165 QLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMV-GRGYLSPDLskvrsnCPKAM 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1318 YQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd14151   243 KRLMAECLKKKRDERPLFPQILASIELLARSL 274
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
1089-1336 1.43e-28

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 116.17  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSRitemQQVEAFLREGLL-----MRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGE---VVAIKEISR----KKLNKKLQENLEseiaiLKSIKHPNIVRLYDVQKTEDFI-YLVLE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNP--TVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARdildre 1238
Cdd:cd14009    73 YCAGGDLSQYIRKRGRLPeaVAR---HFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFAR------ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 yySVQQHRHARL----PVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFL-AQGRRLPQPEY- 1312
Cdd:cd14009   144 --SLQPASMAETlcgsPL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRGSNHVQLLRNIeRSDAVIPFPIAa 219
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1313 -----CPDSLYQVMQQcweaDPAVRPTFR 1336
Cdd:cd14009   220 qlspdCKDLLRRLLRR----DPAERISFE 244
IPT_plexin_repeat1 cd01180
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
569-683 8.68e-28

First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238585  Cd Length: 94  Bit Score: 108.17  E-value: 8.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  569 PKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSglvpEGTHQVTVGQSPCRPLPkdssklrpvPRKDFVEEFECELEPLGTQ 648
Cdd:cd01180     1 PVITEFFPLSGPLEGGTRLTICGSNLGLRKN----DVRHGVRVGGVPCNPEP---------PEYSSSEKIVCTTGPAGNP 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578806145  649 aVGPTNVSLTVTNMPpgkhfrvDGTSVLRGFSFME 683
Cdd:cd01180    68 -VFNGPVEVTVGHGS-------FRTESSEGFSFVD 94
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
1089-1338 1.05e-27

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: 113.90  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGV---VYH---GEYIdqaqnriqcAIKSLSRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd14221     1 LGKGCFGQaikVTHretGEVM---------VMKELIRFDEETQ-RTFLKEVKVMRCLEHPNVLKFIGVLYKDKRL-NFIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd14221    70 EYIKGGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 ------QQHRHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTR--GAPPY--RHID-PFDLTHFLAQGrrl 1307
Cdd:cd14221   150 glrslkKPDRKKRYTVvgnpYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRvnADPDYlpRTMDfGLNVRGFLDRY--- 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578806145 1308 pQPEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd14221   227 -CPPNCPPSFFPIAVLCCDLDPEKRPSFSKL 256
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
1089-1349 1.50e-27

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: 112.95  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYMCHG 1168
Cdd:cd14155     1 IGSGFFSEVY------KVRHRTSGQVMALKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVH-QGQLHALTEYINGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNP-TVKdlISFGLQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARDILDREYysvqq 1244
Cdd:cd14155    74 NLEQLLDSNEPLSwTVR--VKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDYSD----- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 hRHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTR--GAPPY--RHIDpFDLThFLAQGRRLPQpeyCPDS 1316
Cdd:cd14155   147 -GKEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARiqADPDYlpRTED-FGLD-YDAFQHMVGD---CPPD 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578806145 1317 LYQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd14155   221 FLQLAFNCCNMDPKSRPSFHDIVKTLEEILEKL 253
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
1089-1338 5.10e-27

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: 112.34  E-value: 5.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFG---VVYHgeyidQAQNRIQcAIKSLSRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd14222     1 LGKGFFGqaiKVTH-----KATGKVM-VMKELIRCDEETQ-KTFLTEVKVMRSLDHPNVLKFIGVLYKDKRL-NLLTEFI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDlISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD--------- 1236
Cdd:cd14222    73 EGGTLKDFLRADDPFPWQQK-VSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEekkkpppdk 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 ---REYYSVQQHRHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTRgappyRHIDPFDLTHFLAQGRRLPQ 1309
Cdd:cd14222   152 pttKKRTLRKNDRKKRYTVvgnpYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQ-----VYADPDCLPRTLDFGLNVRL 226
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578806145 1310 ------PEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd14222   227 fwekfvPKDCPPAFFPLAAICCRLEPDSRPAFSKL 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
1088-1334 5.21e-27

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: 112.07  E-value: 5.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNriqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd06610     8 VIGSGATAVVYAAYCLPKKEK---VAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDEL-WLVMPLLSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpqRNPT---VKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyySVQ 1243
Cdd:cd06610    84 GSLLDIMKS--SYPRgglDEAIIATVLkEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLAT----GGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPVK----WMALESLQTYR-FTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRlPQPEYCPD--- 1315
Cdd:cd06610   158 RTRKVRKTFVgtpcWMAPEVMEQVRgYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLMLTLQNDP-PSLETGADykk 235
                         250       260
                  ....*....|....*....|..
gi 578806145 1316 ---SLYQVMQQCWEADPAVRPT 1334
Cdd:cd06610   236 yskSFRKMISLCLQKDPSKRPT 257
Pkinase pfam00069
Protein kinase domain;
1084-1336 8.45e-27

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 109.64  E-value: 8.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1084 HSDRVIGKGHFGVVYHGeyIDQAQNRIqCAIKSL--SRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVL 1161
Cdd:pfam00069    2 EVLRKLGSGSFGTVYKA--KHRDTGKI-VAIKKIkkEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNL-YLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1162 LPYMCHGDLLQFIRsPQRNPTVKDLISFGLQVARGMEYlaeqkfvhrdlaarncmlDESFTVKVADFGlardildreyys 1241
Cdd:pfam00069   77 LEYVEGGSLFDLLS-EKGAFSEREAKFIMKQILEGLES------------------GSSLTTFVGTPW------------ 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  1242 vqqhrharlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDL-THFLAQGRRLPQ-PEYCPDSLYQ 1319
Cdd:pfam00069  126 ------------YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIyELIIDQPYAFPElPSNLSEEAKD 192
                          250
                   ....*....|....*..
gi 578806145  1320 VMQQCWEADPAVRPTFR 1336
Cdd:pfam00069  193 LLKKLLKKDPSKRLTAT 209
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
321-502 1.67e-26

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 107.74  E-value: 1.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   321 LRVAHSAPVGAQLATElsiaegqEVLFGVFVTGKDGGPGvgpNSVVCAFPIDLLDTLIdEGVERCCESPVHPGLRR-GLD 399
Cdd:pfam01403    1 LQDVFVLKPGAGDALD-------TVLYGVFTTQWSNSIG---GSAVCAFSLSDINAVF-EGPFKEQEKSDSKWLPYtGKV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   400 FFQSPSFCPNPPGLEALSPNTSC--RHFPLLVSS--SFSRVDLFNGLLgpVQVTALYVTRLD----NVTVAHMGTMDGRI 471
Cdd:pfam01403   70 PYPRPGTCINDPLRLDLPDSVLNfvKDHPLMDEAvqPVGGRPLLVRTG--VRLTSIAVDRVQaldgNYTVLFLGTDDGRL 147
                          170       180       190
                   ....*....|....*....|....*....|.
gi 578806145   472 LQVELVRSlNYLLYVSNFSLGDSGQPVQRDV 502
Cdd:pfam01403  148 HKVVLVGS-EESHIIEEIQVFPEPQPVLNLL 177
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
1087-1334 2.20e-26

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: 109.86  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyidQAQNRIQCAIK--SLSRITEMQQVEAfLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd08215     6 RVIGKGSFGSAYLVR---RKSDGKLYVLKeiDLSNMSEKEREEA-LNEVKLLSKLKHPNIVKYYESFEENGKL-CIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFI---RSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDRE--- 1238
Cdd:cd08215    81 ADGGDLAQKIkkqKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK-VLESTtdl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 --------YYsvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTRgappyRHidPFDLTHFLA------QG 1304
Cdd:cd08215   160 aktvvgtpYY--------------LSPELCENKPYNYKSDIWALGCVLYELCTL-----KH--PFEANNLPAlvykivKG 218
                         250       260       270
                  ....*....|....*....|....*....|
gi 578806145 1305 RRLPQPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd08215   219 QYPPIPSQYSSELRDLVNSMLQKDPEKRPS 248
Sema_plexin_A3 cd11273
The Sema domain, a protein interacting module, of Plexin A3; Plexin-A3 forms a receptor ...
65-523 4.46e-26

The Sema domain, a protein interacting module, of Plexin A3; Plexin-A3 forms a receptor complex with neuropilin-2 and transduces signals for class 3 semaphorins in the nervous system. Both plexins A3 and A4 are essential for normal sympathetic neuron development. They function cooperatively to regulate the migration of sympathetic neurons, and differentially to guide sympathetic axons. Both plexins A3 and A4 are not required for guiding neural crest precursors prior to reaching the sympathetic anlagen. Plexin A3 is a major driving force for intraspinal motor growth cone guidance. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200534 [Multi-domain]  Cd Length: 469  Bit Score: 113.88  E-value: 4.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   65 RNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-------PGCQTCAacgpgPHGPPGDTDTKVLVLDPALPALVSCGS 137
Cdd:cd11273    20 RVTGEVFVGAVNRVYKLSANLTELRAHVTGPVEDnarcyppPSVRVCA-----HRLAPVDNVNKLLLVDYAGNRLVACGS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  138 SLQGRCFLHDLEpqgTAVHLAAPaclfsahHNRPDDCPDCVASPLGTRVTVVEQGQA-SYFYVASSLDAAvaASFSPrSV 216
Cdd:cd11273    95 IWQGVCQFLRLE---DLFKLGEP-------HHRKEHYLSGAQEPDSMAGVIVEQGKGpSKLFVGTAIDGK--SEYFP-TL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  217 SIRRLKADASG-------FAPGFVALSV-LPKHLVS----YSIEYVHSFHTGAFVYFLTVQPAS-----VTDDPSALHTR 279
Cdd:cd11273   162 SSRKLISDEDSadmfslvYQDEFVSSQIkIPSDTLSlypaFDIYYVYGFVSASFVYFLTLQLDTqqtllDTAGEKFFTSK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  280 LARLSATEPELGDYRELVLDCRfapkrrrrgapEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPG 359
Cdd:cd11273   242 IVRMCANDTEFYSYVEFPLGCS-----------KDGVEYRLVQAAHLAKPGLLLAQALGVPEDEDVLFTIFSQGQKNRAS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  360 VGPNSVVCAFPIDLLDTLIDEGVERCcespvhpglRRGLDFFQSPSFcpnppgleaLSPNTSCRHFPLLVSSSFSRVDLf 439
Cdd:cd11273   311 PPRETILCLFTLSNINAHIRERIQSC---------YRGEGTLSLPWL---------LNKELPCINTPMQINGNFCGLVL- 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  440 NGLLGPVQVT---ALYVTRLDNV-----------TVAHMGTMDGRILQVELVRSLNYLLYVSNFSLgdSGQPVQRDVSRL 505
Cdd:cd11273   372 NQPLGGLHVIeglPLLADSTDGMasvaaytyrqhSVVFIGTRSGSLKKVRVDGFQDAHLYETVPVV--DGSPILRDMVFS 449
                         490       500
                  ....*....|....*....|
gi 578806145  506 GD--HLLFASGDQVFQVPIQ 523
Cdd:cd11273   450 PDhrYIYLLSEKQVSQLPVE 469
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
1089-1349 7.34e-26

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: 108.97  E-value: 7.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAqnriqcAIKSLSRITEM-QQVEAFLREGLLMRGLNHPNVLALIGIMLPPEglpHVLLPYMCH 1167
Cdd:cd14149    20 IGSGSFGTVYKGKWHGDV------AVKILKVVDPTpEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN---LAIVTQWCE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GD-LLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdILDREYYSVQQHR 1246
Cdd:cd14149    91 GSsLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA--TVKSRWSGSQQVE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPVKWMALESLQTYR---FTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAqGRRLPQPEY------CPDSL 1317
Cdd:cd14149   169 QPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMT-GELPYSHINNRDQIIFMV-GRGYASPDLsklyknCPKAM 246
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1318 YQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd14149   247 KRLVADCIKKVKEERPLFPQILSSIELLQHSL 278
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
1127-1342 1.35e-24

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: 104.87  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1127 EAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFV 1206
Cdd:cd05037    47 ESFFETASLMSQISHKHLVKLYGVCVADENI--MVQEYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1207 HRDLAARNCML------DESFTVKVADFGLARDILDREYysvqqhRHARLPvkWMALESLQ--TYRFTTKSDVWSFGVLL 1278
Cdd:cd05037   125 HGNVRGRNILLaregldGYPPFIKLSDPGVPITVLSREE------RVDRIP--WIAPECLRnlQANLTIAADKWSFGTTL 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1279 WELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPdsLYQVMQQCWEADPAVRPTFRVLVGEV 1342
Cdd:cd05037   197 WEICSGGEEPLSALSSQEKLQFYEDQHQLPAPDCAE--LAELIMQCWTYEPTKRPSFRAILRDL 258
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1087-1288 1.42e-24

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: 104.48  E-value: 1.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdqaQNRIQCAIKSLS-RITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd05117     6 KVLGRGSFGVVRLAVHK---KTGEEYAVKIIDkKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNL-YLVMELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFI--RSPQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARDIldreyy 1240
Cdd:cd05117    82 TGGELFDRIvkKGSFSEREAAKIMK---QILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIF------ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1241 svQQHRHARLPV---KWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPP 1288
Cdd:cd05117   153 --EEGEKLKTVCgtpYYVAPEVLKGKGYGKKCDIWSLGVILYILLC-GYPP 200
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1087-1334 2.90e-24

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: 103.47  E-value: 2.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeyIDQAQNRIqCAIKSLSRITEMQqvEAFLREGLLMRGLN----HPNVLALIG-IMLPPEGLPHVL 1161
Cdd:cd05118     5 RKIGEGAFGTVWLA--RDKVTGEK-VAIKKIKNDFRHP--KAALREIKLLKHLNdvegHPNIVKLLDvFEHRGGNHLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMcHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDILDREYY 1240
Cdd:cd05118    80 FELM-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSFTSPPYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQHRHARLPvkwmalESLQTYRFTTKS-DVWSFGVLLWELLTrGAPPYRHIDPFDlthFLAQGRRLPQPEYCPDslyq 1319
Cdd:cd05118   159 PYVATRWYRAP------EVLLGAKPYGSSiDIWSLGCILAELLT-GRPLFPGDSEVD---QLAKIVRLLGTPEALD---- 224
                         250
                  ....*....|....*
gi 578806145 1320 VMQQCWEADPAVRPT 1334
Cdd:cd05118   225 LLSKMLKYDPAKRIT 239
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
1089-1284 5.50e-24

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: 104.32  E-value: 5.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDqaqNRIQCAIKslsRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIML--PPE-----GL 1157
Cdd:cd07866    16 LGEGTFGEVYKARQIK---TGRVVALK---KILMHNEKDGFpitaLREIKILKKLKHPNVVPLIDMAVerPDKskrkrGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1158 PHVLLPYMCHgDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI--- 1234
Cdd:cd07866    90 VYMVTPYMDH-DLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYdgp 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1235 ----------LDREYYSVQQHRHARLPvkwmalE-SLQTYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07866   169 ppnpkgggggGTRKYTNLVVTRWYRPP------ElLLGERRYTTAVDIWGIGCVFAEMFTR 223
Sema_plexin_A cd11244
The Sema domain, a protein interacting module, of Plexin A; Plexins serve as receptors of ...
64-523 1.03e-23

The Sema domain, a protein interacting module, of Plexin A; Plexins serve as receptors of semaphorins and may be the ancestor of semaphorins. Members of the Plexin A subfamily are receptors for Sema1s, Sema3s, and Sema6s, and they mediate diverse biological functions including axon guidance, cardiovascular development, and immune function. Guanylyl cyclase Gyc76C and Off-track kinase (OTK), a putative receptor tyrosine kinase, modulate Sema1a-Plexin A mediated axon repulsion. Sema3s do not interact directly with plexin A receptors, but instead bind Neuropilin-1 or Neuropilin-2 toactivate neuropilin-plexin A holoreceptor complexes. In contrast to Sema3s, Sema6s do not require neuropilins for plexin A binding. In the complex, plexin As serve as signal-transducing subunits. An increasing number of molecules that interact with the intracellular region of Plexin A have been identified; among them are IgCAMs (in axon guidance events) and Trem2-DAP12 (in immune responses). The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200505 [Multi-domain]  Cd Length: 470  Bit Score: 106.45  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-------PGCQTCAacgpgPHGPPGDTDTKVLVLDPALPALVSCG 136
Cdd:cd11244    19 HRRTGEVYVGAINRVYKLSSNLTVLVTHETGPVEDnpkcyppPIVQTCN-----EPLTTTNNVNKLLLIDYSENRLIACG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  137 SSLQGRCFLHDLEpqgTAVHLAAPaclfsaHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAvaASFSPrSV 216
Cdd:cd11244    94 SLYQGVCKLLRLE---DLFKLGEP------HHKKEHYLSGVNESGTMFGVIVSYSNGDDKLFIGTAVDGK--SEYFP-TL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  217 SIRRLKADASG-------FAPGFVA---------LSVLPkhlvSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSA----- 275
Cdd:cd11244   162 SSRKLTADEESdgmfayvYHDEFVSsqikipsdtLSIIP----DFDIYYVYGFSSGNFVYFLTLQPETQLTPGDStgeqf 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  276 LHTRLARLSATEPELGDYRELVLDCRfapkrrrrgapEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKD 355
Cdd:cd11244   238 YTSKIVRLCKDDTKFYSYVEFPIGCT-----------RDGVEYRLLQAAYLSKPGKALAQALGISEDEDVLFTIFSKGQK 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  356 GGPGVGPNSVVCAFPIDLLDTLIDEGVERCcespvhpglRRGLDFFQSPSFcpnppgleaLSPNTSCRHFPLLVSSSFSR 435
Cdd:cd11244   307 NRMKPPDESALCLFTLKQINLRIKERLQSC---------YRGEGKLSLPWL---------LNKDLPCINAPLQIDDNFCG 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  436 VDlFNGLLG---PVQVTALYVTRLDNVT-----------VAHMGTMDGRI--LQVELVRSlNYLLY--VSNFslgdSGQP 497
Cdd:cd11244   369 LD-MNQPLGgsdMVEGIPLFTDDRDRMTsvaayvykghsVVFVGTKSGKLkkIRVDGPPH-NALQYetVQVV----EGSP 442
                         490       500
                  ....*....|....*....|....*...
gi 578806145  498 VQRDV--SRLGDHLLFASGDQVFQVPIQ 523
Cdd:cd11244   443 ILRDMafSPDHQYLYIMSERQVTRVPVE 470
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
70-523 1.03e-23

The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor plays important roles in neural tube closure and cerebellar granule cell development. Mice lacking Plexin B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C-Plexin B2 signaling modulates ureteric branching. Plexin B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin B2 results in renal hypoplasia and occasional double ureters. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 106.01  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   70 VFVAIRNRLHVLGPDLKSVQSLATGPAGD-PGCQ---TCAACGPGPhgppgDTDT--KVLVLDPALPALVSCGSSLQGRC 143
Cdd:cd11276    20 VYLGAVNALYQLDADLQLESRVETGPKKDnKKCTppiEENQCTEAK-----MTDNynKLLLLDSANKTLVVCGSLFKGIC 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  144 FLHDLEPQGTAVHLAAPACLFSAhhnrpddcpdcVASPlGTRVTVV------EQGQASYFYVAS---SLDAAVAAS---- 210
Cdd:cd11276    95 SLRNLSNISEVIYYSDTSGEKSF-----------VASN-DEGVSTVglisslKPGNDRVFFVGKgngSNDNGKIIStrll 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  211 FSPRSVSIRRLKADASGFAPGFVAlsvlpkhlvSYSIEYVHSFHTGAFVYFLTVQpasvTDDPSALH-TRLARLSATEPE 289
Cdd:cd11276   163 QNYDDREVFENYIDAATVKSAYVS---------RYTQQFRYAFEDNNYVYFLFNQ----QLGHPDKNrTLIARLCENDHH 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  290 LGDYRELVLDCRfapkrrrrgapEGGQPYPVLRVAHSAPVGAQLATEL-SIAEGQEVLFGVFvtGKDGGPGVGpnSVVCA 368
Cdd:cd11276   230 YYSYTEMDLNCR-----------DGANAYNKCQAAYVSTPGKELAQNYgNSILSDKVLFAVF--SRDEKDSGE--SALCM 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  369 FPIDLLDTLIDEGVERCcespvHPGLRRGLDFFQSP--SFCPNPPGLEA--LSPNTSC--RHFPLLVSSSfSRVDLFNGL 442
Cdd:cd11276   295 FPLKSINAKMEANREAC-----YTGTIDDRDVFYKPfhSQKDIICGSHQqkNSKSFPCgsEHLPYPLGSR-DELALTAPV 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  443 L--GPVQVTALYVTRLDNVTVAHMGTMDGRILQVELvrSLNYLLYVSnfSLGDSGQPVQRDV--SRLGDHLLFASGDQVF 518
Cdd:cd11276   369 LqrGGLNLTAVTVAVENGHTVAFLGTSDGRILKVHL--SPDPEEYNS--ILIEKNKPVNKDLvlDKTLEHLYIMTEDKVF 444

                  ....*
gi 578806145  519 QVPIQ 523
Cdd:cd11276   445 RLPVQ 449
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
1087-1290 1.16e-23

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: 101.88  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdQAQNRIQCAIKSLSR-ITEMQQVEAFL-REGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd14080     6 KTIGEGSYSKVKLAEYT-KSGLKEKVACKIIDKkKAPKDFLEKFLpRELEILRKLRHPNIIQVYSIFERGSKV-FIFMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIrspQRNPTVKDLIS--FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREY--- 1239
Cdd:cd14080    84 AEHGDLLEYI---QKRGALSESQAriWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGdvl 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1240 ---------YSvqqhrharlpvkwmALESLQT--YRfTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd14080   161 sktfcgsaaYA--------------APEILQGipYD-PKKYDIWSLGVILYIMLC-GSMPFD 206
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
1087-1338 5.98e-23

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: 100.40  E-value: 5.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeyIDQAQNRIqCAIK------SLSRITEMQQVEAFLREgllmrgLNHPNVLALIGIMLPPEGLpHV 1160
Cdd:cd06609     7 ERIGKGSFGEVYKG--IDKRTNQV-VAIKvidleeAEDEIEDIQQEIQFLSQ------CDSPYITKYYGSFLKGSKL-WI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSpqrNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRey 1239
Cdd:cd06609    77 IMEYCGGGSVLDLLKP---GPLDETYIAFILrEVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTST-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 ySVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLThFLAQGR---RLPQPEYCPDs 1316
Cdd:cd06609   152 -MSKRNTFVGTPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVL-FLIPKNnppSLEGNKFSKP- 226
                         250       260
                  ....*....|....*....|..
gi 578806145 1317 LYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06609   227 FKDFVELCLNKDPKERPSAKEL 248
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
1087-1284 6.49e-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: 101.45  E-value: 6.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeyIDQAQNRiQCAIKSLSRITEmQQVEA--FLREGLLMRGLNHPNVLALIGIMLPPEGLP----HV 1160
Cdd:cd07834     6 KPIGSGAYGVVCSA--YDKRTGR-KVAIKKISNVFD-DLIDAkrILREIKILRHLKHENIIGLLDILRPPSPEEfndvYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMcHGDLLQFIRSPQrnPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREY 1239
Cdd:cd07834    82 VTELM-ETDLHKVIKSPQ--PLTDDHIQYFLyQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDED 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1240 ------YSVqqHRHARLPvkwmalE---SLQTYrftTKS-DVWSFGVLLWELLTR 1284
Cdd:cd07834   159 kgflteYVV--TRWYRAP------ElllSSKKY---TKAiDIWSVGCIFAELLTR 202
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
64-523 6.97e-23

The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin domains, function as receptors of semaphorins and may be the ancestors of semaphorins. There are three members of the Plexin B subfamily, namely B1, B2 and B3. Plexins B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin B signaling. Plexin B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 103.47  E-value: 6.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-PGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGR 142
Cdd:cd11245     8 DPQTGRLYLGAVNGLFQLSPNLQLESRADTGPKKDsPQCLPPITAAECPQAKETDNFNKLLLVNSANGTLVVCGSLFQGV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  143 CFLHDLEPQGTAVHlaapaclfsahhnRPDDCPDC--VAS--PLGTRVTVVEQGQA--SYFYVASSLDAAVAASFSPrsV 216
Cdd:cd11245    88 CELRNLNSVNKPLY-------------RPETPGDKqyVAAnePSVSTVGLISYFKDglSLLFVGRGYTSSLSGGIPP--I 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  217 SIRRLK--ADASGFAPGFVALSVLPKhLVSYSIEYVHSFHTGAFVYFLTVQPASVTDdpSALHTRLARLSATEPELGDYR 294
Cdd:cd11245   153 TTRLLQehGEMDAFSNEVEAKLVVGS-ASRYHHDFVYAFADNGYIYFLFSRRPGTAD--STKRTYISRLCENDHHYYSYV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  295 ELVLDCRFAPKRRrrgapeggqpYPVLRVAHSAPVGAqlatelsIAEGqEVLFGVFVTGKDGGPGVGPNSVVCAFPIDLL 374
Cdd:cd11245   230 ELPLNCTVNQENT----------YNLVQAAYLAKPGK-------VLNG-KVLFGVFSADEASTAAPDGRSALCMYPLSSV 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  375 DTLIDEGVERCCESPV--HPGLRRGLDFFQSPSFCPNPP--GLEAL------SPNTSCRHFPLLVSSSFSRVDlfngllg 444
Cdd:cd11245   292 DARFERTRESCYTGEGleDDKPETAYIEYNVKSICKTLPdkNVKAYpcgaehTPSPLASRYPLAAKPILTRND------- 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  445 pvQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNyllYVSNFSLGDSGQPVQRDV--SRLGDHLLFASGDQVFQVPI 522
Cdd:cd11245   365 --MLTAVAVAVENGHTIAFLGDSGGQLHKVYLDPNHT---DFYSTIPGDQDSAVNKDLlfDSTLNHLYVMTGKKISKVPV 439

                  .
gi 578806145  523 Q 523
Cdd:cd11245   440 Q 440
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
1079-1339 7.02e-23

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: 100.13  E-value: 7.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1079 ERVVTHSDRvIGKGHFGVVYHGeyIDqaqNRIQ--CAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEG 1156
Cdd:cd06640     3 EELFTKLER-IGKGSFGEVFKG--ID---NRTQqvVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1157 LpHVLLPYMCHGDLLQFIRS-PQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL 1235
Cdd:cd06640    77 L-WIIMEYLGGGSALDLLRAgPFDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 DREyysVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAqgrRLPQPEYCPD 1315
Cdd:cd06640   153 DTQ---IKRNTFVGTPF-WMAPEVIQQSAYDSKADIWSLGITAIE-LAKGEPPNSDMHPMRVLFLIP---KNNPPTLVGD 224
                         250       260
                  ....*....|....*....|....*..
gi 578806145 1316 ---SLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd06640   225 fskPFKEFIDACLNKDPSFRPTAKELL 251
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
1087-1334 1.24e-22

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: 98.74  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdqaQNRIQCAIKSLSRIT-EMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd14003     6 KTLGEGSFGKVKLARHK---LTGEKVAIKIIDKSKlKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKI-YLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQR--NPTVKDLisFGlQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreyySVQ 1243
Cdd:cd14003    82 SGGELFDYIVNNGRlsEDEARRF--FQ-QLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN--------EFR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPV---KWMALESLQ-TYRFTTKSDVWSFGVLLWELLTrGAPPYRHiDPFDLTHFLAQGRRLPQPEYCPDSLYQ 1319
Cdd:cd14003   151 GGSLLKTFCgtpAYAAPEVLLgRKYDGPKADVWSLGVILYAMLT-GYLPFDD-DNDSKLFRKILKGKYPIPSHLSPDARD 228
                         250
                  ....*....|....*
gi 578806145 1320 VMQQCWEADPAVRPT 1334
Cdd:cd14003   229 LIRRMLVVDPSKRIT 243
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
1088-1345 1.35e-22

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: 99.35  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAqnriqcAIKSL--SRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPeglPHV-LLPY 1164
Cdd:cd14063     7 VIGKGRFGRVHRGRWHGDV------AIKLLniDYLNE-EQLEAFKEEVAAYKNTRHDNLVLFMGACMDP---PHLaIVTS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGD-LLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVkVADFGLArDILDREYYSVQ 1243
Cdd:cd14063    77 LCKGRtLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLF-SLSGLLQPGRR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRhARLPVKW---MALESLQTYR----------FTTKSDVWSFGVLLWELLTRGApPYRHIDPFDLTHFLAQGRRLPQP 1310
Cdd:cd14063   155 EDT-LVIPNGWlcyLAPEIIRALSpdldfeeslpFTKASDVYAFGTVWYELLAGRW-PFKEQPAESIIWQVGCGKKQSLS 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578806145 1311 EY-CPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14063   233 QLdIGREVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
1088-1338 1.88e-22

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 98.44  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGeyIDQAQNRiQCAIKSLsRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd06614     7 KIGEGASGEVYKA--TDRATGK-EVAIKKM-RLRK-QNKELIINEILIMKECKHPNIVDYYDSYLVGDEL-WVVMEYMDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRspqrnPTVKDL----ISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREyysv 1242
Cdd:cd06614    81 GSLTDIIT-----QNPVRMnesqIAYvCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAA-QLTKE---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHARL--PVkWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQGR--RLPQPEYCPDSLY 1318
Cdd:cd06614   151 KSKRNSVVgtPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEMA-EGEPPYLEEPPLRALFLITTKGipPLKNPEKWSPEFK 228
                         250       260
                  ....*....|....*....|
gi 578806145 1319 QVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06614   229 DFLNKCLVKDPEKRPSAEEL 248
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
1089-1338 2.51e-22

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: 97.87  E-value: 2.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIQcAIK--SLSRITEMQQVEAfLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYMC 1166
Cdd:cd08529     8 LGKGSFGVVY--KVVRKVDGRVY-ALKqiDISRMSRKMREEA-IDEARVLSKLNSPYVIKYYDSFVD-KGKLNIVMEYAE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDreyysvQQH 1245
Cdd:cd08529    83 NGDLHSLIKSQRGRPLPEDQIwKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK-ILS------DTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVK---WMALESLQTYRFTTKSDVWSFGVLLWELLTrgappYRHidPFD------LTHFLAQGRRLPQPE-YCPD 1315
Cdd:cd08529   156 NFAQTIVGtpyYLSPELCEDKPYNEKSDVWALGCVLYELCT-----GKH--PFEaqnqgaLILKIVRGKYPPISAsYSQD 228
                         250       260
                  ....*....|....*....|...
gi 578806145 1316 sLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd08529   229 -LSQLIDSCLTKDYRQRPDTTEL 250
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
1079-1339 2.63e-22

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 98.59  E-value: 2.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1079 ERVVTHSDRvIGKGHFGVVYHGeyIDQAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLp 1158
Cdd:cd06642     3 EELFTKLER-IGKGSFGEVYKG--IDNRTKEV-VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPYMCHGDLLQFIR-SPQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR 1237
Cdd:cd06642    78 WIIMEYLGGGSALDLLKpGPLEETYIATILR---EILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 EyysVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLaqgrrlpqPEYCPDSL 1317
Cdd:cd06642   155 Q---IKRNTFVGTPF-WMAPEVIKQSAYDFKADIWSLGITAIE-LAKGEPPNSDLHPMRVLFLI--------PKNSPPTL 221
                         250       260       270
                  ....*....|....*....|....*....|
gi 578806145 1318 Y--------QVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd06642   222 EgqhskpfkEFVEACLNKDPRFRPTAKELL 251
Sema_plexin_A1 cd11271
The Sema domain, a protein interacting module, of Plexin A1; Plexin A1 is found in both the ...
70-523 2.80e-22

The Sema domain, a protein interacting module, of Plexin A1; Plexin A1 is found in both the nervous and immune systems. Its external Sema domain is also shared by semaphorin proteins. In the nervous system, Plexin A1 mediates Sema3A axon guidance function by interacting with the Sema3A coreceptor neuropilin, resulting in actin depolarization and cell repulsion. In the immune system, Plexin A1 mediates Sema6D signaling by binding to the Sema6D-Trem2-DAP12 complex on immune cells and osteoclasts to promote Rac activation and DAP12 phosphorylation. In gene profiling experiments, Plexin A1 was identified as a CIITA (class II transactivator) regulated gene in primary dendritic cells (DCs). The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200532 [Multi-domain]  Cd Length: 474  Bit Score: 101.97  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   70 VFVAIRNRLHVLGPDLKSVQSLATGPAGD-------PGCQTCAacgpgPHGPPGDTDTKVLVLDPALPALVSCGSSLQGR 142
Cdd:cd11271    26 VYVGAVNRIYKLSNNLTLLRTHVTGPVEDnekcyppPSVQSCP-----HGLGTTNNVNKLLLVDYAANRLIACGSASQGI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  143 C-FLH--DLepqgtaVHLAAPaclfsaHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAvaASFSPrSVSIR 219
Cdd:cd11271   101 CqFLRldDL------FKLGEP------HHRKEHYLSSVNESGTMSGVIIEVGNGQNKLFVGTPIDGK--SEYFP-TLSSR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  220 RLKA---DASGFapGFV---------------ALSVLPkhlvSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSA-----L 276
Cdd:cd11271   166 KLMAneeNAEMF--GFVyqdefvssqlkipsdTLSKFP----TFDIYYVYSFSSEQFVYYLTLQLDTQLTSPDStgeqfF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  277 HTRLARLSATEPELGDYRELVLDCRfapkrrrrgapEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDG 356
Cdd:cd11271   240 TSKIVRLCVDDPKFYSYVEFPIGCE-----------QDGVEYRLIQDAYLSKPGKALAKQLGISEREDILFTVFSQGQKN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  357 GPGVGPNSVVCAFPIDLLDTLIDEGVERCcespvhpglRRGLDFFQSPSFcpnppgleaLSPNTSCRHFPLLVSSSFSRV 436
Cdd:cd11271   309 RVKPPKESVLCLFTLKKIKDKIKERIQSC---------YRGEGKLSLPWL---------LNKELGCINSPLQIDDNFCGQ 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  437 DlFNGLLG---PVQVTALYVTRLDNV-----------TVAHMGTMDGRI--LQVELVRSLNYLLYVSNFSLGDSGQPVQR 500
Cdd:cd11271   371 D-FNQPLGgtvTIEGTPLFVDKEDGMtsvaaydyrgrTVVFAGTRSGRIkkILVDLSAPSSRPALQYENVVAHEGSPILR 449
                         490       500
                  ....*....|....*....|....*
gi 578806145  501 DVSRLGDH-LLFASGD-QVFQVPIQ 523
Cdd:cd11271   450 DLVLSPDRqYIYAMTEkQVTRVPVE 474
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
1087-1334 2.87e-22

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: 97.99  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVY------HGEYIDQAQNRIQC-AIKSLSRITEMqqVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpH 1159
Cdd:cd06628     6 ALIGSGSFGSVYlgmnasSGELMAVKQVELPSvSAENKDRKKSM--LDALQREIALLRELQHENIVQYLGSSSDANHL-N 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRS--PQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldr 1237
Cdd:cd06628    83 IFLEYVPGGSVATLLNNygAFEESLVRNFVR---QILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKL--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 EYYSVQQHRHARLP-----VKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEY 1312
Cdd:cd06628   157 EANSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGENASPTIPSN 235
                         250       260
                  ....*....|....*....|..
gi 578806145 1313 CPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06628   236 ISSEARDFLEKTFEIDHNKRPT 257
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
1089-1338 3.52e-22

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: 97.84  E-value: 3.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYH------GEYIdqAQNRIQCAIKSLSRITEMQQ--VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHV 1160
Cdd:cd06629     9 IGKGTYGRVYLamnattGEML--AVKQVELPKTSSDRADSRQKtvVDALKSEIDTLKDLDHPNIVQYLGFEETEDYF-SI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSPQRNPtvKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreY 1239
Cdd:cd06629    86 FLEYVPGGSIGSCLRKYGKFE--EDLVrFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDD--I 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YSVQQHRHARLPVKWMALESLQTYR--FTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQ-PE---YC 1313
Cdd:cd06629   162 YGNNGATSMQGSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAMFKLGNKRSAPPvPEdvnLS 240
                         250       260
                  ....*....|....*....|....*
gi 578806145 1314 PDSLyQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06629   241 PEAL-DFLNACFAIDPRDRPTAAEL 264
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
1127-1349 5.18e-22

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: 97.20  E-value: 5.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1127 EAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFV 1206
Cdd:cd14156    33 HKIVREISLLQKLSHPNIVRYLGICVKDEKL-HPILEYVSGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIY 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1207 HRDLAARNCMLDESFTVK---VADFGLARDILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:cd14156   112 HRDLNSKNCLIRVTPRGReavVTDFGLAREVGEMPANDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILA 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1284 RgAPPYRHIDP------FDLTHF--LAQGrrlpqpeyCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd14156   192 R-IPADPEVLPrtgdfgLDVQAFkeMVPG--------CPEPFLDLAASCCRMDAFKRPSFAELLDELEDIAETL 256
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
1089-1345 6.32e-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: 97.18  E-value: 6.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyidQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIG-IMLPPEGLphVLLPYMCH 1167
Cdd:cd14664     1 IGRGGAGTVYKG----VMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGyCSNPTTNL--LVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKDLIS---FGLQVARGMEYLAEQ---KFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYS 1241
Cdd:cd14664    75 GSLGELLHSRPESQPPLDWETrqrIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHArlpVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQpEYC------PD 1315
Cdd:cd14664   155 MSSVAGS---YGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIVDWVRGLLE-EKKvealvdPD 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578806145 1316 -----------SLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14664   230 lqgvykleeveQVFQVALLCTQSSPMERPTMREVVRMLEGD 270
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
1087-1289 6.73e-22

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 96.77  E-value: 6.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeyidQAQNR---IQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIG-------IMLpp 1154
Cdd:cd14007     6 KPLGKGKFGNVY------LAREKksgFIVALKVISKsqLQKSGLEHQLRREIEIQSHLRHPNILRLYGyfedkkrIYL-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1155 eglphvLLPYMCHGDLLQFIrspQRNPTVKDLISFG--LQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGlar 1232
Cdd:cd14007    78 ------ILEYAPNGELYKEL---KKQKRFDEKEAAKyiYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG--- 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1233 dildreyYSVQQHRHARLPV----KWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14007   146 -------WSVHAPSNRRKTFcgtlDYLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPF 198
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
1079-1297 1.08e-21

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: 97.18  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1079 ERVVTHSDRVIGKGHFGVVYHGEyidqaQNRIQCAIKSL---SRITEMQQVEAFLREGLLMRGLNHPNVLALIGimLPPE 1155
Cdd:cd14158    13 ERPISVGGNKLGEGGFGVVFKGY-----INDKNVAVKKLaamVDISTEDLTKQFEQEIQVMAKCQHENLVELLG--YSCD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 GLPHVLL-PYMCHGDLLQFIRSPQRNP--TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR 1232
Cdd:cd14158    86 GPQLCLVyTYMPNGSLLDRLACLNDTPplSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1233 DilDREYYSVQQHRHARLPVKWMALESLQtYRFTTKSDVWSFGVLLWELLTrGAPPY-RHIDPFDL 1297
Cdd:cd14158   166 A--SEKFSQTIMTERIVGTTAYMAPEALR-GEITPKSDIFSFGVVLLEIIT-GLPPVdENRDPQLL 227
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
1087-1334 1.52e-21

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: 95.93  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQ----VEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLL 1162
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGD---FFAVKEVSLVDDDKKsresVKQLEQEIALLSKLRHPNIVQYYGTERE-EDNLYIFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIR--SPQRNPTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdreyy 1240
Cdd:cd06632    82 EYVPGGSIHKLLQryGAFEEPVIR---LYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVE----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 svqQHRHARlPVK----WMALESL--QTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQ-PEYC 1313
Cdd:cd06632   154 ---AFSFAK-SFKgspyWMAPEVImqKNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGVAAIFKIGNSGELPPiPDHL 228
                         250       260
                  ....*....|....*....|.
gi 578806145 1314 PDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06632   229 SPDAKDFIRLCLQRDPEDRPT 249
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
1087-1346 4.60e-21

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: 94.98  E-value: 4.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQaqnRIQCAIKSLSRITEMQQVE--AFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPY 1164
Cdd:cd14026     3 RYLSRGAFGTVSRARHADW---RVTVAIKCLKLDSPVGDSErnCLLKEAEILHKARFSYILPILGICNEPEFLG-IVTEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGL--QVARGMEYLAEQK--FVHRDLAARNCMLDESFTVKVADFGLARdildREYY 1240
Cdd:cd14026    79 MTNGSLNELLHEKDIYPDVAWPLRLRIlyEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSK----WRQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQHRHAR-LP----VKWMALESL---QTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRlpqPEY 1312
Cdd:cd14026   155 SISQSRSSKsAPeggtIIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQGHR---PDT 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1313 CPDSL----------YQVMQQCWEADPAVRPTFRVLVGEVEQIV 1346
Cdd:cd14026   232 GEDSLpvdiphratlINLIESGWAQNPDERPSFLKCLIELEPVL 275
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
1089-1339 5.67e-21

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: 94.75  E-value: 5.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06641    12 IGKGSFGEVFKG--IDNRTQKV-VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKL-WIIMEYLGGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTvkDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysVQQHRHA 1248
Cdd:cd06641    88 SALDLLEPGPLDET--QIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQ---IKRN*FV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVkWMALESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGR-RLPQPEYcPDSLYQVMQQCWEA 1327
Cdd:cd06641   163 GTPF-WMAPEVIKQSAYDSKADIWSLGITAIE-LARGEPPHSELHPMKVLFLIPKNNpPTLEGNY-SKPLKEFVEACLNK 239
                         250
                  ....*....|..
gi 578806145 1328 DPAVRPTFRVLV 1339
Cdd:cd06641   240 EPSFRPTAKELL 251
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1087-1334 6.21e-21

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: 93.87  E-value: 6.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRiQCAIKSLSrITEM--QQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLPY 1164
Cdd:cd08225     6 KKIGEGSFGKIYLAK--AKSDSE-HCVIKEID-LTKMpvKEKEASKKEVILLAKMKHPNIVTFFA-SFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSpQRNPTVKD--LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTV-KVADFGLARDILDreyyS 1241
Cdd:cd08225    81 CDGGDLMKRINR-QRGVLFSEdqILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLND----S 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrgappYRHidPFDLTHF------LAQGRRLP-QPEYCP 1314
Cdd:cd08225   156 MELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCT-----LKH--PFEGNNLhqlvlkICQGYFAPiSPNFSR 228
                         250       260
                  ....*....|....*....|
gi 578806145 1315 DsLYQVMQQCWEADPAVRPT 1334
Cdd:cd08225   229 D-LRSLISQLFKVSPRDRPS 247
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
1086-1294 8.05e-21

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: 95.51  E-value: 8.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVyhGEYIDQAQNRiQCAIKSLSRITEMQQV-EAFLREGLLMRGLNHPNVLALIGIMLPPEGLP-----H 1159
Cdd:cd07855    10 IETIGSGAYGVV--CSAIDTKSGQ-KVAIKKIPNAFDVVTTaKRTLRELKILRHFKHDNIIAIRDILRPKVPYAdfkdvY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMcHGDLLQFIRSPQrnPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI---- 1234
Cdd:cd07855    87 VVLDLM-ESDLHHIIHSDQ--PLTLEHIRYFLyQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLctsp 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1235 LDREYYsVQQH---RHARLPvkwMALESLQTYrfTTKSDVWSFGVLLWELLTRgappyRHIDP 1294
Cdd:cd07855   164 EEHKYF-MTEYvatRWYRAP---ELMLSLPEY--TQAIDMWSVGCIFAEMLGR-----RQLFP 215
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
1088-1334 1.43e-20

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 93.22  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIM--LPPEGLPHVLLPYM 1165
Cdd:cd13979    10 PLGSGGFGSVYKATYKGE-----TVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAEtgTDFASLGLIIMEYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdILDREYYSVQQH 1245
Cdd:cd13979    85 GNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCS--VKLGEGNEVGTP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 R-HARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRRlPQPEYCPDSLY-----Q 1319
Cdd:cd13979   163 RsHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTR-ELPYAGLRQHVLYAVVAKDLR-PDLSGLEDSEFgqrlrS 240
                         250
                  ....*....|....*
gi 578806145 1320 VMQQCWEADPAVRPT 1334
Cdd:cd13979   241 LISRCWSAQPAERPN 255
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1087-1334 2.97e-20

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: 92.36  E-value: 2.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeyidQAQNRI-QC--AIKSLsRITEMQQV-EAFLREGLLMRGLNHPNVL----ALIGimlppEGLP 1158
Cdd:cd13996    12 ELLGSGGFGSVY------KVRNKVdGVtyAIKKI-RLTEKSSAsEKVLREVKALAKLNHPNIVryytAWVE-----EPPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPYMCHGDLLQFIRSPQRNPTV-KDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDI- 1234
Cdd:cd13996    80 YIQMELCEGGTLRDWIDRRNSSSKNdRKLAlELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 -LDREYYSVQQHRHARLPVK--------WMALESLQTYRFTTKSDVWSFGVLLWELLTrgappyrhidPFDL----THFL 1301
Cdd:cd13996   160 nQKRELNNLNNNNNGNTSNNsvgigtplYASPEQLDGENYNEKADIYSLGIILFEMLH----------PFKTamerSTIL 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578806145 1302 AQGRRLPQPEYCPDSLY---QVMQQCWEADPAVRPT 1334
Cdd:cd13996   230 TDLRNGILPESFKAKHPkeaDLIQSLLSKNPEERPS 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
1087-1334 3.38e-20

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: 91.68  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRiqcAIK--SLSRITEMQQVEAfLREGLLMRGLNHPNVLA-----LIGIMLppeglpH 1159
Cdd:cd08530     6 KKLGKGSYGSVYKVKRLSDNQVY---ALKevNLGSLSQKEREDS-VNEIRLLASVNHPNIIRykeafLDGNRL------C 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFI--RSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILD 1236
Cdd:cd08530    76 IVMEYAPFGDLSKLIskRKKKRRLFPEDDIwRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK-VLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 REYYSVQqhrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDS 1316
Cdd:cd08530   155 KNLAKTQ----IGTPL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMAT-FRPPFEARTMQELRYKVCRGKFPPIPPVYSQD 228
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd08530   229 LQQIIRSLLQVNPKKRPS 246
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
1087-1349 3.75e-20

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: 91.79  E-value: 3.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdqaQNRIQCAIK-SLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphvLLPYM 1165
Cdd:cd14025     2 EKVGSGGFGQVYKVRHK---HWKTWLAIKcPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGL---VMEYM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSpqrNPTVKDLiSFGL--QVARGMEYLAEQK--FVHRDLAARNCMLDESFTVKVADFGLARdildreyYS 1241
Cdd:cd14025    76 ETGSLEKLLAS---EPLPWEL-RFRIihETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAK-------WN 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRH-----------ARLPVKwMALESLQTyrFTTKSDVWSFGVLLWELLTRGAPpyrHIDPFDLTHFL---AQGRR- 1306
Cdd:cd14025   145 GLSHSHdlsrdglrgtiAYLPPE-RFKEKNRC--PDTKHDVYSFAIVIWGILTQKKP---FAGENNILHIMvkvVKGHRp 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1307 -LPQ-----PEYCpDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSAL 1349
Cdd:cd14025   219 sLSPiprqrPSEC-QQMICLMKRCWDQDPRKRPTFQDITSETENLLSLL 266
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
1089-1342 3.85e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 91.89  E-value: 3.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRiQCAIKSLSRITEMQQ---VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPYM 1165
Cdd:cd14208     7 LGKGSFTKIYRGLRTDEEDDE-RCETEVLLKVMDPTHgncQESFLEAASIMSQISHKHLVLLHGVCVGKDSI--MVQEFV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKdlISFGLQVAR----GMEYLAEQKFVHRDLAARNCML----DESFT--VKVADFGLARDIL 1235
Cdd:cd14208    84 CHGALDLYLKKQQQKGPVA--ISWKLQVVKqlayALNYLEDKQLVHGNVSAKKVLLsregDKGSPpfIKLSDPGVSIKVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 DREYYSvqqhrhARLPvkWMALESL-QTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCp 1314
Cdd:cd14208   162 DEELLA------ERIP--WVAPECLsDPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPHWI- 232
                         250       260
                  ....*....|....*....|....*...
gi 578806145 1315 dSLYQVMQQCWEADPAVRPTFRVLVGEV 1342
Cdd:cd14208   233 -ELASLIQQCMSYNPLLRPSFRAIIRDL 259
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
1089-1335 4.23e-20

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: 91.68  E-value: 4.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFG----VVYHGEYIDqaqNRIQCAIKSLSRITEMQQveafLREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPY 1164
Cdd:cd13992     6 GASSHTGepkyVKKVGVYGG---RTVAIKHITFSRTEKRTI----LQELNQLKELVHDNLNKFIGICINPPNI--AVVTE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MC-HGDLLQFIRspQRNPTVKDL--ISFGLQVARGMEYLAEQKF-VHRDLAARNCMLDESFTVKVADFGLARDILDREYY 1240
Cdd:cd13992    77 YCtRGSLQDVLL--NREIKMDWMfkSSFIKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQH-RHARLpvKWMALESLQTY----RFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEY--- 1312
Cdd:cd13992   155 QLDEDaQHKKL--LWTAPELLRGSllevRGTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFRPELavl 232
                         250       260
                  ....*....|....*....|....*.
gi 578806145 1313 ---CPDSLYQVMQQCWEADPAVRPTF 1335
Cdd:cd13992   233 ldeFPPRLVLLVKQCWAENPEKRPSF 258
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
1089-1286 7.43e-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: 91.47  E-value: 7.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLPH----- 1159
Cdd:cd07840     7 IGEGTYGQVY------KARNKKTGELVALKKIRMENEKEGFpitaIREIKLLQKLDHPNVVRLKEIVTSKGSAKYkgsiy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHgDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildrey 1239
Cdd:cd07840    81 MVFEYMDH-DLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR------- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1240 ysvqqhrharlpvkWMALESLQTY-------------------RFTTKSDVWSFGVLLWELLTRGA 1286
Cdd:cd07840   153 --------------PYTKENNADYtnrvitlwyrppelllgatRYGPEVDMWSVGCILAELFTGKP 204
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
1087-1297 1.38e-19

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: 90.72  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDqaqNRIQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd05580     7 KTLGTGSFGRVRLVKHKD---SGKYYALKILKKakIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNL-YMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQR--NPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd05580    83 VPGGELFSLLRRSGRfpNDVAKFYAA---EVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTYTLC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1243 QQHrharlpvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDL 1297
Cdd:cd05580   160 GTP-------EYLAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDENPMKI 206
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
1089-1289 1.62e-19

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: 90.05  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHG------EYIdqaqnriqcAIKSlsriTEMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPH--V 1160
Cdd:cd14010     8 IGRGKHSVVYKGrrkgtiEFV---------AIKC----VDKSKRPEVLNEVRLTHELKHPNVLKFYEWY---ETSNHlwL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSPQRNP--TVKDlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR---DIL 1235
Cdd:cd14010    72 VVEYCTGGDLETLLRQDGNLPesSVRK---FGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregEIL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1236 DREYYSVQQHRHARLPVK---------WMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14010   149 KELFGQFSDEGNVNKVSKkqakrgtpyYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPF 210
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
1089-1284 2.48e-19

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: 90.89  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRiQCAIKSLSRITEmQQVEAF--LREGLLMRGLNHPNVLALIGIMLPP--EGLPHVLLPY 1164
Cdd:cd07858    13 IGRGAYGIVCSA--KNSETNE-KVAIKKIANAFD-NRIDAKrtLREIKLLRHLDHENVIAIKDIMPPPhrEAFNDVYIVY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 -MCHGDLLQFIRSPQrnPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR----- 1237
Cdd:cd07858    89 eLMDTDLHQIIRSSQ--TLSDDHCQYFLyQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKgdfmt 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1238 EYYSVQQHRHARLPVKWMaleslqtyRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07858   167 EYVVTRWYRAPELLLNCS--------EYTTAIDVWSVGCIFAELLGR 205
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1088-1334 4.45e-19

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: 88.75  E-value: 4.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYhgEYIDQAQNRIqCAIKSLS--RITEmQQVEAFLREGLLMRGLNHPNVLALIG-IMLPPEGLPHVLLPY 1164
Cdd:cd08217     7 TIGKGSFGTVR--KVRRKSDGKI-LVWKEIDygKMSE-KEKQQLVSEVNILRELKHPNIVRYYDrIVDRANTTLYIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRN--PTVKDLI-SFGLQVARGMEY-----LAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILD 1236
Cdd:cd08217    83 CEGGDLAQLIKKCKKEnqYIPEEFIwKIFTQLLLALYEchnrsVGGGKILHRDLKPANIFLDSDNNVKLGDFGLAR-VLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 REyySVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDS 1316
Cdd:cd08217   162 HD--SSFAKTYVGTPY-YMSPELLNEQSYDEKSDIWSLGCLIYELCA-LHPPFQAANQLELAKKIKEGKFPRIPSRYSSE 237
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd08217   238 LNEVIKSMLNVDPDKRPS 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
1087-1290 8.10e-19

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: 88.43  E-value: 8.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeyIDQAQNRiQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPY 1164
Cdd:cd05581     7 KPLGEGSYSTVVLA--KEKETGK-EYAIKVLDKrhIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL-EY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRspqrnptvkDLISFGLQVAR--------GMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArDILD 1236
Cdd:cd05581    83 APNGDLLEYIR---------KYGSLDEKCTRfytaeivlALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTA-KVLG 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1237 RE---------YYSVQQHRHARLP-----VKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd05581   153 PDsspestkgdADSQIAYNQARAAsfvgtAEYVSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFR 219
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1089-1345 8.18e-19

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 87.57  E-value: 8.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIQcAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05123     1 LGKGSFGKVL--LVRKKDTGKLY-AMKVLrkKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKL-YLVLDYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPtvKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR-------- 1237
Cdd:cd05123    77 GGELFSHLSKEGRFP--EERARFyAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDgdrtytfc 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 ---EYysvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHflaqgRRLPQPEYCP 1314
Cdd:cd05123   155 gtpEY---------------LAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYE-----KILKSPLKFP 213
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578806145 1315 DSLYQVMQ----QCWEADPAVRPTFrvlvGEVEQI 1345
Cdd:cd05123   214 EYVSPEAKslisGLLQKDPTKRLGS----GGAEEI 244
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
1087-1342 1.03e-18

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 87.79  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNR-IQCAIKS--LSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGImLPPEGLPHVLL 1162
Cdd:cd13993     6 SPIGEGAYGVVYLAVDLRTGRKYaIKCLYKSgpNSKDGNDFQKLPQLREiDLHRRVSRHPNIITLHDV-FETEVAIYIVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF-TVKVADFGLA-RDILDREY 1239
Cdd:cd13993    85 EYCPNGDLFEAITENRIYVGKTELIkNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGLAtTEKISMDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 ysvqqhrhARLPVKWMALESL------QTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTH--FLAQGRRLPQpE 1311
Cdd:cd13993   165 --------GVGSEFYMAPECFdevgrsLKGYPCAAGDIWSLGIILLN-LTFGRNPWKIASESDPIFydYYLNSPNLFD-V 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578806145 1312 YCPDS--LYQVMQQCWEADPAVRPTFRVLVGEV 1342
Cdd:cd13993   235 ILPMSddFYNLLRQIFTVNPNNRILLPELQLLV 267
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1086-1349 1.04e-18

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: 87.78  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIdqaQNRIQCAIKSLsRITEMQQVEA---FLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd08228     7 EKKIGRGQFSEVYRATCL---LDRKPVALKKV-QIFEMMDAKArqdCVKEIDLLKQLNHPNVIKYLDSFIEDNEL-NIVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFI---RSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRey 1239
Cdd:cd08228    82 ELADAGDLSQMIkyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 ySVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPY-RHIDPFDLTHFLAQGRRLPQP-EYCPDSL 1317
Cdd:cd08228   160 -TTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYgDKMNLFSLCQKIEQCDYPPLPtEHYSEKL 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1318 YQVMQQCWEADPAVRPTfrvlVGEVEQIVSAL 1349
Cdd:cd08228   238 RELVSMCIYPDPDQRPD----IGYVHQIAKQM 265
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1086-1284 1.23e-18

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: 88.01  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEyiDQAQNRIqCAIKS--LSRITEMQQVEAF--LREGLLMRGLNHPNVLALIGImLPPEGLPHVL 1161
Cdd:cd07841     5 GKKLGEGTYAVVYKAR--DKETGRI-VAIKKikLGERKEAKDGINFtaLREIKLLQELKHPNIIGLLDV-FGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMcHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD--REY 1239
Cdd:cd07841    81 FEFM-ETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSpnRKM 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1240 YSVQQHRHARLPvkwmalESLQTYR-FTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07841   160 THQVVTRWYRAP------ELLFGARhYGVGVDMWSVGCIFAELLLR 199
Sema_plexin_A4 cd11274
The Sema domain, a protein interacting module, of Plexin A4; Plexin A4 forms a receptor ...
64-526 1.27e-18

The Sema domain, a protein interacting module, of Plexin A4; Plexin A4 forms a receptor complex with neuropilins (NRPs) and transduces signals for class 3 semaphorins in the nervous system. It regulates facial nerve development by functioning as a receptor for Sema3A/NRP1. Both plexins A3 and A4 are essential for normal sympathetic development. They function both cooperatively, to regulate the migration of sympathetic neurons, and differentially, to guide sympathetic axons. Plexin A4 is also expressed in lymphoid tissues and functions in the immune system. It negatively regulates T lymphocyte responses. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200535 [Multi-domain]  Cd Length: 473  Bit Score: 90.78  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-PGC------QTCAacgpgPHGPPGDTDTKVLVLDPALPALVSCG 136
Cdd:cd11274    19 DERTGHIYLGAVNRIYKLSSDLKVLVTHQTGPDEDnPKCypprivQTCN-----EPLTLTNNINKMLLIDYKENRLIACG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  137 SSLQGRCFLHDLEpqgTAVHLAAPaclfsaHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAvaASFSPrSV 216
Cdd:cd11274    94 SLYQGICKLLRLD---DLFKLGEP------FHKKEHYLSGVNESGSVFGVIVSYSNLDDKLFIATAVDGK--PEYFP-TI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  217 SIRRLKADASG-------FAPGFVA---------LSVLPkhlvSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALH--- 277
Cdd:cd11274   162 SSRKLTKNSEAdgmfayvFHDEFVAsmikipsdtFTIIP----DFDIYYIYGFSSGNFVYFLTLQPEMISPPGSTTKeqv 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  278 --TRLARLSATEPELGDYRELVLDCRfapkrrrrgapEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKD 355
Cdd:cd11274   238 ytSKLVRLCKEDTAFNSYVEVPIGCE-----------KNGVEYRLLQAAYLSKAGAILARSLGVGPDDDILFTVFSKGQK 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  356 GGPGVGPNSVVCAFPIDLLDTLIDEGVERCC--ESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTscrhfPLLVSSSF 433
Cdd:cd11274   307 RKMKSLDESALCIFVLKEINDRIKDRLQSCYrgEGTLDLAWLKVKDIPCSSALLTIDDNFCGLDMNA-----PLGVSEMV 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  434 SRVDLFNGLLGPVQVTALYVTRldNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGqPVQRDVSRLGDH--LLF 511
Cdd:cd11274   382 RGLPVFTEDRDRMTSVIAYVYK--NHSLAFVGTKSGKLKKIRVDGTTKNALQYETVQVVDTG-PILRDMAFSKDHeqLYI 458
                         490
                  ....*....|....*
gi 578806145  512 ASGDQVFQVPIQGPG 526
Cdd:cd11274   459 MSEKQLTRVPVESCG 473
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
1089-1286 2.04e-18

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: 87.17  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRI---TEMQQVEAF-LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd07860     8 IGEGTYGVVY------KARNKLTGEVVALKKIrldTETEGVPSTaIREISLLKELNHPNIVKLLDVIHTENKL-YLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 McHGDLLQFIRSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreYYSVQ 1243
Cdd:cd07860    81 L-HQDLKKFMDASALTGIPLPLIkSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF----GVPVR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1244 QHRHARLPVKWMALESLQTYRF-TTKSDVWSFGVLLWELLTRGA 1286
Cdd:cd07860   156 TYTHEVVTLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVTRRA 199
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
1087-1347 2.79e-18

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: 86.62  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgEYIDQAQNRiQCAIKSLSrITEMQQVEAFLREGLLMRGL-NHPNVLALIG---IMLPPEGLPHVLL 1162
Cdd:cd13985     6 KQLGEGGFSYVY--LAHDVNTGR-RYALKRMY-FNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDsaiLSSEGRKEVLLLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYmCHGDLLQFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQK--FVHRDLAARNCMLDESFTVKVADFGLArdilDREY 1239
Cdd:cd13985    82 EY-CPGSLVDILEKSPPSPlSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSA----TTEH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YsvQQHRHARLPV------KWMAL-----ESLQTY---RFTTKSDVWSFGVLLWELLTRgappyrhIDPFDLTHFLA--Q 1303
Cdd:cd13985   157 Y--PLERAEEVNIieeeiqKNTTPmyrapEMIDLYskkPIGEKADIWALGCLLYKLCFF-------KLPFDESSKLAivA 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1304 GR-RLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVS 1347
Cdd:cd13985   228 GKySIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIITKDTK 272
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1089-1284 3.55e-18

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: 86.38  E-value: 3.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRIqCAIKsLSRITemQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd07829     7 LGEGTYGVVYKA--KDKKTGEI-VALK-KIRLD--NEEEGIpstaLREISLLKELKHPNIVKLLDVIHTENKL-YLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHgDLLQFIRSPQRN---PTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyys 1241
Cdd:cd07829    80 CDQ-DLKKYLDKRPGPlppNLIK---SIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAF------- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1242 vqqhrhaRLPVK---------WmaleslqtYR----------FTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07829   149 -------GIPLRtythevvtlW--------YRapeillgskhYSTAVDIWSVGCIFAELITG 195
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1087-1334 3.59e-18

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: 85.80  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFG---VVYHgEYIDQaqnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLP 1163
Cdd:cd08219     6 RVVGEGSFGralLVQH-VNSDQ-----KYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKE-SFEADGHLYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd08219    79 YCDGGDLMQKIKLQRGKLFPEDTIlQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYAC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QqhrHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrgappYRHidPF------DLTHFLAQGRRLPQPEYCPDS 1316
Cdd:cd08219   159 T---YVGTPY-YVPPEIWENMPYNNKSDIWSLGCILYELCT-----LKH--PFqanswkNLILKVCQGSYKPLPSHYSYE 227
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd08219   228 LRSLIKQMFKRNPRSRPS 245
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
1112-1338 3.65e-18

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 86.50  E-value: 3.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1112 CAIKSLSRitemQQVE---AFLREGLLMRGLNHPNVLALIGIMLPPeglPHVLL--PYMCHG---DLLQ---------FI 1174
Cdd:cd14042    33 VAIKKVNK----KRIDltrEVLKELKHMRDLQHDNLTRFIGACVDP---PNICIltEYCPKGslqDILEnedikldwmFR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1175 RSpqrnpTVKDLIsfglqvaRGMEYLAEQKFV-HRDLAARNCMLDESFTVKVADFGLA--RDIlDREYYSVQQHRHARLp 1251
Cdd:cd14042   106 YS-----LIHDIV-------KGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHsfRSG-QEPPDDSHAYYAKLL- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1252 vkWMALESL----QTYRFTTKSDVWSFGVLLWELLTRGAPPYrhIDPFDLT------HFLAQGRRLP-----QPEYCPDS 1316
Cdd:cd14042   172 --WTAPELLrdpnPPPPGTQKGDVYSFGIILQEIATRQGPFY--EEGPDLSpkeiikKKVRNGEKPPfrpslDELECPDE 247
                         250       260
                  ....*....|....*....|..
gi 578806145 1317 LYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd14042   248 VLSLMQRCWAEDPEERPDFSTL 269
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
1089-1334 5.47e-18

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: 85.68  E-value: 5.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidQAQNRIQCAIKSLSR----------------ITEMQQVEaflREGLLMRGLNHPNVLALIGIML 1152
Cdd:cd14008     1 LGRGSFGKVKLAL---DTETGQLYAIKIFNKsrlrkrregkndrgkiKNALDDVR---REIAIMKKLDHPNIVRLYEVID 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1153 PPEGLpHVLL--PYMCHGDLLQFIRSPQRNPTVKDLI--SFgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADF 1228
Cdd:cd14008    75 DPESD-KLYLvlEYCEGGPVMELDSGDRVPPLPEETArkYF-RDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1229 GLARdIL--DREYYSVQQHRHARLPVKwMALESLQTYRfTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTH-FLAQGR 1305
Cdd:cd14008   153 GVSE-MFedGNDTLQKTAGTPAFLAPE-LCDGDSKTYS-GKAADIWALGVTLYCLVF-GRLPFNGDNILELYEaIQNQND 228
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1306 RLPQPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14008   229 EFPIPPELSPELKDLLRRMLEKDPEKRIT 257
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1087-1347 5.96e-18

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: 85.30  E-value: 5.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgEYIDQAQNRIQcAIK--SLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPHV-LLP 1163
Cdd:cd14099     7 KFLGKGGFAKCY--EVTDMSTGKVY-AGKvvPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCF---EDEENVyILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCH-GDLLQFIRspQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyys 1241
Cdd:cd14099    81 ELCSnGSLMELLK--RRKAlTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDG--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 vqqHRHARL---PvKWMALESLQTYR-FTTKSDVWSFGVLLWELLTrGAPP---------YRHIDPFDLThflaqgrrLP 1308
Cdd:cd14099   156 ---ERKKTLcgtP-NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLV-GKPPfetsdvketYKRIKKNEYS--------FP 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTfrvlvgeVEQIVS 1347
Cdd:cd14099   223 SHLSISDEAKDLIRSMLQPDPTKRPS-------LDEILS 254
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
1097-1335 6.29e-18

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 85.30  E-value: 6.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1097 VYHGEYIdqAQNRIQCAIKSLSRI--TEMQQVeaflregllmRGLNHPNVLALIG--IMLPPEGlphVLLPYMCHGDLLQ 1172
Cdd:cd14045    27 IYDGRTV--AIKKIAKKSFTLSKRirKEVKQV----------RELDHPNLCKFIGgcIEVPNVA---IITEYCPKGSLND 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1173 FIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA---RDILDREYYSVQQH-RHA 1248
Cdd:cd14045    92 VLLNEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTtyrKEDGSENASGYQQRlMQV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKwmaLESLQTYRFTTKSDVWSFGVLLWELLTRGAPPyrhidPFDlTHFLAQGRRLPQPEY----------CPDSLY 1318
Cdd:cd14045   172 YLPPE---NHSNTDTEPTQATDVYSYAIILLEIATRNDPV-----PED-DYSLDEAWCPPLPELisgktenscpCPADYV 242
                         250
                  ....*....|....*..
gi 578806145 1319 QVMQQCWEADPAVRPTF 1335
Cdd:cd14045   243 ELIRRCRKNNPAQRPTF 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
1089-1287 7.46e-18

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: 85.05  E-value: 7.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVV--YHGEYIDQaqnRIQCAIKSLSRI----TEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLL 1162
Cdd:cd13994     1 IGKGATSVVriVTKKNPRS---GVLYAVKEYRRRddesKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWCLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdildrEYYSV 1242
Cdd:cd13994    78 EYCPGGDLFTLIEK-ADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA------EVFGM 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1243 QQHRHARLPVK------WMALESLQTYRFTTKS-DVWSFGVLLWELLTRGAP 1287
Cdd:cd13994   151 PAEKESPMSAGlcgsepYMAPEVFTSGSYDGRAvDVWSCGIVLFALFTGRFP 202
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
1087-1297 9.25e-18

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: 85.56  E-value: 9.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeyidQAQNRIQ---CAIK--SLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVL 1161
Cdd:cd05612     7 KTIGTGTFGRVH------LVRDRISehyYALKvmAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFL-YML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIRSPQRNPTVKDLIsFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYS 1241
Cdd:cd05612    80 MEYVPGGELFSYLRNSGRFSNSTGLF-YASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1242 VQQhrharlPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDL 1297
Cdd:cd05612   159 CGT------P-EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFDDNPFGI 206
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
1089-1338 9.72e-18

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: 85.18  E-value: 9.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRiQCAIKSLSRITEMQ---QVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYm 1165
Cdd:cd06611    13 LGDGAFGKVY------KAQHK-ETGLFAAAKIIQIEseeELEDFMVEIDILSECKHPNIVGLYEAYFY-ENKLWILIEF- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdreyySVQQ 1244
Cdd:cd06611    84 CDGGALDSIMLELERGLTEPQIRYvCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNK-----STLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPVK-WMALESL--QTYR---FTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGR--RLPQPEYCPDS 1316
Cdd:cd06611   159 KRDTFIGTPyWMAPEVVacETFKdnpYDYKADIWSLGITLIE-LAQMEPPHHELNPMRVLLKILKSEppTLDQPSKWSSS 237
                         250       260
                  ....*....|....*....|..
gi 578806145 1317 LYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06611   238 FNDFLKSCLVKDPDDRPTAAEL 259
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1087-1283 1.85e-17

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: 84.48  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDqaqNRIQCAIKSlsriteMQQVEAFL-REGLLMRGLNHPNVLALIGIMLPPEGLPHVL---- 1161
Cdd:cd14137    10 KVIGSGSFGVVYQAKLLE---TGEVVAIKK------VLQDKRYKnRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVylnl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 ----LPYMCHGDLLQFIRSPQRNPT--VKdLISFglQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDI 1234
Cdd:cd14137    81 vmeyMPETLYRVIRHYSKNKQTIPIiyVK-LYSY--QLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSAKRL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1235 LDRE---------YYsvqqhrhaRLPvkwmalESL---QTYrfTTKSDVWSFGVLLWELLT 1283
Cdd:cd14137   158 VPGEpnvsyicsrYY--------RAP------ELIfgaTDY--TTAIDIWSAGCVLAELLL 202
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1087-1334 1.89e-17

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: 84.01  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSRIT--EMQQVEAF--LREGLLMRGLNHPNVLALIGIMLPPEGLPhVLL 1162
Cdd:cd08222     6 RKLGSGNFGTVY---LVSDLKATADEELKVLKEISvgELQPDETVdaNREAKLLSKLDHPAIVKFHDSFVEKESFC-IVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKD---LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFtVKVADFGLARDILDR-- 1237
Cdd:cd08222    82 EYCEGGDLDDKISEYKKSGTTIDenqILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILMGTsd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 --------EYYsvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrgappYRHidPFDLTHFLAQGRR--- 1306
Cdd:cd08222   161 lattftgtPYY--------------MSPEVLKHEGYNSKSDIWSLGCILYEMCC-----LKH--AFDGQNLLSVMYKive 219
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578806145 1307 --LPQ-PEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd08222   220 geTPSlPDKYSKELNAIYSRMLNKDPALRPS 250
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
1088-1334 2.19e-17

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 83.64  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVY-----HGEYIDQAQnriqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLL 1162
Cdd:cd06631     8 VLGKGAYGTVYcgltsTGQLIAVKQ----VELDTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLE-DNVVSIFM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIR--SPQRNPTvkdLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYY 1240
Cdd:cd06631    83 EFVPGGSIASILArfGALEEPV---FCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQH--RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRL-PQ-PEYCPDS 1316
Cdd:cd06631   160 GSQSQllKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRKPvPRlPDKFSPE 238
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd06631   239 ARDFVHACLTRDQDERPS 256
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
1088-1295 3.54e-17

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: 83.08  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIdqaQNRIQCAIKSLSRITEMQQVEaflREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd06612    10 KLGEGSYGSVYKAIHK---ETGQVVAIKVVPVEEDLQEII---KEISILKQCDSPYIVKYYGSYFKNTDL-WIVMEYCGA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTvKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyySVQQHR 1246
Cdd:cd06612    83 GSVSDIMKITNKTLT-EEEIAAILyQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDT---MAKRNT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1247 HARLPVkWMALESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPF 1295
Cdd:cd06612   159 VIGTPF-WMAPEVIQEIGYNNKADIWSLGITAIE-MAEGKPPYSDIHPM 205
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
1136-1335 4.83e-17

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: 82.84  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1136 MRGLNHPNVLALIGIMLPPeGLPHVLLPYMCHGDLLQFIRSPQ-------RNPTVKDLIsfglqvaRGMEYLAEQKFVHR 1208
Cdd:cd14043    50 LRELRHENVNLFLGLFVDC-GILAIVSEHCSRGSLEDLLRNDDmkldwmfKSSLLLDLI-------KGMRYLHHRGIVHG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1209 DLAARNCMLDESFTVKVADFGLArDILDREYYSVQQHRHARLpvKWMALESLQ----TYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd14043   122 RLKSRNCVVDGRFVLKITDYGYN-EILEAQNLPLPEPAPEEL--LWTAPELLRdprlERRGTFPGDVFSFAIIMQEVIVR 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1285 GaPPYRHID--PFDLTHFLAQGRRLPQPEYCPDS----LYQVMQQCWEADPAVRPTF 1335
Cdd:cd14043   199 G-APYCMLGlsPEEIIEKVRSPPPLCRPSVSMDQapleCIQLMKQCWSEAPERRPTF 254
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
1087-1343 5.20e-17

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: 83.11  E-value: 5.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyidQAQNRIQCAIKSLsRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPH----VLL 1162
Cdd:cd13986     6 RLLGEGGFSFVYLVE---DLSTGRLYALKKI-LCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEAGGKkevyLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRN----PTVKDLISFgLQVARGMEYLAEQK---FVHRDLAARNCMLDESFTVKVADFGLARdil 1235
Cdd:cd13986    82 PYYKRGSLQDEIERRLVKgtffPEDRILHIF-LGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILMDLGSMN--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 dREYYSVQQHRHARLPVKWMALESLQTYR------------FTTKSDVWSFGVLLWELLTrgappyrHIDPFDLTHF--- 1300
Cdd:cd13986   158 -PARIEIEGRREALALQDWAAEHCTMPYRapelfdvkshctIDEKTDIWSLGCTLYALMY-------GESPFERIFQkgd 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1301 -LAQGR-----RLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVE 1343
Cdd:cd13986   230 sLALAVlsgnySFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVH 278
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
1087-1334 5.33e-17

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: 82.97  E-value: 5.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRiqcAIKSLSRITE-----MQqveafLREGLLMRGLN-HPNVLALIGIMLPPEGLpHV 1160
Cdd:cd07830     5 KQLGDGTFGSVYLARNKETGELV---AIKKMKKKFYsweecMN-----LREVKSLRKLNeHPNIVKLKEVFRENDEL-YF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMcHGDLLQFIRSPQRNP----TVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD 1236
Cdd:cd07830    76 VFEYM-EGNLYQLMKDRKGKPfsesVIRSII---YQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 R----EYYSVQQHRharlpvkwmALESL--QTYrFTTKSDVWSFGVLLWELLTR--------------------GAPpyr 1290
Cdd:cd07830   152 RppytDYVSTRWYR---------APEILlrSTS-YSSPVDIWALGCIMAELYTLrplfpgsseidqlykicsvlGTP--- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1291 HIDPFDLTHFLAQ--GRRLPQpeYCPDSLYQV-----------MQQCWEADPAVRPT 1334
Cdd:cd07830   219 TKQDWPEGYKLASklGFRFPQ--FAPTSLHQLipnaspeaidlIKDMLRWDPKKRPT 273
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
1088-1314 5.89e-17

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 82.75  E-value: 5.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYidQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlPPEGLPHVLLPYMCH 1167
Cdd:cd14202     9 LIGHGAFAVVFKGRH--KEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQ-EIANSVYLVMEYCNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpqRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCMLD---------ESFTVKVADFGLARdildr 1237
Cdd:cd14202    86 GDLADYLHT--MRTLSEDTIRLFLQqIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFAR----- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 eyYSVQQHRHARL---PVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRL----PQP 1310
Cdd:cd14202   159 --YLQNNMMAATLcgsPM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSLspniPRE 234

                  ....
gi 578806145 1311 EYCP 1314
Cdd:cd14202   235 TSSH 238
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1089-1305 7.06e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 83.71  E-value: 7.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVY------HGEYIdqaqnriqcAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALI-GIMlpPEGLPH 1159
Cdd:PTZ00263   26 LGTGSFGRVRiakhkgTGEYY---------AIKCLKKreILKMKQVQHVAQEKSILMELSHPFIVNMMcSFQ--DENRVY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRSPQRNPTvkDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE 1238
Cdd:PTZ00263   95 FLLEFVVGGELFTHLRKAGRFPN--DVAKFyHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRT 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1239 YYSVQQhrharlPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR 1305
Cdd:PTZ00263  173 FTLCGT------P-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPFFDDTPFRIYEKILAGR 231
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
1088-1334 7.24e-17

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: 82.25  E-value: 7.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYhgEYIDQAQNRIqCAIKSL---SRITEMQQVEAFLRegLLMRGlNHPNVLALIGiMLPPEGLPHVLLPY 1164
Cdd:cd06623     8 VLGQGSSGVVY--KVRHKPTGKI-YALKKIhvdGDEEFRKQLLRELK--TLRSC-ESPYVVKCYG-AFYKEGEISIVLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRspqRNPTVKD--LISFGLQVARGMEYL-AEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyyS 1241
Cdd:cd06623    81 MDGGSLADLLK---KVGKIPEpvLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLEN----T 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY---RHIDPFDLTHFLAQGRRLPQP-EYCPDSL 1317
Cdd:cd06623   154 LDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECAL-GKFPFlppGQPSFFELMQAICDGPPPSLPaEEFSPEF 232
                         250
                  ....*....|....*..
gi 578806145 1318 YQVMQQCWEADPAVRPT 1334
Cdd:cd06623   233 RDFISACLQKDPKKRPS 249
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
1129-1345 8.99e-17

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: 81.77  E-value: 8.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1129 FLREGLLMRGLNHPNVLALIGIMLPPeglPH--VLLPYMCHGDLLQFIRSpQRNPTVK--DLISFGLQVARGMEYL--AE 1202
Cdd:cd14057    39 FNEEYPRLRIFSHPNVLPVLGACNSP---PNlvVISQYMPYGSLYNVLHE-GTGVVVDqsQAVKFALDIARGMAFLhtLE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1203 QKFVHRDLAARNCMLDESFTVKV--ADFGlardildreyYSVQQHRHARLPVkWMALESLQTYRFTTK---SDVWSFGVL 1277
Cdd:cd14057   115 PLIPRHHLNSKHVMIDEDMTARInmADVK----------FSFQEPGKMYNPA-WMAPEALQKKPEDINrrsADMWSFAIL 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1278 LWELLTRGApPYRHIDPFDLTHFLA-QGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14057   184 LWELVTREV-PFADLSNMEIGMKIAlEGLRVTIPPGISPHMCKLMKICMNEDPGKRPKFDMIVPILEKM 251
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
1088-1332 1.21e-16

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: 81.75  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIdqAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNH---PNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd06917     8 LVGRGSYGAVYRGYHV--KTGRV-VALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSL-WIIMDY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 mCHGDLLQFIRSPQrnPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreyySVQ 1243
Cdd:cd06917    84 -CEGGSIRTLMRAG--PIAERYIAVIMrEVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAA--------SLN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPV----KWMALESLQTYR-FTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR--RLPQPEYCPdS 1316
Cdd:cd06917   153 QNSSKRSTFvgtpYWMAPEVITEGKyYDTKADIWSLGITTYEMAT-GNPPYSDVDALRAVMLIPKSKppRLEGNGYSP-L 230
                         250
                  ....*....|....*.
gi 578806145 1317 LYQVMQQCWEADPAVR 1332
Cdd:cd06917   231 LKEFVAACLDEEPKDR 246
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
1087-1334 1.58e-16

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 81.37  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRiqcAIKSLSR---ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd14098     6 DRLGSGTFAEVKKAVEVETGKMR---AIKQIVKrkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHI-YLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML--DESFTVKVADFGLARDILDREYYS 1241
Cdd:cd14098    82 YVEGGDLMDFIMAWGAIPE-QHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAKVIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARL-PVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrgappyRHIdPFDLTHFLAQGRRLPQPEYC--PDSLY 1318
Cdd:cd14098   161 TFCGTMAYLaPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLT------GAL-PFDGSSQLPVEKRIRKGRYTqpPLVDF 233
                         250       260
                  ....*....|....*....|...
gi 578806145 1319 QVMQQC-------WEADPAVRPT 1334
Cdd:cd14098   234 NISEEAidfilrlLDVDPEKRMT 256
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
1086-1334 1.86e-16

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: 80.78  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNriqCAIKSLsRITEM---QQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd08224     5 EKKIGKGQFSVVYRARCLLDGRL---VALKKV-QIFEMmdaKARQDCLKEIDLLQQLNHPNIIKYLASFIENNEL-NIVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTV---KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreY 1239
Cdd:cd08224    80 ELADAGDLSRLIKHFKKQKRLipeRTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR------F 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YS---VQQHRHARLPVkWMALESL--QTYRFttKSDVWSFGVLLWELLTRGAPPYR-HIDPFDLTHFLAQGRRLPQPEYC 1313
Cdd:cd08224   154 FSsktTAAHSLVGTPY-YMSPERIreQGYDF--KSDIWSLGCLLYEMAALQSPFYGeKMNLYSLCKKIEKCEYPPLPADL 230
                         250       260
                  ....*....|....*....|..
gi 578806145 1314 -PDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd08224   231 ySQELRDLVAACIQPDPEKRPD 252
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
1089-1290 2.29e-16

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 80.39  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHgeyIDQAQNRIQCAIKSLSrITEMQQVEAfLREGLLMRGLNHPNVLALIGIMLPPEGLphVL-LPYMCH 1167
Cdd:cd14006     1 LGRGRFGVVKR---CIEKATGREFAAKFIP-KRDKKKEAV-LREISILNQLQHPRIIQLHEAYESPTEL--VLiLELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNpTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDE--SFTVKVADFGLARDILDREYysvQQH 1245
Cdd:cd14006    74 GELLDRLAERGSL-SEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARKLNPGEE---LKE 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1246 RHARLpvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd14006   150 IFGTP--EFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFL 191
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
1087-1333 2.62e-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: 80.63  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQ---VEAFLREGLLMRGLNHPNVLALIGImLPPEGLPHVLLP 1163
Cdd:cd14070     8 RKLGEGSFAKVREGLHAVTGE---KVAIKVIDKKKAKKDsyvTKNLRREGRIQQMIRHPNITQLLDI-LETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGL---ARDILDREYY 1240
Cdd:cd14070    84 LCPGGNLMHRIYDKKRLEE-REARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsncAGILGYSDPF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQHRHArlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRhIDPFDLTHF---LAQGRRLPQPEYCPDSL 1317
Cdd:cd14070   163 STQCGSPA-----YAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFT-VEPFSLRALhqkMVDKEMNPLPTDLSPGA 235
                         250
                  ....*....|....*.
gi 578806145 1318 YQVMQQCWEADPAVRP 1333
Cdd:cd14070   236 ISFLRSLLEPDPLKRP 251
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
1089-1339 3.41e-16

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


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 80.36  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06647    15 IGQGASGTVYTAIDVATGQ---EVAIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDEL-WVVMEYLAGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTvkDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyySVQQHRHA 1248
Cdd:cd06647    90 SLTDVVTETCMDEG--QIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI------TPEQSKRS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RL---PVkWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQGRR--LPQPEYCPDSLYQVMQQ 1323
Cdd:cd06647   162 TMvgtPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYLNENPLRALYLIATNGTpeLQNPEKLSAIFRDFLNR 239
                         250
                  ....*....|....*.
gi 578806145 1324 CWEADPAVRPTFRVLV 1339
Cdd:cd06647   240 CLEMDVEKRGSAKELL 255
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
1087-1290 3.62e-16

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: 79.99  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd05578     6 RVIGKGSFGKVC---IVQKKDTKKMFAMKYMNKqkCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDM-YMVVDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRspQRNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYysvQ 1243
Cdd:cd05578    82 LLGGDLRYHLQ--QKVKFSEETVKFYIcEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTL---A 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1244 QHRHARLPvkWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYR 1290
Cdd:cd05578   157 TSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYEML-RGKRPYE 200
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
1088-1307 3.62e-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: 80.44  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYidQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd14201    13 LVGHGAFAVVFKGRH--RKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSV-FLVMEYCNG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpqRNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLD---------ESFTVKVADFGLARdildr 1237
Cdd:cd14201    90 GDLADYLQA--KGTLSEDTIRVFLqQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFAR----- 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1238 eyYSVQQHRHARL---PVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRL 1307
Cdd:cd14201   163 --YLQSNMMAATLcgsPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCLV-GKPPFQANSPQDLRMFYEKNKNL 231
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
1087-1334 3.67e-16

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: 80.19  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSrITEMQQVEAF---LREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLP 1163
Cdd:cd06607     7 REIGHGSFGAVY---YARNKRTSEVVAIKKMS-YSGKQSTEKWqdiIKEVKFLRQLRHPNTIEYKGCYLR-EHTAWLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YmCHG---DLLQFIRSPQRNPTVKDLISFGLQvarGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGlardildreyy 1240
Cdd:cd06607    82 Y-CLGsasDIVEVHKKPLQEVEIAAICHGALQ---GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG----------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVQQHRHARLPVK---WMALE---SLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGR--RLPQPEY 1312
Cdd:cd06607   147 SASLVCPANSFVGtpyWMAPEvilAMDEGQYDGKVDVWSLGITCIELAER-KPPLFNMNAMSALYHIAQNDspTLSSGEW 225
                         250       260
                  ....*....|....*....|..
gi 578806145 1313 cPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06607   226 -SDDFRNFVDSCLQKIPQDRPS 246
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
1089-1289 4.98e-16

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: 79.64  E-value: 4.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQN--RIQCAIK-SLSRITemqqVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd14121     3 LGSGTYATVYKAYRKSGAREvvAVKCVSKsSLNKAS----TENLLTEIELLKKLKHPHIVELKDFQWDEEHI-YLIMEYC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNP--TVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTV--KVADFGLARDILDREyyS 1241
Cdd:cd14121    78 SGGDLSRFIRSRRTLPesTVR---RFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQHLKPND--E 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1242 VQQHRHARLpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14121   153 AHSLRGSPL---YMAPEMILKKKYDARVDLWSVGVILYECLF-GRAPF 196
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
1088-1334 5.35e-16

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: 80.04  E-value: 5.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNriqCAIKSLSRITEMQqvEAFLREGLLMRGL-NHPNVLALIGIML--PPEGLPHVL--- 1161
Cdd:cd06608    13 VIGEGTYGKVYKARHKKTGQL---AAIKIMDIIEDEE--EEIKLEINILRKFsNHPNIATFYGAFIkkDPPGGDDQLwlv 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHG---DLLQ-FIRSPQRNPtvKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDiLD 1236
Cdd:cd06608    88 MEYCGGGsvtDLVKgLRKKGKRLK--EEWIAYILReTLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQ-LD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 REyysvQQHRHARL--PVkWMALESLQ-----TYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGR--RL 1307
Cdd:cd06608   165 ST----LGRRNTFIgtPY-WMAPEVIAcdqqpDASYDARCDVWSLGITAIE-LADGKPPLCDMHPMRALFKIPRNPppTL 238
                         250       260
                  ....*....|....*....|....*..
gi 578806145 1308 PQPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06608   239 KSPEKWSKEFNDFISECLIKNYEQRPF 265
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
1088-1334 6.09e-16

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: 79.58  E-value: 6.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQ---------------AQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIML 1152
Cdd:cd14000     1 LLGDGGFGSVYRASYKGEpvavkifnkhtssnfANVPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1153 PPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML-----DESFTVKVAD 1227
Cdd:cd14000    81 HPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1228 FGLARdildreyysvQQHRHARLPVK----WMALESLQ-TYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDpFDLTHFLA 1302
Cdd:cd14000   161 YGISR----------QCCRMGAKGSEgtpgFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLK-FPNEFDIH 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578806145 1303 QGRR--LPQPEYCPDSLYQV-MQQCWEADPAVRPT 1334
Cdd:cd14000   230 GGLRppLKQYECAPWPEVEVlMKKCWKENPQQRPT 264
IPT_PCSR cd00603
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
684-768 6.76e-16

IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238337 [Multi-domain]  Cd Length: 90  Bit Score: 74.03  E-value: 6.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGT-SRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGA----QV 758
Cdd:cd00603     1 PVITSISPSSGPLSGGTRLTITGSNLGSGSpRVRVTVGGVPCKVLNVSSTEIVCRTPAAATPGEGPVEVTVDGAnvsaRV 80
                          90
                  ....*....|
gi 578806145  759 PGSWTFQYRE 768
Cdd:cd00603    81 LSNTTFTYVE 90
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
1089-1334 6.92e-16

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: 79.63  E-value: 6.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRIqCAIKSLSRITEMQQVEAF-LREGLLMRGL---NHPNVLALIGIMLPPEgLPHVLLPY 1164
Cdd:cd07838     7 IGEGAYGTVYKAR--DLQDGRF-VALKKVRVPLSEEGIPLStIREIALLKQLesfEHPNVVRLLDVCHGPR-TDRELKLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 M----CHGDLLQFI-RSPQRN---PTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILD 1236
Cdd:cd07838    83 LvfehVDQDLATYLdKCPKPGlppETIKDLMR---QLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLAR-IYS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 REyysvqqhrharlpvkwMALES-------------LQTYrFTTKSDVWSFGVLLWELLTRGA--PPYRHIDP----FDL 1297
Cdd:cd07838   159 FE----------------MALTSvvvtlwyrapevlLQSS-YATPVDMWSVGCIFAELFNRRPlfRGSSEADQlgkiFDV 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1298 T-----------------HFLAQGRRLPQ---PEYCPDSLyQVMQQCWEADPAVRPT 1334
Cdd:cd07838   222 IglpseeewprnsalprsSFPSYTPRPFKsfvPEIDEEGL-DLLKKMLTFNPHKRIS 277
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
1087-1289 7.69e-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: 78.90  E-value: 7.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgEYIDQAQNRIQCA-IKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYm 1165
Cdd:cd14188     7 KVLGKGGFAKCY--EMTDLTTNKVYAAkIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENI-YILLEY- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysvQQH 1245
Cdd:cd14188    83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLE----HRR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1246 RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14188   159 RTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLL-GRPPF 201
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
1087-1282 1.04e-15

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: 78.49  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidqAQNRIQCAIKSLSRiteMQQVEAFL-----REGLLMRGLNHPNVLALIGIMlppEGLPHV- 1160
Cdd:cd14162     6 KTLGHGSYAVVKKAYS---TKHKCKVAIKIVSK---KKAPEDYLqkflpREIEVIKGLKHPNLICFYEAI---ETTSRVy 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 -LLPYMCHGDLLQFIRSPQRNPTVKDLISFGlQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDildrey 1239
Cdd:cd14162    77 iIMELAENGDLLDYIRKNGALPEPQARRWFR-QLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARG------ 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1240 ysvqQHRHArlPVKWMAlesLQTY------------RFT----TKSDVWSFGVLLWELL 1282
Cdd:cd14162   150 ----VMKTK--DGKPKL---SETYcgsyayaspeilRGIpydpFLSDIWSMGVVLYTMV 199
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
1088-1332 1.06e-15

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: 79.29  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaqnriQCAIKslsrITEMQQVEAFLREGLLMR--GLNHPNVLALIGIMLPPEGLPHVLL--- 1162
Cdd:cd14053     2 IKARGRFGAVWKAQYLNR-----LVAVK----IFPLQEKQSWLTEREIYSlpGMKHENILQFIGAEKHGESLEAEYWlit 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSpqRNPTVKDLISFGLQVARGMEYLAEQ----------KFVHRDLAARNCMLDESFTVKVADFGLAR 1232
Cdd:cd14053    73 EFHERGSLCDYLKG--NVISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLLKSDLTACIADFGLAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1233 DIldrEYYSVQQHRHARLPVK-WMALESLQ-TYRFTTKS----DVWSFGVLLWELLTR----GAPPYRHIDPF------- 1295
Cdd:cd14053   151 KF---EPGKSCGDTHGQVGTRrYMAPEVLEgAINFTRDAflriDMYAMGLVLWELLSRcsvhDGPVDEYQLPFeeevgqh 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1296 ----DLTHFLAQGRRLPQ--PEYCPDS----LYQVMQQCWEADPAVR 1332
Cdd:cd14053   228 ptleDMQECVVHKKLRPQirDEWRKHPglaqLCETIEECWDHDAEAR 274
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
1089-1334 1.23e-15

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: 78.50  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIdqaQNRIQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYmCHG 1168
Cdd:cd06613     8 IGSGTYGDVYKARNI---ATGELAAVKVIK-LEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKL-WIVMEY-CGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSpQRNPTVKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA----RDILDREYYSVQ 1243
Cdd:cd06613    82 GSLQDIYQ-VTGPLSELQIAYvCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSaqltATIAKRKSFIGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHrharlpvkWMALESLQTYR---FTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGRRLP-----QPEYCPD 1315
Cdd:cd06613   161 PY--------WMAPEVAAVERkggYDGKCDIWALGITAIE-LAELQPPMFDLHPMRALFLIPKSNFDPpklkdKEKWSPD 231
                         250
                  ....*....|....*....
gi 578806145 1316 sLYQVMQQCWEADPAVRPT 1334
Cdd:cd06613   232 -FHDFIKKCLTKNPKKRPT 249
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
1089-1297 1.50e-15

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: 79.70  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidQAQNRIQCAIKSLSR-ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHV----LLP 1163
Cdd:cd07877    25 VGSGAYGSVCAAF---DTKTGLRVAVKKLSRpFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFndvyLVT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQrnpTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE--YY 1240
Cdd:cd07877   102 HLMGADLNNIVKCQK---LTDDHVQFLIyQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMtgYV 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1241 SVQQHRHARLPVKWMaleslqtyRFTTKSDVWSFGVLLWELLTRGA--PPYRHIDPFDL 1297
Cdd:cd07877   179 ATRWYRAPEIMLNWM--------HYNQTVDIWSVGCIMAELLTGRTlfPGTDHIDQLKL 229
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
1084-1347 1.55e-15

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: 78.30  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSRITEMQQVEAFLrEGLLMRGL-NHPNVLALIGIMLPPE----GLP 1158
Cdd:cd13975     3 KLGRELGRGQYGVVY---ACDSWGGHFPCALKSVVPPDDKHWNDLAL-EFHYTRSLpKHERIVSLHGSVIDYSygggSSI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPY-MCHGDLLQFIRspqRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDildr 1237
Cdd:cd13975    79 AVLLIMeRLHRDLYTGIK---AGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKP---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 eyYSVQQHRHARLPVKwMALEsLQTYRFTTKSDVWSFGVLLWELLtrgAPPYRHIDPF-------DLTHFLAQGRRlpqP 1310
Cdd:cd13975   152 --EAMMSGSIVGTPIH-MAPE-LFSGKYDNSVDVYAFGILFWYLC---AGHVKLPEAFeqcaskdHLWNNVRKGVR---P 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578806145 1311 EYCP---DSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVS 1347
Cdd:cd13975   222 ERLPvfdEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMD 261
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
1084-1284 1.82e-15

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: 79.79  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHgeyIDQAQNRIQCAIKSLSRITE-MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLP---- 1158
Cdd:cd07853     3 EPDRPIGYGAFGVVWS---VTDPRDGKRVALKKMPNVFQnLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDPfeei 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPYMcHGDLLQFIRSPQrnPTVKDLIS-FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildr 1237
Cdd:cd07853    80 YVVTELM-QSDLHKIIVSPQ--PLSSDHVKvFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR----- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1238 eyysVQQHRHArlpvKWMALESL-QTYR----------FTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07853   152 ----VEEPDES----KHMTQEVVtQYYRapeilmgsrhYTSAVDIWSVGCIFAELLGR 201
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
1086-1289 2.32e-15

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: 77.68  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNriqCAIKSLSRITEMQ-QVEAFL-REGLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd14081     6 GKTLGKGQTGLVKLAKHCVTGQK---VAIKIVNKEKLSKeSVLMKVeREIAIMKLIEHPNVLKLYDVYENKKYL-YLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRnPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdildreyySVQ 1243
Cdd:cd14081    82 YVSGGELFDYLVKKGR-LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA---------SLQ 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1244 QhrharlPVKWmalesLQT-----------------YRfTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14081   152 P------EGSL-----LETscgsphyacpevikgekYD-GRKADIWSCGVILYALLV-GALPF 201
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1089-1295 2.49e-15

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: 78.04  E-value: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGImlPPE------GLPHVLL 1162
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGE---KIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDV--PEEmnflvnDVPLLAM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKD--LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDE---SFTVKVADFGLARDI--- 1234
Cdd:cd14039    76 EYCSGGDLRKLLNKPENCCGLKEsqVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEingKIVHKIIDLGYAKDLdqg 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1235 -LDREYYSVQQhrharlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPF 1295
Cdd:cd14039   156 sLCTSFVGTLQ---------YLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPF 208
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
1084-1289 2.68e-15

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: 77.29  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRI--TEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVL 1161
Cdd:cd14002     4 HVLELIGEGSFGKVYKGRRKYTGQ---VVALKFIPKRgkSE-KELRNLRQEIEILRKLNHPNIIEMLDSFETKKEF--VV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIRSPQRNPtvKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreyy 1240
Cdd:cd14002    78 VTEYAQGELFQILEDDGTLP--EEEVrSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR-------- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1241 SVQQHRHARLPVK----WMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14002   148 AMSCNTLVLTSIKgtplYMAPELVQEQPYDHTADLWSLGCILYELFV-GQPPF 199
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
1089-1345 2.95e-15

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: 77.30  E-value: 2.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVyhGEYID-QAQNRIQCAI---KSLSRITEMQQ-VEaflREGLLMRGLNHPNVLALIGIMLPPE-GLPHVLL 1162
Cdd:cd14119     1 LGEGSYGKV--KEVLDtETLCRRAVKIlkkRKLRRIPNGEAnVK---REIQILRRLNHRNVIKLVDVLYNEEkQKLYMVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYmCHGDLLQFI-RSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--DILDREY 1239
Cdd:cd14119    76 EY-CVGGLQEMLdSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEalDLFAEDD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 Y-SVQQHRHARLPVKwmaLESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGrRLPQPEYCPDSLY 1318
Cdd:cd14119   155 TcTTSQGSPAFQPPE---IANGQDSFSGFKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGKG-EYTIPDDVDPDLQ 229
                         250       260
                  ....*....|....*....|....*..
gi 578806145 1319 QVMQQCWEADPAVRPTfrvlvgeVEQI 1345
Cdd:cd14119   230 DLLRGMLEKDPEKRFT-------IEQI 249
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
1086-1289 3.19e-15

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: 77.05  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVyhgeyiDQAQNRI---QCAIKSL--SRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMlPPEGLPHV 1160
Cdd:cd14071     5 ERTIGKGNFAVV------KLARHRItktEVAIKIIdkSQLDE-ENLKKIYREVQIMKMLNHPHIIKLYQVM-ETKDMLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSPQRNPTVKDLISFgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdildrEYY 1240
Cdd:cd14071    77 VTEYASNGEIFDYLAQHGRMSEKEARKKF-WQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS------NFF 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1241 SVQQHRHArlpvkW------MALESLQTYRFT-TKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14071   150 KPGELLKT-----WcgsppyAAPEVFEGKEYEgPQLDIWSLGVVLYVLVC-GALPF 199
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
1061-1294 3.81e-15

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: 77.35  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1061 RDLDSALLAEVKDVLIPHERVvthsdRVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVEAFLREGLLMRGLN 1140
Cdd:cd06636     1 RSLDDIDLSALRDPAGIFELV-----EVVGNGTYGQVYKGRHVKTGQ---LAAIKVMD-VTEDEEEEIKLEINMLKKYSH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1141 HPNVLALIGIMLPPEGLPH-----VLLPYMCHGDLLQFIRSPQRNPTVKDLISF-GLQVARGMEYLAEQKFVHRDLAARN 1214
Cdd:cd06636    72 HRNIATYYGAFIKKSPPGHddqlwLVMEFCGAGSVTDLVKNTKGNALKEDWIAYiCREILRGLAHLHAHKVIHRDIKGQN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1215 CMLDESFTVKVADFGLARDiLDReyySVQQHRHARLPVKWMALESL-------QTYRFttKSDVWSFGVLLWElLTRGAP 1287
Cdd:cd06636   152 VLLTENAEVKLVDFGVSAQ-LDR---TVGRRNTFIGTPYWMAPEVIacdenpdATYDY--RSDIWSLGITAIE-MAEGAP 224

                  ....*..
gi 578806145 1288 PYRHIDP 1294
Cdd:cd06636   225 PLCDMHP 231
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
1087-1339 4.34e-15

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 77.76  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSRITEM--QQVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPY 1164
Cdd:cd06634    21 REIGHGSFGAVY---FARDVRNNEVVAIKKMSYSGKQsnEKWQDIIKEVKFLQKLRHPNTIEYRGCYLR-EHTAWLVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 mCHG---DLLQFIRSPQRNPTVKDLISFGLQvarGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYS 1241
Cdd:cd06634    97 -CLGsasDLLEVHKKPLQEVEIAAITHGALQ---GLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPANSFV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHrharlpvkWMALE---SLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRR-LPQPEYCPDSL 1317
Cdd:cd06634   173 GTPY--------WMAPEvilAMDEGQYDGKVDVWSLGITCIELAER-KPPLFNMNAMSALYHIAQNESpALQSGHWSEYF 243
                         250       260
                  ....*....|....*....|..
gi 578806145 1318 YQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd06634   244 RNFVDSCLQKIPQDRPTSDVLL 265
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1079-1284 5.11e-15

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: 77.54  E-value: 5.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1079 ERVVTHSDRV--IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIM- 1151
Cdd:cd07864     3 KRCVDKFDIIgiIGEGTYGQVY------KAKDKDTGELVALKKVRLDNEKEGFpitaIREIKILRQLNHRSVVNLKEIVt 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1152 --------LPPEGLPHVLLPYMCHgDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTV 1223
Cdd:cd07864    77 dkqdaldfKKDKGAFYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1224 KVADFGLARdildreYYSVQQHR--HARLPVKWMALES--LQTYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07864   156 KLADFGLAR------LYNSEESRpyTNKVITLWYRPPEllLGEERYGPAIDVWSCGCILGELFTK 214
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
1089-1284 6.79e-15

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: 76.88  E-value: 6.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRIqCAIKslsRITEMQQVEAF----LRE-GLLMRgLNHPNVLALIGIMLPpEGLPHVLL- 1162
Cdd:cd07843    13 IEEGTYGVVYRAR--DKKTGEI-VALK---KLKMEKEKEGFpitsLREiNILLK-LQHPNIVTVKEVVVG-SNLDKIYMv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 -PYMCHG--DLLQFIRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreY 1239
Cdd:cd07843    85 mEYVEHDlkSLMETMKQPFLQSEVKCLM---LQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAR------E 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1240 YSVQQHRHARLPVK-WM-ALESL-QTYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07843   156 YGSPLKPYTQLVVTlWYrAPELLlGAKEYSTAIDMWSVGCIFAELLTK 203
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
1087-1289 7.84e-15

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: 76.02  E-value: 7.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRiTEMQ--QVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd14072     6 KTIGKGNFAKVKLARHVLTGR---EVAIKIIDK-TQLNpsSLQKLFREVRIMKILNHPNIVKLFEVIETEKTL-YLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdildREYYSVQQ 1244
Cdd:cd14072    81 ASGGEVFDYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS-----NEFTPGNK 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1245 HRHARLPVKWMALESLQTYRFT-TKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14072   155 LDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPF 199
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
1089-1307 9.51e-15

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 75.87  E-value: 9.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIqcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKPDLPV--AIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSV-YLVMEYCNGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIrspQRNPTV-KDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDES---------FTVKVADFGLARDILDr 1237
Cdd:cd14120    78 DLADYL---QAKGTLsEDTIrVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNsgrkpspndIRLKIADFGFARFLQD- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1238 eyysvqQHRHARL---PVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRL 1307
Cdd:cd14120   154 ------GMMAATLcgsPM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEKNANL 218
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1086-1333 1.14e-14

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: 76.22  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIdqaQNRIQCAIKSLsRITEMQQVEA---FLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd08229    29 EKKIGRGQFSEVYRATCL---LDGVPVALKKV-QIFDLMDAKAradCIKEIDLLKQLNHPNVIKYYASFIEDNEL-NIVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTV---KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRey 1239
Cdd:cd08229   104 ELADAGDLSRMIKHFKKQKRLipeKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK-- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 ySVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPY-RHIDPFDLTHFLAQGRRLPQP-EYCPDSL 1317
Cdd:cd08229   182 -TTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYgDKMNLYSLCKKIEQCDYPPLPsDHYSEEL 259
                         250
                  ....*....|....*.
gi 578806145 1318 YQVMQQCWEADPAVRP 1333
Cdd:cd08229   260 RQLVNMCINPDPEKRP 275
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1087-1334 1.15e-14

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: 75.52  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdqaQNRIQCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd14663     6 RTLGEGTFAKVKFARNT---KTGESVAIKIIdkEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKI-FFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGlQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdILDReyySVQQ 1244
Cdd:cd14663    82 VTGGELFSKIAKNGRLKEDKARKYFQ-QLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLS--ALSE---QFRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 ----HRHARLPvKWMALESLQTYRFT-TKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGrRLPQPEYCPDSLYQ 1319
Cdd:cd14663   156 dgllHTTCGTP-NYVAPEVLARRGYDgAKADIWSCGVILFVLLA-GYLPFDDENLMALYRKIMKG-EFEYPRWFSPGAKS 232
                         250
                  ....*....|....*
gi 578806145 1320 VMQQCWEADPAVRPT 1334
Cdd:cd14663   233 LIKRILDPNPSTRIT 247
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
1125-1282 1.23e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 77.22  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1125 QVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLP-YMChgDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQ 1203
Cdd:PHA03209  100 QKGTTLIEAMLLQNVNHPSVIRMKD-TLVSGAITCMVLPhYSS--DLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1204 KFVHRDLAARNCMLDESFTVKVADFGLAR-DILDREYYSVQQhrharlPVKWMALESLQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:PHA03209  177 RIIHRDVKTENIFINDVDQVCIGDLGAAQfPVVAPAFLGLAG------TVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
1089-1339 1.42e-14

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 75.92  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06655    27 IGQGASGTVFTAIDVATGQ---EVAIKQIN-LQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDEL-FVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTvkDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyysvQQHRHA 1248
Cdd:cd06655   102 SLTDVVTETCMDEA--QIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPE-----QSKRST 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVK-WMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQG--RRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd06655   175 MVGTPyWMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYLNENPLRALYLIATNgtPELQNPEKLSPIFRDFLNRCL 253
                         250
                  ....*....|....
gi 578806145 1326 EADPAVRPTFRVLV 1339
Cdd:cd06655   254 EMDVEKRGSAKELL 267
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
1089-1283 1.50e-14

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: 76.17  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRiQCAIKSLSriTEMQQVEAF----LREGLLMRGLNHPNVLALIGIML-PPEGLPHVLLP 1163
Cdd:cd07842     8 IGRGTYGRVYKAKRKNGKDGK-EYAIKKFK--GDKEQYTGIsqsaCREIALLRELKHENVVSLVEVFLeHADKSVYLLFD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHgDLLQFI---RSPQRN----PTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLAR 1232
Cdd:cd07842    85 YAEH-DLWQIIkfhRQAKRVsippSMVKSLL---WQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLAR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1233 dildrEYYSVQQHRHARLPVK---WM-ALESLQTYRFTTKS-DVWSFGVLLWELLT 1283
Cdd:cd07842   161 -----LFNAPLKPLADLDPVVvtiWYrAPELLLGARHYTKAiDIWAIGCIFAELLT 211
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
1089-1334 1.59e-14

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: 76.23  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRIqCAIKSLS----RITEMQQveAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPY 1164
Cdd:cd06633    29 IGHGSFGAVYFAT--NSHTNEV-VAIKKMSysgkQTNEKWQ--DIIKEVKFLQQLKHPNTIEYKGCYLK-DHTAWLVMEY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 mCHG---DLLQFIRSPQRNPTVKDLISFGLQvarGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreyYS 1241
Cdd:cd06633   103 -CLGsasDLLEVHKKPLQEVEIAAITHGALQ---GLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSAS-------IA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARLPVkWMALE---SLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRR--LPQPEYCpDS 1316
Cdd:cd06633   172 SPANSFVGTPY-WMAPEvilAMDEGQYDGKVDIWSLGITCIELAER-KPPLFNMNAMSALYHIAQNDSptLQSNEWT-DS 248
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd06633   249 FRGFVDYCLQKIPQERPS 266
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
1087-1308 1.61e-14

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: 75.90  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhgEYIDQAQNRIQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd14209     7 KTLGTGSFGRV---MLVRHKETGNYYAMKILDKqkVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNL-YMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR------- 1237
Cdd:cd14209    83 VPGGEMFSHLRRIGRFSE-PHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRtwtlcgt 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1238 -EYysvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-RLP 1308
Cdd:cd14209   162 pEY---------------LAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGKvRFP 218
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
1087-1334 1.70e-14

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: 75.08  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQ----AQNRIQ-CAIKSLSRitemQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVL 1161
Cdd:cd06625     6 KLLGQGAFGQVYLCYDADTgrelAVKQVEiDPINTEAS----KEVKALECEIQLLKNLQHERIVQYYGCLQDEKSL-SIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIR---SPQRNPTVKdlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldre 1238
Cdd:cd06625    81 MEYMPGGSVKDEIKaygALTENVTRK----YTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRL---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 yysvqQHRHARLPVK-------WMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRRLPQ-P 1310
Cdd:cd06625   153 -----QTICSSTGMKsvtgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLTT-KPPWAEFEPMAAIFKIATQPTNPQlP 226
                         250       260
                  ....*....|....*....|....
gi 578806145 1311 EYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06625   227 PHVSEDARDFLSLIFVRNKKQRPS 250
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
1087-1340 1.90e-14

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: 75.07  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVY---H---GEYIdqAQNRIQCAIKSlsritEMQQveAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHV 1160
Cdd:cd06605     7 GELGEGNGGVVSkvrHrpsGQIM--AVKVIRLEIDE-----ALQK--QILRELDVLHKCNSPYIVGFYGAFYS-EGDISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSPQRNPtvKDLISF-GLQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFG--------L 1230
Cdd:cd06605    77 CMEYMDGGSLDKILKEVGRIP--ERILGKiAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGvsgqlvdsL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 ARDILDREYYsvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHID------PFDLTHFLAQG 1304
Cdd:cd06605   155 AKTFVGTRSY--------------MAPERISGGKYTVKSDIWSLGLSLVELAT-GRFPYPPPNakpsmmIFELLSYIVDE 219
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578806145 1305 R--RLPQPEYCPDsLYQVMQQCWEADPAVRPTFRVLVG 1340
Cdd:cd06605   220 PppLLPSGKFSPD-FQDFVSQCLQKDPTERPSYKELME 256
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
1088-1345 2.16e-14

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 75.04  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYidqaQNRIQCAIKSLSRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPeglPHV-LLPYMC 1166
Cdd:cd14153     7 LIGKGRFGQVYHGRW----HGEVAIRLIDIERDNE-EQLKAFKREVMAYRQTRHENVVLFMGACMSP---PHLaIITSLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HG-DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESfTVKVADFGLARdiLDREYYSVQQH 1245
Cdd:cd14153    79 KGrTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLFT--ISGVLQAGRRE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVKWMALESLQTYR------------FTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRR--LPQPE 1311
Cdd:cd14153   156 DKLRIQSGWLCHLAPEIIRqlspeteedklpFSKHSDVFAFGTIWYELHAR-EWPFKTQPAEAIIWQVGSGMKpnLSQIG 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578806145 1312 YCPDsLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14153   235 MGKE-ISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
1089-1287 2.36e-14

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: 75.16  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRI---TEMQQVEAF-LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlpY 1164
Cdd:cd07839     8 IGEGTYGTVF------KAKNRETHEIVALKRVrldDDDEGVPSSaLREICLLKELKHKNIVRLYDVLHSDKKLTLVF--E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDildreyYSVqq 1244
Cdd:cd07839    80 YCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA------FGI-- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1245 hrharlPVKWMALESLQT-YR----------FTTKSDVWSFGVLLWELLTRGAP 1287
Cdd:cd07839   152 ------PVRCYSAEVVTLwYRppdvlfgaklYSTSIDMWSAGCIFAELANAGRP 199
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
1128-1342 2.47e-14

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


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 74.95  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1128 AFLREGLLMRGLNHPNVLALIGIMLP-PEGLphVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFV 1206
Cdd:cd05076    61 AFFETASLMSQVSHTHLVFVHGVCVRgSENI--MVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLV 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1207 HRDLAARNCML-------DESFTVKVADFGLARDILDREyysvqqHRHARLPvkWMALESLQT-YRFTTKSDVWSFGVLL 1278
Cdd:cd05076   139 HGNVCAKNILLarlgleeGTSPFIKLSDPGVGLGVLSRE------ERVERIP--WIAPECVPGgNSLSTAADKWGFGATL 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1279 WELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEyCPDsLYQVMQQCWEADPAVRPTFRVLVGEV 1342
Cdd:cd05076   211 LEICFNGEAPLQSRTPSEKERFYQRQHRLPEPS-CPE-LATLISQCLTYEPTQRPSFRTILRDL 272
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
1088-1334 2.71e-14

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 74.22  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQqveaFLREGL-LMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC 1166
Cdd:cd14068     1 LLGDGGFGSVYRAVYRGE-----DVAVKIFNKHTSFR----LLRQELvVLSHLHHPSLVALLAAGTAPRMLVMELAPKGS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFiRSPQRNPTVKDLISfgLQVARGMEYLAEQKFVHRDLAARNCML-----DESFTVKVADFGLARDILDREYYS 1241
Cdd:cd14068    72 LDALLQQ-DNASLTRTLQHRIA--LHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARLPvkwmaleslQTYR----FTTKSDVWSFGVLLWELLTRGAppyRHID----PFDLTHFLAQGrRLPQP--E 1311
Cdd:cd14068   149 SEGTPGFRAP---------EVARgnviYNQQADVYSFGLLLYDILTCGE---RIVEglkfPNEFDELAIQG-KLPDPvkE 215
                         250       260
                  ....*....|....*....|....*.
gi 578806145 1312 Y-CP--DSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14068   216 YgCApwPGVEALIKDCLKENPQCRPT 241
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
1089-1334 2.73e-14

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: 74.40  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVyhgEYIDQAQNRIQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06648    15 IGEGSTGIV---CIATDKSTGRQVAVKKMD-LRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDEL-WVVMEFLEGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIrsPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyySVQQHRHA 1248
Cdd:cd06648    90 ALTDIV--THTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSK----EVPRRKSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFL--AQGRRLPQPEYCPDSLYQVMQQCWE 1326
Cdd:cd06648   164 VGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMV-DGEPPYFNEPPLQAMKRIrdNEPPKLKNLHKVSPRLRSFLDRMLV 242

                  ....*...
gi 578806145 1327 ADPAVRPT 1334
Cdd:cd06648   243 RDPAQRAT 250
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
1087-1282 2.92e-14

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: 74.23  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPY 1164
Cdd:cd14079     8 KTLGVGSFGKVKLAEHELTGH---KVAVKILNRqkIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIF-MVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYY--SV 1242
Cdd:cd14079    84 VSGGELFDYIVQKGRLSE-DEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLktSC 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578806145 1243 QQHRHArlpvkwmALE--SLQTYRfTTKSDVWSFGVLLWELL 1282
Cdd:cd14079   163 GSPNYA-------APEviSGKLYA-GPEVDVWSCGVILYALL 196
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
1089-1283 3.02e-14

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: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRItEMQQVE-----AFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLP 1163
Cdd:cd07845    15 IGEGTYGIVY------RARDTTSGEIVALKKV-RMDNERdgipiSSLREITLLLNLRHPNIVELKEVVVG-KHLDSIFLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 Y-MCHGD---LLQFIRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdildREY 1239
Cdd:cd07845    87 MeYCEQDlasLLDNMPTPFSESQVKCLM---LQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA-----RTY 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1240 YSVQQHRHARLPVKWM-ALESL---QTYrfTTKSDVWSFGVLLWELLT 1283
Cdd:cd07845   159 GLPAKPMTPKVVTLWYrAPELLlgcTTY--TTAIDMWAVGCILAELLA 204
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1088-1282 3.05e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 77.00  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLsriteMQQVEAFLREGLLMRGLNHPNVLAL---------------IGIML 1152
Cdd:PTZ00036   73 IIGNGSFGVVYEAICIDTSE---KVAIKKV-----LQDPQYKNRELLIMKNLNHINIIFLkdyyytecfkkneknIFLNV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1153 PPEGLPHVLLPYMCHgdllqFIRSPQRNPT--VKdLISFglQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFG 1229
Cdd:PTZ00036  145 VMEFIPQTVHKYMKH-----YARNNHALPLflVK-LYSY--QLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFG 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1230 LARDIL-DREYYSVQQHRHARLPvKWMalesLQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:PTZ00036  217 SAKNLLaGQRSVSYICSRFYRAP-ELM----LGATNYTTHIDLWSLGCIIAEMI 265
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
1087-1322 3.11e-14

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: 74.21  E-value: 3.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlPPEGLPHVLLPYMC 1166
Cdd:cd14185     6 RTIGDGNFAVVKECRHWNENQ---EYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVY-ETEKEIYLILEYVR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARDILdREYYSV 1242
Cdd:cd14185    82 GGDLFDAIIESVKFTE-HDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT-GPIFTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 qqhrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRhidpfdlthflaqgrrlpQPEYCPDSLYQVMQ 1322
Cdd:cd14185   160 -----CGTPT-YVAPEILSEKGYGLEVDMWAAGVILYILLC-GFPPFR------------------SPERDQEELFQIIQ 214
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
1089-1289 3.32e-14

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: 74.61  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPYMcHG 1168
Cdd:cd07870     8 LGEGSYATVYKG--ISRINGQL-VALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVF-EYM-HT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--DILDREYYSVQQHR 1246
Cdd:cd07870    83 DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARakSIPSQTYSSEVVTL 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1247 HARLPVKWMAleslqTYRFTTKSDVWSFGVLLWELLtRGAPPY 1289
Cdd:cd07870   163 WYRPPDVLLG-----ATDYSSALDIWGAGCIFIEML-QGQPAF 199
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
1088-1287 4.26e-14

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 75.20  E-value: 4.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVyhGEYIDQaQNRIQCAIKSLSRITE-MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLP----HVLL 1162
Cdd:cd07859     7 VIGKGSYGVV--CSAIDT-HTGEKVAIKKINDVFEhVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRREfkdiYVVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMcHGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--------DI 1234
Cdd:cd07859    84 ELM-ESDLHQVIKA-NDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARvafndtptAI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1235 LDREYYSVQQHRHARLPVKWMAleslqtyRFTTKSDVWSFGVLLWELLTrGAP 1287
Cdd:cd07859   162 FWTDYVATRWYRAPELCGSFFS-------KYTPAIDIWSIGCIFAEVLT-GKP 206
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
1087-1304 5.36e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 75.02  E-value: 5.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidQAQNRIQCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLPY 1164
Cdd:PTZ00426   36 RTLGTGSFGRVILATY--KNEDFPPVAIKRFekSKIIKQKQVDHVFSERKILNYINHPFCVNLYG-SFKDESYLYLVLEF 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTvkDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREYYSVq 1243
Cdd:PTZ00426  113 VIGGEFFTFLRRNKRFPN--DVGCFyAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK-VVDTRTYTL- 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1244 qhrhARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQG 1304
Cdd:PTZ00426  189 ----CGTP-EYIAPEILLNVGHGKAADWWTLGIFIYEILV-GCPPFYANEPLLIYQKILEG 243
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1087-1334 5.88e-14

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: 73.49  E-value: 5.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLsRITEMQQ--VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd06626     6 NKIGEGTFGKVYTAVNLDTGE---LMAMKEI-RFQDNDPktIKEIADEMKVLEGLDHPNLVRYYGVEVHREEV-YIFMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVkdLIS-FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysvQ 1243
Cdd:cd06626    81 CQEGTLEELLRHGRILDEA--VIRvYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNT----T 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARL------PVkWMALESLQTYRFTTK---SDVWSFGVLLWELLTrGAPP-YRHIDPFDLTHFLAQGRR--LPQPE 1311
Cdd:cd06626   155 TMAPGEVnslvgtPA-YMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPwSELDNEWAIMYHVGMGHKppIPDSL 232
                         250       260
                  ....*....|....*....|...
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06626   233 QLSPEGKDFLSRCLESDPKKRPT 255
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
1087-1296 6.16e-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: 75.02  E-value: 6.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVV------YHGEYIdqaqnriqcAIKSLSR--ITEMQQVEAFlREGLLMRGLNHPNVLALIGIMLPPEGLP 1158
Cdd:cd07851    21 SPVGSGAYGQVcsafdtKTGRKV---------AIKKLSRpfQSAIHAKRTY-RELRLLKHMKHENVIGLLDVFTPASSLE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 H-----VLLPYMcHGDLLQFIRSPQRNptvKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR 1232
Cdd:cd07851    91 DfqdvyLVTHLM-GADLNNIVKCQKLS---DDHIQFLVyQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1233 DiLDREYYSVQQHRHARLP---VKWMaleslqtyRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFD 1296
Cdd:cd07851   167 H-TDDEMTGYVATRWYRAPeimLNWM--------HYNQTVDIWSVGCIMAELLT-GKTLFPGSDHID 223
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
1089-1295 6.30e-14

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 74.45  E-value: 6.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMC-H 1167
Cdd:cd13988     1 LGQGATANVFRGRHKKTGD---LYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRHKVLVMELCpC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRnptvkdliSFGL----------QVARGMEYLAEQKFVHRDLAARNCML---DESFTV-KVADFGLARD 1233
Cdd:cd13988    78 GSLYTVLEEPSN--------AYGLpeseflivlrDVVAGMNHLRENGIVHRDIKPGNIMRvigEDGQSVyKLTDFGAARE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1234 ILDRE----YYSVQQHRHARLPVKWMALESLQTyRFTTKSDVWSFGVLLWELLTrGAPPYRhidPF 1295
Cdd:cd13988   150 LEDDEqfvsLYGTEEYLHPDMYERAVLRKDHQK-KYGATVDLWSIGVTFYHAAT-GSLPFR---PF 210
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
1089-1287 6.70e-14

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: 73.90  E-value: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIqCAIK--SLSRITEMQQVEAfLREGLLMRGLN-HPNVLALIGIMLPPEGLPHVLlPYM 1165
Cdd:cd07832     8 IGEGAHGIVF--KAKDRETGET-VALKkvALRKLEGGIPNQA-LREIKALQACQgHPYVVKLRDVFPHGTGFVLVF-EYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHgDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR---DILDREYYSv 1242
Cdd:cd07832    83 LS-SLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARlfsEEDPRLYSH- 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1243 qqhrhaRLPVKW-MALESL---QTYrfTTKSDVWSFGVLLWELLtRGAP 1287
Cdd:cd07832   161 ------QVATRWyRAPELLygsRKY--DEGVDLWAVGCIFAELL-NGSP 200
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
1089-1284 7.39e-14

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: 74.36  E-value: 7.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNrIQCAIKSLSRI--TEMQQVEAfLREGLLMRGL-NHPNVLALIGIMLP-PEGLPHVLLpY 1164
Cdd:cd07857     8 LGQGAYGIVCSARNAETSEE-ETVAIKKITNVfsKKILAKRA-LRELKLLRHFrGHKNITCLYDMDIVfPGNFNELYL-Y 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 M--CHGDLLQFIRSPQRnPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIlDREYYSV 1242
Cdd:cd07857    85 EelMEADLHQIIRSGQP-LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGF-SENPGEN 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1243 QQHRHARLPVKWM-ALESLQTYRFTTKS-DVWSFGVLLWELLTR 1284
Cdd:cd07857   163 AGFMTEYVATRWYrAPEIMLSFQSYTKAiDVWSVGCILAELLGR 206
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
1085-1279 7.45e-14

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 73.22  E-value: 7.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1085 SDRVIGKGHFGVVYHGEyidQAQNRIQCAIKSLSRITEMQQVEAFLR-EGLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd14082     7 PDEVLGSGQFGIVYGGK---HRKTGRDVAIKVIDKLRFPTKQESQLRnEVAILQQLSHPGVVNLECMFETPERV-FVVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMcHGDLLQFIRSPQR----NPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCML--DESF-TVKVADFGLARDILD 1236
Cdd:cd14082    83 KL-HGDMLEMILSSEKgrlpERITKFLVT---QILVALRYLHSKNIVHCDLKPENVLLasAEPFpQVKLCDFGFARIIGE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1237 REYysvqqHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLW 1279
Cdd:cd14082   159 KSF-----RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
1089-1296 8.41e-14

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: 74.60  E-value: 8.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeYIDQAQNRIQCAIKSLSRI--TEMQQVEAFlREGLLMRGLNHPNVLALIGIMLPPEGLP-----HVL 1161
Cdd:cd07880    23 VGSGAYGTVC---SALDRRTGAKVAIKKLYRPfqSELFAKRAY-RELRLLKHMKHENVIGLLDVFTPDLSLDrfhdfYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMcHGDLLQFIRSPQRNptvKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIlDRE-- 1238
Cdd:cd07880    99 MPFM-GTDLGKLMKHEKLS---EDRIQFLVyQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQT-DSEmt 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1239 -YYSVQQHRHARLPVKWMaleslqtyRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFD 1296
Cdd:cd07880   174 gYVVTRWYRAPEVILNWM--------HYTQTVDIWSVGCIMAEMLT-GKPLFKGHDHLD 223
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
1089-1339 8.71e-14

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: 73.60  E-value: 8.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06656    27 IGQGASGTVYTAIDIATGQ---EVAIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDEL-WVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPtvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyysvQQHRHA 1248
Cdd:cd06656   102 SLTDVVTETCMDE--GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE-----QSKRST 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVK-WMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQG--RRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd06656   175 MVGTPyWMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYLNENPLRALYLIATNgtPELQNPERLSAVFRDFLNRCL 253
                         250
                  ....*....|....
gi 578806145 1326 EADPAVRPTFRVLV 1339
Cdd:cd06656   254 EMDVDRRGSAKELL 267
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
1089-1318 9.60e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.03  E-value: 9.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIqCAIK-------SLSRITEMQQVE------AFLREGLLMRGLNHPNVLALIGIMLPpE 1155
Cdd:PTZ00024   17 LGEGTYGKVE--KAYDTLTGKI-VAIKkvkiieiSNDVTKDRQLVGmcgihfTTLRELKIMNEIKHENIMGLVDVYVE-G 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 GLPHVLLPYMcHGDLLQFIRSPQR--NPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR- 1232
Cdd:PTZ00024   93 DFINLVMDIM-ASDLKKVVDRKIRltESQVKCIL---LQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARr 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1233 --------DILDREYYSVQQHRHARLPVKWM-ALESLQ-TYRFTTKSDVWSFGVLLWELLTRGA--PPYRHIDPFDLTHF 1300
Cdd:PTZ00024  169 ygyppysdTLSKDETMQRREEMTSKVVTLWYrAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPlfPGENEIDQLGRIFE 248
                         250
                  ....*....|....*...
gi 578806145 1301 LaqgRRLPQPEYCPDSLY 1318
Cdd:PTZ00024  249 L---LGTPNEDNWPQAKK 263
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
1088-1294 1.13e-13

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 73.21  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLP--PEGLPHVL---L 1162
Cdd:cd06637    13 LVGNGTYGQVYKGRHVKTGQ---LAAIKVMD-VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKknPPGMDDQLwlvM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDiLDReyyS 1241
Cdd:cd06637    89 EFCGAGSVTDLIKNTKGNTLKEEWIAYiCREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ-LDR---T 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARLPVKWMALESL-------QTYRFttKSDVWSFGVLLWElLTRGAPPYRHIDP 1294
Cdd:cd06637   165 VGRRNTFIGTPYWMAPEVIacdenpdATYDF--KSDLWSLGITAIE-MAEGAPPLCDMHP 221
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
1084-1339 1.21e-13

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 72.67  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHG---EYIDQAQ-NRIQCAIKSLSRiTEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPpeGLPH 1159
Cdd:cd05078     2 IFNESLGQGTFTKIFKGirrEVGDYGQlHETEVLLKVLDK-AHRNYSESFFEAASMMSQLSHKHLVLNYGVCVC--GDEN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLL-PYMCHGDLLQFIRspqRNPTVKDlISFGLQVAR----GMEYLAEQKFVHRDLAARNCML---DESFT-----VKVA 1226
Cdd:cd05078    79 ILVqEYVKFGSLDTYLK---KNKNCIN-ILWKLEVAKqlawAMHFLEEKTLVHGNVCAKNILLireEDRKTgnppfIKLS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1227 DFGLARDILDREYYsvqqhrHARLPvkWMALESLQTYR-FTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGR 1305
Cdd:cd05078   155 DPGISITVLPKDIL------LERIP--WVPPECIENPKnLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRH 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578806145 1306 RLPQPEYCpdSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd05078   227 QLPAPKWT--ELANLINNCMDYEPDHRPSFRAII 258
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
1088-1289 1.28e-13

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 72.59  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPHV-LLPY 1164
Cdd:cd14186     8 LLGKGSFACVYRARSLHTGL---EVAIKMIDKkaMQKAGMVQRVRNEVEIHCQLKHPSILELYNYF---EDSNYVyLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCH-GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyySVQ 1243
Cdd:cd14186    82 MCHnGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQL------KMP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1244 QHRHARL--PVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14186   156 HEKHFTMcgTPNYISPEIATRSAHGLESDVWSLGCMFYTLLV-GRPPF 202
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
1089-1334 1.28e-13

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 73.14  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNR---IQCAIKSLSRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd06643    13 LGDGAFGKVY------KAQNKetgILAAAKVIDTKSE-EELEDYMVEIDILASCDHPNIVKLLDAFYYENNL-WILIEFC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA----RDILDREYYS 1241
Cdd:cd06643    85 AGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSakntRTLQRRDSFI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHrharlpvkWMA-----LESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGR--RLPQPEYCP 1314
Cdd:cd06643   165 GTPY--------WMApevvmCETSKDRPYDYKADVWSLGVTLIE-MAQIEPPHHELNPMRVLLKIAKSEppTLAQPSRWS 235
                         250       260
                  ....*....|....*....|
gi 578806145 1315 DSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06643   236 PEFKDFLRKCLEKNVDARWT 255
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
1089-1293 1.31e-13

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: 73.93  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidQAQNRIQCAIKSLSR-ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPP---EGLPHVLLPY 1164
Cdd:cd07878    23 VGSGAYGSVCSAY---DTRLRQKVAVKKLSRpFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPAtsiENFNEVYLVT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRnpTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE--YYS 1241
Cdd:cd07878   100 NLMGADLNNIVKCQK--LSDEHVQFLIyQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEMtgYVA 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1242 VQQHRHARLPVKWMaleslqtyRFTTKSDVWSFGVLLWELLTRGA--PPYRHID 1293
Cdd:cd07878   178 TRWYRAPEIMLNWM--------HYNQTVDIWSVGCIMAELLKGKAlfPGNDYID 223
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
1089-1310 1.42e-13

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: 72.29  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidQAQNRIqCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMC 1166
Cdd:cd14161    11 LGKGTYGRVKKAR---DSSGRL-VAIKSIrkDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIV-IVMEYAS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRnPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArDILDREYYsVQQHR 1246
Cdd:cd14161    86 RGDLYDYISERQR-LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS-NLYNQDKF-LQTYC 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1247 HARLpvkWMALESLQTYRFT-TKSDVWSFGVLLWeLLTRGAPPYRHIDPFDLTHFLAQG--RRLPQP 1310
Cdd:cd14161   163 GSPL---YASPEIVNGRPYIgPEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGayREPTKP 225
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
1089-1284 1.48e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 72.84  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyidqaQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd07861     8 IGEGTYGVVYKG------RNKKTGQIVAMKKIRLESEEEGVpstaIREISLLKELQHPNIVCLEDVLMQENRL-YLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHgDLLQFIRSPQRNPTV-KDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreYYSV 1242
Cdd:cd07861    81 LSM-DLKKYLDSLPKGKYMdAELVkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF----GIPV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1243 QQHRHARLPVKWMALESL-QTYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07861   156 RVYTHEVVTLWYRAPEVLlGSPRYSTPVDIWSIGTIFAEMATK 198
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
1089-1339 1.53e-13

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: 72.83  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06654    28 IGQGASGTVYTAMDVATGQ---EVAIRQMN-LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDEL-WVVMEYLAGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPtvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyysvQQHRHA 1248
Cdd:cd06654   103 SLTDVVTETCMDE--GQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE-----QSKRST 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVK-WMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQG--RRLPQPEYCPDSLYQVMQQCW 1325
Cdd:cd06654   176 MVGTPyWMAPEVVTRKAYGPKVDIWSLGIMAIEMI-EGEPPYLNENPLRALYLIATNgtPELQNPEKLSAIFRDFLNRCL 254
                         250
                  ....*....|....
gi 578806145 1326 EADPAVRPTFRVLV 1339
Cdd:cd06654   255 EMDVEKRGSAKELL 268
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
1087-1322 1.60e-13

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: 72.12  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyHGEYidqaQNRIQC--AIKSLSRITEMQQ-VEAFL-REGLLMRGLNHPNVLALIGIMLPPEGLPHVLL 1162
Cdd:cd14165     7 INLGEGSYAKV-KSAY----SERLKCnvAIKIIDKKKAPDDfVEKFLpRELEILARLNHKSIIKTYEIFETSDGKVYIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd14165    82 ELGVQGDLLEFIKL-RGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHARLPVKWMALESLQTYRFTTK-SDVWSFGVLLWELLTrGAPPY-----RHIDPFDLTHFLAQGRRLPQPEYCPDS 1316
Cdd:cd14165   161 VLSKTFCGSAAYAAPEVLQGIPYDPRiYDIWSLGVILYIMVC-GSMPYddsnvKKMLKIQKEHRVRFPRSKNLTSECKDL 239

                  ....*.
gi 578806145 1317 LYQVMQ 1322
Cdd:cd14165   240 IYRLLQ 245
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1089-1289 1.63e-13

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: 72.69  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQaQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGI-----MLPPEGLPHVLLP 1163
Cdd:cd14038     2 LGTGGFGNVL--RWINQ-ETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVpeglqKLAPNDLPLLAME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQ-----RNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARDI- 1234
Cdd:cd14038    79 YCQGGDLRKYLNQFEnccglREGAILTLLS---DISSALRYLHENRIIHRDLKPENIVLqqgEQRLIHKIIDLGYAKELd 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1235 ---LDREYYSVQQhrharlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14038   156 qgsLCTSFVGTLQ---------YLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
1122-1334 1.66e-13

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: 72.01  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1122 EMQQVEAFLrEGLLmrGLNHPNVLALIGIMLPPEGLP-----HVLLPYM---CHGDLLQFIRS-PqrnptVKDLISFGLQ 1192
Cdd:cd14012    41 QIQLLEKEL-ESLK--KLRHPNLVSYLAFSIERRGRSdgwkvYLLTEYApggSLSELLDSVGSvP-----LDTARRWTLQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1193 VARGMEYLAEQKFVHRDLAARNCMLDESF---TVKVADFGLARDILDreyYSVQQHRHARLPVKWMALESLQTY-RFTTK 1268
Cdd:cd14012   113 LLEALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLLD---MCSRGSLDEFKQTYWLPPELAQGSkSPTRK 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1269 SDVWSFGVLLWELLTRGAPPYRHIDPFDlthflaqgrrLPQPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14012   190 TDVWDLGLLFLQMLFGLDVLEKYTSPNP----------VLVSLDLSASLQDFLSKCLSLDPKKRPT 245
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
1087-1290 1.78e-13

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 71.97  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgEYIDQAQNRiQCAIKSLSRiTEMQQVEAFLR-EGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd14095     6 RVIGDGNFAVVK--ECRDKATDK-EYALKIIDK-AKCKGKEHMIEnEVAILRRVKHPNIVQLIEEYDTDTEL-YLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNP------TVKDLisfglqvARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARdIL 1235
Cdd:cd14095    81 KGGDLFDAITSSTKFTerdasrMVTDL-------AQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLAT-EV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1236 DREYYSVqqhrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd14095   153 KEPLFTV-----CGTPT-YVAPEILAETGYGLKVDIWAAGVITYILLC-GFPPFR 200
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
1089-1345 1.83e-13

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: 72.31  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAqnriqcAIKSLSRITEMQQ-VEAFLREGLLMRGLNHPNVLALIGIMLPPeglPHV-LLPYMC 1166
Cdd:cd14152     8 IGQGRWGKVHRGRWHGEV------AIRLLEIDGNNQDhLKLFKKEVMNYRQTRHENVVLFMGACMHP---PHLaIITSFC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HG-DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESfTVKVADFGLardildreyYS---- 1241
Cdd:cd14152    79 KGrTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGL---------FGisgv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHA---RLPVKWMALESLQTYR------------FTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQG-- 1304
Cdd:cd14152   149 VQEGRREnelKLPHDWLCYLAPEIVRemtpgkdedclpFSKAADVYAFGTIWYELQAR-DWPLKNQPAEALIWQIGSGeg 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578806145 1305 -RRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQI 1345
Cdd:cd14152   228 mKQVLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
1078-1334 1.92e-13

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 72.06  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1078 HERVVthsdrvIGKGHFGVVYHGEYIDqaqNRIQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGL 1157
Cdd:cd06624    11 GERVV------LGKGTFGVVYAARDLS---TQVRIAIKEIP-ERDSREVQPLHEEIALHSRLSHKNIVQYLG-SVSEDGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1158 PHVLLPYMCHGDLLQFIRS---PQRNPtvKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDE-SFTVKVADFGLAR 1232
Cdd:cd06624    80 FKIFMEQVPGGSLSALLRSkwgPLKDN--ENTIGYyTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1233 dildreyysvqqhRHARL-PV--------KWMALESL-QTYR-FTTKSDVWSFGVLLWELLTRGAPPYRHIDP----FDL 1297
Cdd:cd06624   158 -------------RLAGInPCtetftgtlQYMAPEVIdKGQRgYGPPADIWSLGCTIIEMATGKPPFIELGEPqaamFKV 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578806145 1298 THFlaqgRRLPQ-PEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06624   225 GMF----KIHPEiPESLSEEAKSFILRCFEPDPDKRAT 258
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
1089-1334 1.95e-13

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: 72.35  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHgeyIDQAQNRIQCAIKSLSRITEM-QQVEAflrEGLLMRGL-NHPNVLALIGIMLPPE---GLPHVLLP 1163
Cdd:cd06638    26 IGKGTYGKVFK---VLNKKNGSKAAVKILDPIHDIdEEIEA---EYNILKALsDHPNVVKFYGMYYKKDvknGDQLWLVL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHG----DLLQ-FIRSPQRnpTVKDLISFGLQVA-RGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdr 1237
Cdd:cd06638   100 ELCNGgsvtDLVKgFLKRGER--MEEPIIAYILHEAlMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT-- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 eyySVQQHRHARLPVK-WMALESLQTYR-----FTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQG--RRLPQ 1309
Cdd:cd06638   176 ---STRLRRNTSVGTPfWMAPEVIACEQqldstYDARCDVWSLGITAIE-LGDGDPPLADLHPMRALFKIPRNppPTLHQ 251
                         250       260
                  ....*....|....*....|....*
gi 578806145 1310 PEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06638   252 PELWSNEFNDFIRKCLTKDYEKRPT 276
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1087-1336 2.15e-13

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: 71.70  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLS-RITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYM 1165
Cdd:cd08223     6 RVIGKGSYGEVW---LVRHKRDRKQYVIKKLNlKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMGFC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKD-LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDRE------ 1238
Cdd:cd08223    83 EGGDLYTRLKEQKGVLLEERqVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR-VLESSsdmatt 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 -----YYsvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrgappYRHI----DPFDLTHFLAQGRRLPQ 1309
Cdd:cd08223   162 ligtpYY--------------MSPELFSNKPYNHKSDVWALGCCVYEMAT-----LKHAfnakDMNSLVYKILEGKLPPM 222
                         250       260
                  ....*....|....*....|....*...
gi 578806145 1310 P-EYCPDsLYQVMQQCWEADPAVRPTFR 1336
Cdd:cd08223   223 PkQYSPE-LGELIKAMLHQDPEKRPSVK 249
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1089-1334 2.29e-13

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 71.55  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVvyhGEYIDQAQNRIQCAIKSLSRITEMQqvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMCHG 1168
Cdd:cd14665     8 IGSGNFGV---ARLMRDKQTKELVAVKYIERGEKID--ENVQREIINHRSLRHPNIVRFKEVILTPTHLA-IVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGlQVARGMEYLAEQKFVHRDLAARNCMLDESFT--VKVADFGLARdildreyySVQQHR 1246
Cdd:cd14665    82 ELFERICNAGRFSEDEARFFFQ-QLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSK--------SSVLHS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 HARLPV---KWMALESLQTYRFTTK-SDVWSFGVLLWELLTrGAPPYRhiDPFDLTHFLAQGRRLPQPEYC-PDSLY--- 1318
Cdd:cd14665   153 QPKSTVgtpAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLV-GAYPFE--DPEEPRNFRKTIQRILSVQYSiPDYVHisp 229
                         250
                  ....*....|....*....
gi 578806145 1319 ---QVMQQCWEADPAVRPT 1334
Cdd:cd14665   230 ecrHLISRIFVADPATRIT 248
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
1087-1334 2.84e-13

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: 72.39  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRIqCAIKSLSRITEM--QQVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPY 1164
Cdd:cd06635    31 REIGHGSFGAVYFAR--DVRTSEV-VAIKKMSYSGKQsnEKWQDIIKEVKFLQRIKHPNSIEYKGCYLR-EHTAWLVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 mCHG---DLLQFIRSPQRNPTVKDLISFGLQvarGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYS 1241
Cdd:cd06635   107 -CLGsasDLLEVHKKPLQEIEIAAITHGALQ---GLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHrharlpvkWMALE---SLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRR--LPQPEYCpDS 1316
Cdd:cd06635   183 GTPY--------WMAPEvilAMDEGQYDGKVDVWSLGITCIELAER-KPPLFNMNAMSALYHIAQNESptLQSNEWS-DY 252
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd06635   253 FRNFVDSCLQKIPQDRPT 270
IPT_PCSR cd00603
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
569-683 2.89e-13

IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238337 [Multi-domain]  Cd Length: 90  Bit Score: 66.71  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  569 PKLTEFHPHSGPLRGSTRLTLCGSNFYLHPsglvpeGTHQVTVGQSPCRPLPKDSSKLrpvprkdfveefECELEPLGTQ 648
Cdd:cd00603     1 PVITSISPSSGPLSGGTRLTITGSNLGSGS------PRVRVTVGGVPCKVLNVSSTEI------------VCRTPAAATP 62
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578806145  649 AVGPTNVSLTVTNMppgkhfrVDGTSVLRGFSFME 683
Cdd:cd00603    63 GEGPVEVTVDGANV-------SARVLSNTTFTYVE 90
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
1087-1347 3.09e-13

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: 71.22  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhGEYIDQAQNRiQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd14184     7 KVIGDGNFAVV--KECVERSTGK-EFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAEL-YLVMELVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNpTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLArDILDREYYSV 1242
Cdd:cd14184    83 GGDLFDAITSSTKY-TERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLA-TVVEGPLYTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 qqhrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR-----HIDPFDltHFLAQGRRLPQPEY--CPD 1315
Cdd:cd14184   161 -----CGTPT-YVAPEIIAETGYGLKVDIWAAGVITYILLC-GFPPFRsennlQEDLFD--QILLGKLEFPSPYWdnITD 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578806145 1316 SLYQVMQQCWEADPAVRPTfrvlvgeVEQIVS 1347
Cdd:cd14184   232 SAKELISHMLQVNVEARYT-------AEQILS 256
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
1089-1334 3.55e-13

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: 71.95  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHgeyIDQAQNRIQCAIKSLSRITEM-QQVEAflrEGLLMRGL-NHPNVLALIGIMLPPE---GLPHVLLP 1163
Cdd:cd06639    30 IGKGTYGKVYK---VTNKKDGSLAAVKILDPISDVdEEIEA---EYNILRSLpNHPNVVKFYGMFYKADqyvGGQLWLVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHG----DLLQ-FIRSPQRnpTVKDLISFGLQVAR-GMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdr 1237
Cdd:cd06639   104 ELCNGgsvtELVKgLLKCGQR--LDEAMISYILYGALlGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT-- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 eyySVQQHRHARLPVK-WMALESLQT-----YRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLthfLAQGRRLPQP- 1310
Cdd:cd06639   180 ---SARLRRNTSVGTPfWMAPEVIACeqqydYSYDARCDVWSLGITAIE-LADGDPPLFDMHPVKA---LFKIPRNPPPt 252
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1311 -----EYCpDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06639   253 llnpeKWC-RGFSHFISQCLIKDFEKRPS 280
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
1088-1289 3.64e-13

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: 72.33  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNriqCAIKSLSR--ITEMQQVEAFLREGLLMRGLN---HPNVLALIGIMLPPEglpHV-- 1160
Cdd:cd05589     6 VLGRGHFGKVLLAEYKPTGEL---FAIKALKKgdIIARDEVESLMCEKRIFETVNsarHPFLVNLFACFQTPE---HVcf 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSpqrnptvkDLIS------FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI 1234
Cdd:cd05589    80 VMEYAAGGDLMMHIHE--------DVFSepravfYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1235 L---DR--------EYysvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05589   152 MgfgDRtstfcgtpEF---------------LAPEVLTDTSYTRAVDWWGLGVLIYEMLV-GESPF 201
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
1088-1334 3.74e-13

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: 72.01  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAqnriqCAIKSLSRitemQQVEAFLREGLLMR--GLNHPNVLALIGI--MLPPEGLPH--VL 1161
Cdd:cd14054     2 LIGQGRYGTVWKGSLDERP-----VAVKVFPA----RHRQNFQNEKDIYElpLMEHSNILRFIGAdeRPTADGRMEylLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIRspqrNPTVkDLISF---GLQVARGMEYLAEQK---------FVHRDLAARNCMLDESFTVKVADFG 1229
Cdd:cd14054    73 LEYAPKGSLCSYLR----ENTL-DWMSScrmALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGSCVICDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1230 LARDILDREYYSVQ-QHRHARLP-----VKWMALESL-------QTYRFTTKSDVWSFGVLLWELLTR--------GAPP 1288
Cdd:cd14054   148 LAMVLRGSSLVRGRpGAAENASIsevgtLRYMAPEVLegavnlrDCESALKQVDVYALGLVLWEIAMRcsdlypgeSVPP 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1289 YR---------HIDPFDLTHFLAQGRRLPQ-PEY------CPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14054   228 YQmpyeaelgnHPTFEDMQLLVSREKARPKfPDAwkenslAVRSLKETIEDCWDQDAEARLT 289
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
1087-1290 3.95e-13

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: 71.18  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgEYIDQAQNRiQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd14183    12 RTIGDGNFAVVK--ECVERSTGR-EYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTEL-YLVMELVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNpTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLArDILDREYYSV 1242
Cdd:cd14183    88 GGDLFDAITSTNKY-TERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLA-TVVDGPLYTV 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1243 qqhrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd14183   166 -----CGTPT-YVAPEIIAETGYGLKVDIWAAGVITYILLC-GFPPFR 206
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1089-1282 4.19e-13

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 71.32  E-value: 4.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIdqaQNRIQCAIKSLSRIT--------------EMQQVEAFLREGLLMRGLNHPNVLALIGIMLPP 1154
Cdd:cd14077     9 IGAGSMGKVKLAKHI---RTGEKCAIKIIPRASnaglkkerekrlekEISRDIRTIREAALSSLLNHPHICRLRDFLRTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1155 EGLpHVLLPYMCHGDLLQFIRSpqRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArd 1233
Cdd:cd14077    86 NHY-YMLFEYVDGGQLLDYIIS--HGKLKEKQArKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1234 ildrEYYSVQQHRHARL-PVKWMALESLQTYRFT-TKSDVWSFGVLLWELL 1282
Cdd:cd14077   161 ----NLYDPRRLLRTFCgSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLV 207
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1087-1341 4.75e-13

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: 71.12  E-value: 4.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHgeyIDQAQNRIQCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLPy 1164
Cdd:cd14187    13 RFLGKGGFAKCYE---ITDADTKEVFAGKIVpkSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHG-FFEDNDFVYVVLE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldrEYYSVQQ 1244
Cdd:cd14187    88 LCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKV---EYDGERK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYrHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQC 1324
Cdd:cd14187   165 KTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV-GKPPF-ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKM 241
                         250
                  ....*....|....*..
gi 578806145 1325 WEADPAVRPTFRVLVGE 1341
Cdd:cd14187   242 LQTDPTARPTINELLND 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
1089-1334 4.78e-13

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: 71.60  E-value: 4.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNR---IQCAIKSLSRITEmQQVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYm 1165
Cdd:cd06644    20 LGDGAFGKVY------KAKNKetgALAAAKVIETKSE-EELEDYMVEIEILATCNHPYIVKLLGAFYW-DGKLWIMIEF- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGD-----LLQFIRSPQRnPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGL-ARDIldrey 1239
Cdd:cd06644    91 CPGGavdaiMLELDRGLTE-PQIQVICR---QMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVsAKNV----- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 ySVQQHRHARLPVK-WMA-----LESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYRHIDPFDLTHFLAQGR--RLPQPE 1311
Cdd:cd06644   162 -KTLQRRDSFIGTPyWMApevvmCETMKDTPYDYKADIWSLGITLIE-MAQIEPPHHELNPMRVLLKIAKSEppTLSQPS 239
                         250       260
                  ....*....|....*....|...
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd06644   240 KWSMEFRDFLKTALDKHPETRPS 262
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
1088-1334 4.91e-13

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 71.15  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVV----YHGEYIdqaqnriqcAIKSLSRITEmqqvEAFLREGLL--MRGLNHPNVLALIGI-MLPPEGLPHV 1160
Cdd:cd14056     2 TIGKGRYGEVwlgkYRGEKV---------AVKIFSSRDE----DSWFRETEIyqTVMLRHENILGFIAAdIKSTGSWTQL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LL--PYMCHGDLLQFIrspQRNP-TVKDLISFGLQVARGMEYL------AEQK--FVHRDLAARNCMLDESFTVKVADFG 1229
Cdd:cd14056    69 WLitEYHEHGSLYDYL---QRNTlDTEEALRLAYSAASGLAHLhteivgTQGKpaIAHRDLKSKNILVKRDGTCCIADLG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1230 LA-RDILDREYYSVQQHRHARlPVKWMALE----SLQTYRFTT--KSDVWSFGVLLWELLTRG---------APPYRHID 1293
Cdd:cd14056   146 LAvRYDSDTNTIDIPPNPRVG-TKRYMAPEvlddSINPKSFESfkMADIYSFGLVLWEIARRCeiggiaeeyQLPYFGMV 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1294 PFDLTH------FLAQGRRLPQPEY-----CPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14056   225 PSDPSFeemrkvVCVEKLRPPIPNRwksdpVLRSMVKLMQECWSENPHARLT 276
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
1084-1339 5.05e-13

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: 70.49  E-value: 5.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHGEyiDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGL-NHPNVLALI------GIMLppeg 1156
Cdd:cd13997     3 HELEQIGSGSFSEVFKVR--SKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYssweegGHLY---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1157 lphVLLPYMCHGDLLQFIRSPQRNPTVK--DLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdi 1234
Cdd:cd13997    77 ---IQMELCENGSLQDALEELSPISKLSeaEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 ldreyysvqqhrhARLPVKW---------MALESLQ-TYRFTTKSDVWSFGVLLWEL-----LTRGAPPYRHidpfdlth 1299
Cdd:cd13997   151 -------------TRLETSGdveegdsryLAPELLNeNYTHLPKADIFSLGVTVYEAatgepLPRNGQQWQQ-------- 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578806145 1300 fLAQGR--RLPQPEYcPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd13997   210 -LRQGKlpLPPGLVL-SQELTRLLKVMLDPDPTRRPTADQLL 249
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1087-1334 5.61e-13

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: 70.54  E-value: 5.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFG--VVYHgeyidQAQNRIQCAIK--SLSRITEMQQVEAfLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd08221     6 RVLGRGAFGeaVLYR-----KTEDNSLVVWKevNLSRLSEKERRDA-LNEIDILSLLNHDNIITYYNHFLDGESL-FIEM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSpQRNPTV--KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREYy 1240
Cdd:cd08221    79 EYCNGGNLHDKIAQ-QKNQLFpeEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISK-VLDSES- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 svqqhRHARLPVK---WMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSL 1317
Cdd:cd08221   156 -----SMAESIVGtpyYMSPELVQGVKYNFKSDIWAVGCVLYELLTL-KRTFDATNPLRLAVKIVQGEYEDIDEQYSEEI 229
                         250
                  ....*....|....*..
gi 578806145 1318 YQVMQQCWEADPAVRPT 1334
Cdd:cd08221   230 IQLVHDCLHQDPEDRPT 246
IPT smart00429
ig-like, plexins, transcription factors;
683-767 6.04e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 65.90  E-value: 6.04e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    683 EPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN--GTECLLARVSEGQLLCATPPGAT-VASVPLS-LQVGGAQV 758
Cdd:smart00429    1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGvgEAPCTFSPSSSTAIVCKTPPYHNiPGSVPVRtVGLRNGGV 80
                            90
                    ....*....|
gi 578806145    759 PGS-WTFQYR 767
Cdd:smart00429   81 PSSpQPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
684-768 6.54e-13

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 65.56  E-value: 6.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNG-TECLLARVSEGQLLCATPPGATVASVPLSLQVGGA---QVP 759
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGSNLRVTFGGgVPCSVLSVSSTAIVCTTPPYANPGPGPVEVTVDRGnggITS 80

                  ....*....
gi 578806145  760 GSWTFQYRE 768
Cdd:cd00102    81 SPLTFTYVP 89
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
1087-1337 6.95e-13

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: 70.97  E-value: 6.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQaqnriQCAIK--------SLSRITEMQQVeaflregLLMRglnHPNVLALIGIMLPPEG-- 1156
Cdd:cd14144     1 RSVGKGRYGEVWKGKWRGE-----KVAVKifftteeaSWFRETEIYQT-------VLMR---HENILGFIAADIKGTGsw 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1157 -LPHVLLPYMCHGDLLQFIRSPQRNPtvKDLISFGLQVARGMEYLAEQKF--------VHRDLAARNCMLDESFTVKVAD 1227
Cdd:cd14144    66 tQLYLITDYHENGSLYDFLRGNTLDT--QSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIAD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1228 FGLARDILDrEYYSVQQHRHARLPVK-WMALESL------QTYRFTTKSDVWSFGVLLWEL----LTRG-----APPYRH 1291
Cdd:cd14144   144 LGLAVKFIS-ETNEVDLPPNTRVGTKrYMAPEVLdeslnrNHFDAYKMADMYSFGLVLWEIarrcISGGiveeyQLPYYD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1292 IDPFDLTH------FLAQGRRLPQP-----EYCPDSLYQVMQQCWEADPAVRPT-FRV 1337
Cdd:cd14144   223 AVPSDPSYedmrrvVCVERRRPSIPnrwssDEVLRTMSKLMSECWAHNPAARLTaLRV 280
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
1089-1333 6.99e-13

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: 70.76  E-value: 6.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFG-VVYHGEY-----------IDQAQNRIQCA----IKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIML 1152
Cdd:cd14067     1 LGQGGSGtVIYRARYqgqpvavkrfhIKKCKKRTDGSadtmLKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1153 PPEGLPHVLLPYmchGDLLQFIRSPQRNPT---VKDLISFGL--QVARGMEYLAEQKFVHRDLAARNCML-----DESFT 1222
Cdd:cd14067    81 HPLCFALELAPL---GSLNTVLEENHKGSSfmpLGHMLTFKIayQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHIN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1223 VKVADFGLARdildreyysvQQHRHARLPVK----WMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHiDPFDLT 1298
Cdd:cd14067   158 IKLSDYGISR----------QSFHEGALGVEgtpgYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGH-HQLQIA 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578806145 1299 HFLAQGRR--LPQPE----YCPDSLyqvMQQCWEADPAVRP 1333
Cdd:cd14067   227 KKLSKGIRpvLGQPEevqfFRLQAL---MMECWDTKPEKRP 264
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
1085-1289 7.02e-13

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: 70.33  E-value: 7.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1085 SDRVIGKGHFGVVYHGEyidQAQNRIQCAIKSLsRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPHVLL-- 1162
Cdd:cd14193     8 KEEILGGGRFGQVHKCE---EKSSGLKLAAKII-KARSQKEKEEVKNEIEVMNQLNHANLIQLYDAF---ESRNDIVLvm 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN--CMLDESFTVKVADFGLARDILDREYY 1240
Cdd:cd14193    81 EYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENilCVSREANQVKIIDFGLARRYKPREKL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578806145 1241 SVqqhrHARLPvKWMALESLQtYRFTT-KSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14193   161 RV----NFGTP-EFLAPEVVN-YEFVSfPTDMWSLGVIAYMLLS-GLSPF 203
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
1088-1334 7.06e-13

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: 70.93  E-value: 7.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGeyidQAQNRIqCAIKslsrITEMQQVEAFLREGLLMR--GLNHPNVLALIGIMLPPEGLPHVLL--- 1162
Cdd:cd13998     2 VIGKGRFGEVWKA----SLKNEP-VAVK----IFSSRDKQSWFREKEIYRtpMLKHENILQFIAADERDTALRTELWlvt 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRspqRNP-TVKDLISFGLQVARGMEYLAEQKF---------VHRDLAARNCMLDESFTVKVADFGLA- 1231
Cdd:cd13998    73 AFHPNGSL*DYLS---LHTiDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKSKNILVKNDGTCCIADFGLAv 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 -----RDILDREyysvqqhRHARLPVK-WMALESL----QTYRFTT--KSDVWSFGVLLWELLTR-----GA-----PPY 1289
Cdd:cd13998   150 rlspsTGEEDNA-------NNGQVGTKrYMAPEVLegaiNLRDFESfkRVDIYAMGLVLWEMASRctdlfGIveeykPPF 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1290 RHIDPFDLT------HFLAQGRRLPQPEY---CPD--SLYQVMQQCWEADPAVRPT 1334
Cdd:cd13998   223 YSEVPNHPSfedmqeVVVRDKQRPNIPNRwlsHPGlqSLAETIEECWDHDAEARLT 278
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
1086-1289 7.18e-13

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 70.33  E-value: 7.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHG----EYIDQAQNRIQcaIKSLSRiTEMQQveaFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVL 1161
Cdd:cd13983     6 NEVLGRGSFKTVYRAfdteEGIEVAWNEIK--LRKLPK-AERQR---FKQEIEILKSLKHPNIIKFYDSWESKSKKEVIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCH-GDLLQFIRSPQRnPTVKDLISFGLQVARGMEYL--AEQKFVHRDLAARNCMLDESF-TVKVADFGLArdildr 1237
Cdd:cd13983    80 ITELMTsGTLKQYLKRFKR-LKLKVIKSWCRQILEGLNYLhtRDPPIIHRDLKCDNIFINGNTgEVKIGDLGLA------ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1238 eyySVQQHRHARLPV---KWMALEslqTY--RFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd13983   153 ---TLLRQSFAKSVIgtpEFMAPE---MYeeHYDEKVDIYAFGMCLLEMAT-GEYPY 202
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
1087-1290 9.50e-13

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: 70.71  E-value: 9.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidQAQNRIqCAIKSLS--RITEMQQVEAFLREG-LLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd05570     1 KVLGKGSFGKVMLAER--KKTDEL-YAIKVLKkeVIIEDDDVECTMTEKrVLALANRHPFLTGLHACFQTEDRLYFVM-E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIrspQRNptvkdlISFGLQVAR--------GMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR-DI 1234
Cdd:cd05570    77 YVNGGDLMFHI---QRA------RRFTEERARfyaaeiclALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKeGI 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1235 LDR----------EYysvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd05570   148 WGGnttstfcgtpDY---------------IAPEILREQDYGFSVDWWALGVLLYEMLA-GQSPFE 197
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
1089-1334 9.80e-13

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: 69.72  E-value: 9.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPYMC 1166
Cdd:cd14073     9 LGKGTYGKVKLAIERATGR---EVAIKSIkkDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVM-EYAS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLArdildrEYYSVQQhr 1246
Cdd:cd14073    85 GGELYDYISERRRLPE-REARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS------NLYSKDK-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1247 harlpvkwmaleSLQTY----------------RFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQGRRLPQP 1310
Cdd:cd14073   156 ------------LLQTFcgsplyaspeivngtpYQGPEVDCWSLGVLLYTLV-YGTMPFDGSDFKRLVKQISSGDYREPT 222
                         250       260
                  ....*....|....*....|....
gi 578806145 1311 EycPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14073   223 Q--PSDASGLIRWMLTVNPKRRAT 244
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
1087-1293 1.04e-12

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: 69.57  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgEYIDQAQNRIQcAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPy 1164
Cdd:cd14189     7 RLLGKGGFARCY--EMTDLATNKTY-AVKVIphSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENI-YIFLE- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildREYYSVQQ 1244
Cdd:cd14189    82 LCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAA----RLEPPEQR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1245 HRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHID 1293
Cdd:cd14189   158 KKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFETLD 205
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
1089-1312 1.15e-12

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 71.09  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRiQCAIKSLSRI--TEMQQVEAFlREGLLMRGLNHPNVLALIGIMLPPEGLP-----HVL 1161
Cdd:cd07879    23 VGSGAYGSVCSA--IDKRTGE-KVAIKKLSRPfqSEIFAKRAY-RELTLLKHMQHENVIGLLDVFTSAVSGDefqdfYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMcHGDLLQFIRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIlDRE--- 1238
Cdd:cd07879    99 MPYM-QTDLQKIMGHPLSEDKVQYLV---YQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHA-DAEmtg 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1239 YYSVQQHRHARLPVKWMaleslqtyRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFD-LTHFLaQGRRLPQPEY 1312
Cdd:cd07879   174 YVVTRWYRAPEVILNWM--------HYNQTVDIWSVGCIMAEMLT-GKTLFKGKDYLDqLTQIL-KVTGVPGPEF 238
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
1084-1291 1.28e-12

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


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 69.73  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHGEyidQAQNRIQCAIK-------SLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEG 1156
Cdd:cd14084     9 IMSRTLGSGACGEVKLAY---DKSTCKKVAIKiinkrkfTIGSRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1157 LpHVLLPYMCHGDLLQFIRSPQR--NPTVKdLISFglQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLA 1231
Cdd:cd14084    86 Y-YIVLELMEGGELFDRVVSNKRlkEAICK-LYFY--QMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1232 RDILDReyySVQQHRHArlPVKWMALESLQTYR---FTTKSDVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd14084   162 KILGET---SLMKTLCG--TPTYLAPEVLRSFGtegYTRAVDCWSLGVILFICLS-GYPPFSE 218
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
1113-1344 1.40e-12

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: 70.12  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1113 AIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYmCH---GDLLQFIRSPQRNP-TVK 1184
Cdd:cd14001    32 AVKKINSKCDKGQRSLYqerlKEEAKILKSLNHPNIVGFRAFTKSEDGSLCLAMEY-GGkslNDLIEERYEAGLGPfPAA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1185 DLISFGLQVARGMEYL-AEQKFVHRDLAARNCMLDESF-TVKVADFGLARDiLDrEYYSVQQHRHARL----PvkWMALE 1258
Cdd:cd14001   111 TILKVALSIARALEYLhNEKKILHGDIKSGNVLIKGDFeSVKLCDFGVSLP-LT-ENLEVDSDPKAQYvgteP--WKAKE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1259 SL-QTYRFTTKSDVWSFGVLLWELLTRGAPpyrHIDPFDLTHF--------------LAQGRRLPQPE---YCPDSLYQV 1320
Cdd:cd14001   187 ALeEGGVITDKADIFAYGLVLWEMMTLSVP---HLNLLDIEDDdedesfdedeedeeAYYGTLGTRPAlnlGELDDSYQK 263
                         250       260
                  ....*....|....*....|....*...
gi 578806145 1321 MQQ----CWEADPAVRPTFRVLVGEVEQ 1344
Cdd:cd14001   264 VIElfyaCTQEDPKDRPSAAHIVEALEA 291
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
1089-1370 1.46e-12

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: 70.06  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYH-------GEYIDQAQNRIQCAIKS--LSRITEMqqveAFLREgllMRGLNHPNVLALIGI--------- 1150
Cdd:cd07862     9 IGEGAYGKVFKardlkngGRFVALKRVRVQTGEEGmpLSTIREV----AVLRH---LETFEHPNVVRLFDVctvsrtdre 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1151 ---MLPPEGLPHVLLPYmchgdlLQFIRSPQRNP-TVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVA 1226
Cdd:cd07862    82 tklTLVFEHVDQDLTTY------LDKVPEPGVPTeTIKDMM---FQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1227 DFGLARdildreYYSVQQHRHARLPVKWM-ALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGR 1305
Cdd:cd07862   153 DFGLAR------IYSFQMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAEMFRR-KPLFRGSSDVDQLGKILDVI 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1306 RLPQPEYCPDSLyQVMQQCWEADPAvRPTFRvLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSH 1370
Cdd:cd07862   226 GLPGEEDWPRDV-ALPRQAFHSKSA-QPIEK-FVTDIDELGKDLLLKCLTFNPAKRISAYSALSH 287
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
1089-1289 1.52e-12

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: 69.18  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYidQAQNRIQcAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd05572     1 LGVGGFGRVELVQL--KSKGRTF-ALKCVKKrhIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYL-YMLMEYCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRspqrnptvkDLISFGLQVAR--------GMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR- 1237
Cdd:cd05572    77 GGELWTILR---------DRGLFDEYTARfytacvvlAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGr 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1238 ---------EYysvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05572   148 ktwtfcgtpEY---------------VAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPF 192
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
1128-1342 1.70e-12

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


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 69.19  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1128 AFLREGLLMRGLNHPNVLALIGIMLppEGLPHVLLP-YMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFV 1206
Cdd:cd05077    54 AFFETASMMRQVSHKHIVLLYGVCV--RDVENIMVEeFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1207 HRDLAARNCML-------DESFTVKVADFGLARDILDReyysvqQHRHARLPvkWMALESLQTYR-FTTKSDVWSFGVLL 1278
Cdd:cd05077   132 HGNVCTKNILLaregidgECGPFIKLSDPGIPITVLSR------QECVERIP--WIAPECVEDSKnLSIAADKWSFGTTL 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1279 WELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEyCpDSLYQVMQQCWEADPAVRPTFRVLVGEV 1342
Cdd:cd05077   204 WEICYNGEIPLKDKTLAEKERFYEGQCMLVTPS-C-KELADLMTHCMNYDPNQRPFFRAIMRDI 265
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
1087-1289 1.71e-12

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 70.39  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRIqCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd05573     7 KVIGRGAFGEVWLVR--DKDTGQV-YAMKILRKsdMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHL-YLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQF-IRSPQ-RNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL---DREY 1239
Cdd:cd05573    83 MPGGDLMNLlIKYDVfPEETARFYIA---ELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNksgDRES 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1240 YSVQQH-------------------RHARLPV---KWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05573   160 YLNDSVntlfqdnvlarrrphkqrrVRAYSAVgtpDYIAPEVLRGTGYGPECDWWSLGVILYEMLY-GFPPF 230
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1088-1338 1.78e-12

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: 69.38  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYhgeyidQAQNR---IQCAIKSLS--RITEMQQ---VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpH 1159
Cdd:cd06630     7 LLGTGAFSSCY------QARDVktgTLMAVKQVSfcRNSSSEQeevVEAIREEIRMMARLNHPNIVRMLGATQHKSHF-N 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRS--PQRNPTVkdlISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFT-VKVADFGLArdild 1236
Cdd:cd06630    80 IFVEWMAGGSVASLLSKygAFSENVI---INYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAA----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 reyysvqqhrhARLPVK----------------WMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY---RHIDPFDL 1297
Cdd:cd06630   152 -----------ARLASKgtgagefqgqllgtiaFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPWnaeKISNHLAL 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578806145 1298 THFLAQGRRLPQ-PEYCPDSLYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06630   220 IFKIASATTPPPiPEHLSPGLRDVTLRCLELQPEDRPPAREL 261
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
1089-1279 1.95e-12

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: 69.61  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVyhgEYIDQAQNRIQCAIKSLSRITEMQQ-------------------------VEAFLREGLLMRGLNHPN 1143
Cdd:cd14199    10 IGKGSYGVV---KLAYNEDDNTYYAMKVLSKKKLMRQagfprrppprgaraapegctqprgpIERVYQEIAILKKLDHPN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1144 VLALIGIML-PPEGLPHVLLPYMCHGDLLQFirsPQRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCMLDESF 1221
Cdd:cd14199    87 VVKLVEVLDdPSEDHLYMVFELVKQGPVMEV---PTLKPLSEDQARFYFQdLIKGIEYLHYQKIIHRDVKPSNLLVGEDG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1222 TVKVADFGLARDILDREYYSVQQhrhARLPVkWMALESLQTYR--FTTKS-DVWSFGVLLW 1279
Cdd:cd14199   164 HIKIADFGVSNEFEGSDALLTNT---VGTPA-FMAPETLSETRkiFSGKAlDVWAMGVTLY 220
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
1089-1291 2.22e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 69.27  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeYIDQAQNRIQCAIKSLSRitEMQQ------VEAFLREGLLMRGLNHPNVLALIGIM-LPPEGLPHVL 1161
Cdd:cd13990     8 LGKGGFSEVYKA-FDLVEQRYVACKIHQLNK--DWSEekkqnyIKHALREYEIHKSLDHPRIVKLYDVFeIDTDSFCTVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 lpYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQK--FVHRDLAARNCMLDESFT---VKVADFGLARdILD 1236
Cdd:cd13990    85 --EYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDFGLSK-IMD 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1237 REYYSVQQhrharlpvkwMALESlQ---TY---------------RFTTKSDVWSFGVLLWELLtRGAPPYRH 1291
Cdd:cd13990   162 DESYNSDG----------MELTS-QgagTYwylppecfvvgktppKISSKVDVWSVGVIFYQML-YGRKPFGH 222
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
1087-1283 2.39e-12

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: 68.90  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyidQAQNRIQCAIKSLSRITEMQQ-VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd14069     7 QTLGEGAFGEVFLAV---NRNTEEAVAVKFVDMKRAPGDcPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQ-YLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIrSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQH 1245
Cdd:cd14069    83 SGGELFDKI-EPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERLLNK 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578806145 1246 RHARLPvkWMALESLQTYRF-TTKSDVWSFGVLLWELLT 1283
Cdd:cd14069   162 MCGTLP--YVAPELLAKKKYrAEPVDVWSCGIVLFAMLA 198
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
1130-1339 3.48e-12

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: 68.62  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1130 LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIR-SPQRNPTVKDLISFGlqVARGMEYLAEQ-KFVH 1207
Cdd:cd06620    51 LRELQILHECHSPYIVSFYGAFLNENNNIIICMEYMDCGSLDKILKkKGPFPEEVLGKIAVA--VLEGLTYLYNVhRIIH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1208 RDLAARNCMLDESFTVKVADFGLARDILDreyySVqqhrhARLPV---KWMALESLQTYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd06620   129 RDIKPSNILVNSKGQIKLCDFGVSGELIN----SI-----ADTFVgtsTYMSPERIQGGKYSVKSDVWSLGLSIIELALG 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1285 GAPPYRHIDP----------FDLTHFLAQ--GRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd06620   200 EFPFAGSNDDddgyngpmgiLDLLQRIVNepPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLL 266
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
1087-1289 3.61e-12

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: 68.28  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNR--IQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLL 1162
Cdd:cd14076     7 RTLGEGEFGKVKLGWPLPKANHRsgVQVAIKLIRRdtQQENCQTSKIMREINILKGLTHPNIVRLLD-VLKTKKYIGIVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIrspQRNPTVKDLISFGL--QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--DILDRE 1238
Cdd:cd14076    86 EFVSGGELFDYI---LARRRLKDSVACRLfaQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANtfDHFNGD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1239 YYSVQQHRHARLPVKWMALESLQTYRfttKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14076   163 LMSTSCGSPCYAAPELVVSDSMYAGR---KADIWSCGVILYAMLA-GYLPF 209
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1089-1295 3.97e-12

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: 68.63  E-value: 3.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVV---YH---GEYIdqaqnriqcAIKSLSRITEM--QQVEAFLREGLLMRGLNHPNVLAliGIMLPPE----- 1155
Cdd:cd13989     1 LGSGGFGYVtlwKHqdtGEYV---------AIKKCRQELSPsdKNRERWCLEVQIMKKLNHPNVVS--ARDVPPElekls 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 --GLPHVLLPYMCHGDLLQFIRSPQRNPTVK--DLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDES---FTVKVADF 1228
Cdd:cd13989    70 pnDLPLLAMEYCSGGDLRKVLNQPENCCGLKesEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGggrVIYKLIDL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1229 GLARDiLDreyysvQQHRHARL--PVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPF 1295
Cdd:cd13989   150 GYAKE-LD------QGSLCTSFvgTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQPV 211
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
1089-1283 4.42e-12

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 68.70  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNR-IQCAIKSLSRITEMQQV---EAFLREGLLMRGLNHPNVLALIGIMLPPEG--LPHVLL 1162
Cdd:cd14159     1 IGEGGFGCVY------QAVMRnTEYAVKRLKEDSELDWSvvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNycLIYVYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PymcHGDLLQFIRSPQRNP--TVKDLISFGLQVARGMEYLAEQK--FVHRDLAARNCMLDESFTVKVADFGLARdiLDR- 1237
Cdd:cd14159    75 P---NGSLEDRLHCQVSCPclSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLAR--FSRr 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1238 -----EYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:cd14159   150 pkqpgMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT 200
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
1089-1296 4.56e-12

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: 67.73  E-value: 4.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGvvyhgeYIDQAQNRI---QCAIKSLSRITEMQQveAFLREGLLMRGLN-HPNVLALIGIMLPPEGLPHVLLPY 1164
Cdd:cd13987     1 LGEGTYG------KVLLAVHKGsgtKMALKFVPKPSTKLK--DFLREYNISLELSvHPHIIKTYDVAFETEDYYVFAQEY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIrSPQR---NPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCML-DESFT-VKVADFGLARDILDREY 1239
Cdd:cd13987    73 APYGDLFSII-PPQVglpEERVKRCAA---QLASALDFMHSKNLVHRDIKPENVLLfDKDCRrVKLCDFGLTRRVGSTVK 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1240 YsvqqhRHARLPvkWMALESLQT-----YRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFD 1296
Cdd:cd13987   149 R-----VSGTIP--YTAPEVCEAkknegFVVDPSIDVWAFGVLLFCCLT-GNFPWEKADSDD 202
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1087-1306 4.65e-12

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 68.06  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyidQAQNRIQCAIKSLSRIT-EMQQVEAFLR-EGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd14116    11 RPLGKGKFGNVYLAR---EKQSKFILALKVLFKAQlEKAGVEHQLRrEVEIQSHLRHPNILRLYGYFHDATRV-YLILEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLqfiRSPQRNPTVKDLIS--FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGlardildreyYSV 1242
Cdd:cd14116    87 APLGTVY---RELQKLSKFDEQRTatYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG----------WSV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1243 Q--QHRHARL--PVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPP---------YRHIDPFDLTH--FLAQGRR 1306
Cdd:cd14116   154 HapSSRRTTLcgTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV-GKPPfeantyqetYKRISRVEFTFpdFVTEGAR 231
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
1087-1284 4.95e-12

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: 68.87  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVV---YHGeyidqaQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPP--EGLPHVL 1161
Cdd:cd07849    11 SYIGEGAYGMVcsaVHK------PTGQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPtfESFKDVY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 L--PYMcHGDLLQFIRSpqrNPTVKDLIS-FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldre 1238
Cdd:cd07849    85 IvqELM-ETDLYKLIKT---QHLSNDHIQyFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIA---- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1239 yysVQQHRHARLPVKWMAL------ESLQTYRFTTKS-DVWSFGVLLWELLTR 1284
Cdd:cd07849   157 ---DPEHDHTGFLTEYVATrwyrapEIMLNSKGYTKAiDIWSVGCILAEMLSN 206
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
1089-1282 4.96e-12

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: 68.57  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyidqaQNRIQCAIKSLsRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPY 1164
Cdd:cd07869    13 LGEGSYATVYKG------KSKVNGKLVAL-KVIRLQEEEGTpftaIREASLLKGLKHANIVLLHDIIHTKETL--TLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreYYSVQQ 1244
Cdd:cd07869    84 YVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR------AKSVPS 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578806145 1245 HRHARLPVK-WMALES--LQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:cd07869   158 HTYSNEVVTlWYRPPDvlLGSTEYSTCLDMWGVGCIFVEMI 198
Sema_plexin_B1 cd11275
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the ...
64-522 6.27e-12

The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200536 [Multi-domain]  Cd Length: 461  Bit Score: 69.60  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDP-GCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGR 142
Cdd:cd11275    14 DPESGTLYLGATNFLFQLTPDLLLENMVQTGPVLDSkDCLPPVSKLECPQAQHTNNHNKLLLVNPVQKELIVCGSVHQGI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  143 CFLHDLepqGTAVHLaapacLFSAHhnRPDDCPDCVAS-PLGTRVTVVEQGQAS---YFYVASSLDAAVAASFSPrsVSI 218
Cdd:cd11275    94 CEKRRL---GSIDHV-----LFRPE--RPGDTQYVAANdPNVTTVGLVAYSKDGvplLFVGRGYTSRGVGGGIPP--ITT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  219 RRLKADASGFAPGFVALS------VLPKHLVSYSIEYVHSFHTGAFVYFLTVQpASVTDDPSALHTRLARLSATEPELGD 292
Cdd:cd11275   162 RNLRAHGDDATDSHSIFSyeetakLAVGRLSEYNHHFIKAFTYGSSVYFLFYR-RDLKSQSREYKTYISRICLDDSHYYS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  293 YRELVLDCRFAPKRrrrgapeggqpYPVLRVAHSAPVGAQLATELSIAEGqEVLFGVFVTGKDGGPGVGPNSVVCAFPID 372
Cdd:cd11275   241 YVELPLLCQSKANT-----------YSLLQAAYVTQPGERLAQGQLDTDG-EVLFAAFSAWQASSGKLSEESALCAYPMD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  373 LLDTLIDEGVERCC--ESPVHPGLRRGLDFFQSPSFCPNPPG--LEAL------SPNTSCRHFPLLVSSSFSRVDlfngl 442
Cdd:cd11275   309 EVDRLTNWTRDVCYtrDGKAEDGTEVAYIEYDVSSNCVQLPAdtLDAYpcgsdhTPSPMASRVPLEATPLLEWTE----- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  443 lgpVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGqpVQRDV--SRLGDHLLFASGDQVFQV 520
Cdd:cd11275   384 ---IRLTAVAVNVEDGHTIAFLGDSRGRLHKVYLGAGGDAHTYSSQSIQQNSA--VSGDLlfDQLQEHLYVMTQSTVLKV 458

                  ..
gi 578806145  521 PI 522
Cdd:cd11275   459 PI 460
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1089-1334 6.61e-12

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: 67.53  E-value: 6.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFG---VVYHGEyidqaqNRIQCAIK--SLSRITEMQQVEAfLREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLP 1163
Cdd:cd08218     8 IGEGSFGkalLVKSKE------DGKQYVIKeiNISKMSPKEREES-RKEVAVLSKMKHPNIVQYQE-SFEENGNLYIVMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDReyySV 1242
Cdd:cd08218    80 YCDGGDLYKRINAQRGVLFPEDQIlDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIAR-VLNS---TV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrgappYRHidPFD------LTHFLAQGRRLPQPEYCPDS 1316
Cdd:cd08218   156 ELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCT-----LKH--AFEagnmknLVLKIIRGSYPPVPSRYSYD 228
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd08218   229 LRSLVSQLFKRNPRDRPS 246
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1087-1334 6.66e-12

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: 67.98  E-value: 6.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYI----DQAQNRIQCAIKSLSRitemqqvEAFLREGLLMRGLNHPNVLALIGIML--PPEGLP-- 1158
Cdd:cd14048    12 QCLGRGGFGVVFEAKNKvddcNYAVKRIRLPNNELAR-------EKVLREVRALAKLDHPGIVRYFNAWLerPPEGWQek 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 ------HVLLPYMCHGDLLQFIRspqRNPTVKD-----LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVAD 1227
Cdd:cd14048    85 mdevylYIQMQLCRKENLKDWMN---RRCTMESrelfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1228 FGLARDI-LDREYYSVQQ-----HRHA-RLPVK-WMALESLQTYRFTTKSDVWSFGVLLWELLtrgappYRHIDPFDLTH 1299
Cdd:cd14048   162 FGLVTAMdQGEPEQTVLTpmpayAKHTgQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELI------YSFSTQMERIR 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578806145 1300 FLAQGRRLPQP----EYCPDSlYQVMQQCWEADPAVRPT 1334
Cdd:cd14048   236 TLTDVRKLKFPalftNKYPEE-RDMVQQMLSPSPSERPE 273
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
1087-1339 7.04e-12

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: 67.41  E-value: 7.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVV----YHGE-------YIDQAQNRIQCAIKS--LSRITEMQQVEAFLREGllmrglNHPNVLALIGImLP 1153
Cdd:cd14004     6 KEMGEGAYGQVnlaiYKSKgkevvikFIFKERILVDTWVRDrkLGTVPLEIHILDTLNKR------SHPNIVKLLDF-FE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1154 PEGLPHVLLPymCHG---DLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGL 1230
Cdd:cd14004    79 DDEFYYLVME--KHGsgmDLFDFIER-KPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 ARDILDREYYSVqqhrhaRLPVKWMALESLQTYRFTTKS-DVWSFGVLLWELLTRGAPPYrhidpfDLTHFLAQGRRLPQ 1309
Cdd:cd14004   156 AAYIKSGPFDTF------VGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLVFKENPFY------NIEEILEADLRIPY 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 578806145 1310 PEYcpDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd14004   224 AVS--EDLIDLISRMLNRDVGDRPTIEELL 251
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
1089-1290 7.08e-12

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: 67.89  E-value: 7.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyidqaQNRIQCAIKSLSRI---TEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPYM 1165
Cdd:cd07836     8 LGEGTYATVYKG------RNRTTGEIVALKEIhldAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKL--MLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFI-----RSPQRNPTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyy 1240
Cdd:cd07836    80 MDKDLKKYMdthgvRGALDPNTVK---SFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF------ 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1241 svqqhrhaRLPVKWMALESLQT-YR----------FTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd07836   151 --------GIPVNTFSNEVVTLwYRapdvllgsrtYSTSIDIWSVGCIMAEMIT-GRPLFP 202
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1086-1289 8.14e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.82  E-value: 8.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEyiDQAQNRIQcAIKSLSriTEMQQ----VEAFLREGLLMRGLNHPNVLAligimlppeglphVL 1161
Cdd:NF033483   12 GERIGRGGMAEVYLAK--DTRLDRDV-AVKVLR--PDLARdpefVARFRREAQSAASLSHPNIVS-------------VY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 -------LPYMC----HG-DLLQFIRSpqRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADF 1228
Cdd:NF033483   74 dvgedggIPYIVmeyvDGrTLKDYIRE--HGPlSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1229 GLAR-----------DILDreyySVQ-----QHRHArlpvkwMAleslqtyrfTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:NF033483  152 GIARalssttmtqtnSVLG----TVHylspeQARGG------TV---------DARSDIYSLGIVLYEMLT-GRPPF 208
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1087-1312 9.42e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 68.03  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEM--QQVEAFLREG-LLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd05619    11 KMLGKGSFGKVFLAELKGTNQ---FFAIKALKKDVVLmdDDVECTMVEKrVLSLAWEHPFLTHLFCTFQTKENLFFVM-E 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLIsFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysVQ 1243
Cdd:cd05619    87 YLNGGDLMFHIQSCHKFDLPRATF-YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGD---AK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1244 QHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLaqgrRLPQPEY 1312
Cdd:cd05619   163 TSTFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEMLI-GQSPFHGQDEEELFQSI----RMDNPFY 225
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
1187-1347 1.06e-11

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 67.22  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1187 ISFGLQVARGMEYLAEQKF-VHRDLAARNCMLDESFTVKVADFGlARDILDreyysvqqhrharlPVK--WMALESLQTY 1263
Cdd:cd14044   112 ISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFG-CNSILP--------------PSKdlWTAPEHLRQA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1264 RFTTKSDVWSFGVLLWELLTRGAPPY-RHIDPFDLTHFLAQGRRLPQPeYCPD-----------SLYQVMQQCWEADPAV 1331
Cdd:cd14044   177 GTSQKGDVYSYGIIAQEIILRKETFYtAACSDRKEKIYRVQNPKGMKP-FRPDlnlesagererEVYGLVKNCWEEDPEK 255
                         170
                  ....*....|....*.
gi 578806145 1332 RPTFRVLVGEVEQIVS 1347
Cdd:cd14044   256 RPDFKKIENTLAKIFS 271
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
1087-1332 1.09e-11

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: 67.66  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEM--QQVEAFLREG-LLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGE---YFAVKALKKDVVLidDDVECTMVEKrVLALAWENPFLTHLYCTFQTKEHLFFVM-E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLIsFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdreYYSVQ 1243
Cdd:cd05620    77 FLNGGDLMFHIQDKGRFDLYRATF-YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENV---FGDNR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYrHIDPFDLthfLAQGRRLPQPEYcPDSLYQ---- 1319
Cdd:cd05620   153 ASTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEMLI-GQSPF-HGDDEDE---LFESIRVDTPHY-PRWITKeskd 225
                         250
                  ....*....|...
gi 578806145 1320 VMQQCWEADPAVR 1332
Cdd:cd05620   226 ILEKLFERDPTRR 238
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1088-1334 1.14e-11

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 67.34  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEyiDQAQNRIqCAIKSLSRITEMQQV-EAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYmC 1166
Cdd:cd07833     8 VVGEGAYGVVLKCR--NKATGEI-VAIKKFKESEDDEDVkKTALREVKVLRQLRHENIVNLKEAFRR-KGRLYLVFEY-V 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFI-RSPQRNP--TVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR------ 1237
Cdd:cd07833    83 ERTLLELLeASPGGLPpdAVRSYI---WQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARpasplt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 EYYSVQQHRHARLpvkwmaLESLQTYRFTTksDVWSFGVLLWELLTrGAP---------------------PYRHIDPFD 1296
Cdd:cd07833   160 DYVATRWYRAPEL------LVGDTNYGKPV--DVWAIGCIMAELLD-GEPlfpgdsdidqlyliqkclgplPPSHQELFS 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1297 LTHFLAqGRRLPQPEY-----------CPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd07833   231 SNPRFA-GVAFPEPSQpeslerrypgkVSSPALDFLKACLRMDPKERLT 278
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1089-1333 1.21e-11

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: 66.76  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIqcAIKSLS------RITEM---QQVEAFLREGLLMR-GLNHPNVL----------ALI 1148
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNGQTLL--ALKEINmtnpafGRTEQerdKSVGDIISEVNIIKeQLRHPNIVryyktflendRLY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1149 GIMLPPEGLPHvllpymchGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYL-AEQKFVHRDLAARNCMLDESFTVKVAD 1227
Cdd:cd08528    86 IVMELIEGAPL--------GEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKVTITD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1228 FGLARDILDREYY--SVQQHRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGR 1305
Cdd:cd08528   158 FGLAKQKGPESSKmtSVVGTILYSCP------EIVQNEPYGEKADIWALGCILYQMCTL-QPPFYSTNMLTLATKIVEAE 230
                         250       260
                  ....*....|....*....|....*....
gi 578806145 1306 RLPQPEYC-PDSLYQVMQQCWEADPAVRP 1333
Cdd:cd08528   231 YEPLPEGMySDDITFVIRSCLTPDPEARP 259
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
1087-1339 1.44e-11

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 66.59  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQ----VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLP-HVL 1161
Cdd:cd06653     8 KLLGRGAFGEVYLCYDADTGR---ELAVKQVPFDPDSQEtskeVNALECEIQLLKNLRHDRIVQYYGCLRDPEEKKlSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHG---DLLQFIRSPQRNPTVKdlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIlDRE 1238
Cdd:cd06653    85 VEYMPGGsvkDQLKAYGALTENVTRR----YTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRI-QTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRRLPQ-PEYCPDSL 1317
Cdd:cd06653   160 CMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTE-KPPWAEYEAMAAIFKIATQPTKPQlPDGVSDAC 238
                         250       260
                  ....*....|....*....|..
gi 578806145 1318 YQVMQQCWeADPAVRPTFRVLV 1339
Cdd:cd06653   239 RDFLRQIF-VEEKRRPTAEFLL 259
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
1089-1295 1.45e-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: 67.60  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPP-EGLphVLLPYMCH 1167
Cdd:cd07856    18 VGMGAFGLVCSAR--DQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPlEDI--YFVTELLG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpqrNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdILDREYYSVQQHR 1246
Cdd:cd07856    94 TDLHRLLTS---RPLEKQFIQYFLyQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR-IQDPQMTGYVSTR 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1247 HARLPvkwmalESLQTYR-FTTKSDVWSFGVLLWELLtRGAPPY---RHIDPF 1295
Cdd:cd07856   170 YYRAP------EIMLTWQkYDVEVDIWSAGCIFAEML-EGKPLFpgkDHVNQF 215
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
1089-1284 1.45e-11

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: 66.93  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd07835     7 IGEGTYGVVY------KARDKLTGEIVALKKIRLETEDEGVpstaIREISLLKELNHPNIVRLLDVVHSENKL-YLVFEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 McHGDLLQFIRSPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--DILDREYys 1241
Cdd:cd07835    80 L-DLDLKKYMDSSPLTGLDPPLIkSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARafGVPVRTY-- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1242 vqqhRHARLPVKWMALESLQTYR-FTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07835   157 ----THEVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTR 196
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
1089-1284 1.55e-11

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 67.01  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPeGLPH----- 1159
Cdd:cd07865    20 IGQGTFGEVF------KARHRKTGQIVALKKVLMENEKEGFpitaLREIKILQLLKHENVVNLIEICRTK-ATPYnrykg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 --VLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR 1237
Cdd:cd07865    93 siYLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSLA 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 EyySVQQHRHA-RLPVKWM-ALESLQTYR-FTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07865   173 K--NSQPNRYTnRVVTLWYrPPELLLGERdYGPPIDMWGAGCIMAEMWTR 220
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
1084-1289 1.58e-11

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: 66.48  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHgeyIDQAQNRIQCAIKSLSRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLP 1163
Cdd:cd14190     7 HSKEVLGGGKFGKVHT---CTEKRTGLKLAAKVINKQNSKDK-EMVLLEIQVMNQLNHRNLIQLYEAIETPNEIV-LFME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN--CMLDESFTVKVADFGLARDILDREYYS 1241
Cdd:cd14190    82 YVEGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENilCVNRTGHQVKIIDFGLARRYNPREKLK 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1242 VqqhrHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14190   162 V----NFGTP-EFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPF 203
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
1089-1282 1.81e-11

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: 66.10  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRiQCAIKSLsRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVL-LPYMCH 1167
Cdd:cd14103     1 LGRGKFGTVY--RCVEKATGK-ELAAKFI-KCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREM--VLvMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN--CMLDESFTVKVADFGLARDILDREyysvqqh 1245
Cdd:cd14103    75 GELFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENilCVSRTGNQIKIIDFGLARKYDPDK------- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578806145 1246 rhaRLPVKW-----MALESLQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:cd14103   148 ---KLKVLFgtpefVAPEVVNYEPISYATDMWSVGVICYVLL 186
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
1089-1289 1.97e-11

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: 66.55  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRiQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06659    29 IGEGSTGVVCIAR--EKHSGR-QVAVKMMD-LRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEEL-WVLMEYLQGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyySVQQHRHA 1248
Cdd:cd06659   104 ALTDIVSQTRLNEEQIATVC--EAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK----DVPKRKSL 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd06659   178 VGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPY 217
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1089-1289 2.08e-11

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: 66.69  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIqcAIKSL------SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd14096     9 IGEGAFSNVYKAVPLRNTGKPV--AIKVVrkadlsSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYY-YIVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLlqFIRSPQRNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCM----------------------LDE 1219
Cdd:cd14096    86 ELADGGEI--FHQIVRLTYFSEDLSRHVItQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkadddetkVDE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1220 S-FT----------VKVADFGLARDILDreyysvqqhRHARLP---VKWMALESLQTYRFTTKSDVWSFGVLLWELLTrG 1285
Cdd:cd14096   164 GeFIpgvggggigiVKLADFGLSKQVWD---------SNTKTPcgtVGYTAPEVVKDERYSKKVDMWALGCVLYTLLC-G 233

                  ....
gi 578806145 1286 APPY 1289
Cdd:cd14096   234 FPPF 237
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
1087-1289 2.49e-11

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: 66.66  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRIT--EMQQVEAFLREGLLMRgLNHPNVLALiGIMLPPEGLPHVLLPY 1164
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATlkVRDRVRTKMERDILAD-VNHPFIVKL-HYAFQTEGKLYLILDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLlqFIR-SPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE--YYS 1241
Cdd:cd05582    79 LRGGDL--FTRlSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEkkAYS 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1242 VQQhrharlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05582   157 FCG------TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPF 197
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
1089-1336 2.68e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 66.01  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLS--RITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPYMC 1166
Cdd:cd05577     1 LGRGGFGEVCACQVKATGK---MYACKKLDkkRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVL-TLMN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRS-PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyySVQQH 1245
Cdd:cd05577    77 GGDLKYHIYNvGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEF------KGGKK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARL-PVKWMALESLQTYR-FTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTHFLAQgRRLPQPEYCPDS----LYQ 1319
Cdd:cd05577   151 IKGRVgTHGYMAPEVLQKEVaYDFSVDWFALGCMLYEMI-AGRSPFRQRKEKVDKEELKR-RTLEMAVEYPDSfspeARS 228
                         250
                  ....*....|....*..
gi 578806145 1320 VMQQCWEADPAVRPTFR 1336
Cdd:cd05577   229 LCEGLLQKDPERRLGCR 245
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
1089-1282 3.33e-11

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: 65.46  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeYIDQAQNRIqcAIKSLSRITEMQQVeAFLREGLLMRG-----------------------LNHPNVL 1145
Cdd:cd14118     2 IGKGSYGIVKLA-YNEEDNTLY--AMKILSKKKLLKQA-GFFRRPPPRRKpgalgkpldpldrvyreiailkkLDHPNVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1146 ALIGIMLPP-EGLPHVLLPYMCHGDLLqfiRSPQRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCMLDESFTV 1223
Cdd:cd14118    78 KLVEVLDDPnEDNLYMVFELVDKGAVM---EVPTDNPLSEETARSYFRdIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1224 KVADFGLARDIL-DREYYSVQQHRHArlpvkWMALESLQTYR--FTTKS-DVWSFGVLLWELL 1282
Cdd:cd14118   155 KIADFGVSNEFEgDDALLSSTAGTPA-----FMAPEALSESRkkFSGKAlDIWAMGVTLYCFV 212
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1087-1335 3.73e-11

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 65.45  E-value: 3.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQ----AQNRIQCAIKSLSRITEMQQVEAflrEGLLMRGLNHPNVLALIGIML-PPEGLPHVL 1161
Cdd:cd06652     8 KLLGQGAFGRVYLCYDADTgrelAVKQVQFDPESPETSKEVNALEC---EIQLLKNLLHERIVQYYGCLRdPQERTLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHG---DLLQFIRSPQRNPTVKdlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE 1238
Cdd:cd06652    85 MEYMPGGsikDQLKSYGALTENVTRK----YTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYSVQQHRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDPFDLTHFLAQGRRLPQ-----PEYC 1313
Cdd:cd06652   161 LSGTGMKSVTGTPY-WMSPEVISGEGYGRKADIWSVGCTVVEMLTE-KPPWAEFEAMAAIFKIATQPTNPQlpahvSDHC 238
                         250       260
                  ....*....|....*....|....*
gi 578806145 1314 PDSLYQVM---QQCWEADPAVRPTF 1335
Cdd:cd06652   239 RDFLKRIFveaKLRPSADELLRHTF 263
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1089-1287 3.81e-11

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 64.94  E-value: 3.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRIQCAikslsRIT--EMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPYMC 1166
Cdd:cd14110    11 INRGRFSVVRQCE--EKRSGQMLAA-----KIIpyKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHL--VLIEELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HG-DLLQFI--RSPQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQ 1243
Cdd:cd14110    82 SGpELLYNLaeRNSYSEAEVTDYLW---QILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTD 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1244 QHRHARLPvkwMALESLQTYRFTTKSDVWSFGVLLWELLTRGAP 1287
Cdd:cd14110   159 KKGDYVET---MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYP 199
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
1088-1289 3.94e-11

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: 64.98  E-value: 3.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQNRIQCAIKslsrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMCH 1167
Cdd:cd14192    11 VLGGGRFGQVHKCTELSTGLTLAAKIIK----VKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLT-LIMEYVDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN--CMLDESFTVKVADFGLARDILDREyysvqqh 1245
Cdd:cd14192    86 GELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENilCVNSTGNQIKIIDFGLARRYKPRE------- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1246 rhaRLPVKWMALESLQ----TYRFTT-KSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14192   159 ---KLKVNFGTPEFLApevvNYDFVSfPTDMWSVGVITYMLLS-GLSPF 203
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
1087-1348 4.23e-11

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: 65.22  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRiQCAIKSLSRiTEMQQVEAFLREGLLMRGLN-HPNVLALIGIM-LPPE-----GLPH 1159
Cdd:cd14036     6 RVIAEGGFAFVYEAQ--DVGTGK-EYALKRLLS-NEEEKNKAIIQEINFMKKLSgHPNIVQFCSAAsIGKEesdqgQAEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRS-PQRNPTVKD-LISFGLQVARGMEYLAEQK--FVHRDLAARNCMLDESFTVKVADFGLARDIL 1235
Cdd:cd14036    82 LLLTELCKGQLVDFVKKvEAPGPFSPDtVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 DREYYSVQQHRHARL---------PVkWMALESLQTYR---FTTKSDVWSFGVLLWELLTRgappyRHidPFDLTHFLA- 1302
Cdd:cd14036   162 HYPDYSWSAQKRSLVedeitrnttPM-YRTPEMIDLYSnypIGEKQDIWALGCILYLLCFR-----KH--PFEDGAKLRi 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1303 --QGRRLPQpeycPDSLYQVMQQ----CWEADPAVRPTFRVLVGEVEQIVSA 1348
Cdd:cd14036   234 inAKYTIPP----NDTQYTVFHDlirsTLKVNPEERLSITEIVEQLQELAAA 281
Sema_plexin_B3 cd11277
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
64-522 4.99e-11

The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The stimulation of plexin B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200538 [Multi-domain]  Cd Length: 434  Bit Score: 66.76  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   64 DRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGD-PGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGR 142
Cdd:cd11277    14 DPGSGTLYVGAVNRLYQLSPDLQLLGEAVTGPVLDsPDCLPFRDPADCPQARLTDNANKLLLVSERAGELVACGQVRQGV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  143 C---FLHDL-------EPQGTAVHLAApaclfsahhNRPDdcpdcvaspLGTRVTVVEQGQASYFYVASSLDAAVAASFS 212
Cdd:cd11277    94 CekrRLGNVaqvlyqaEDPGDGQFVAA---------NDPG---------VATVGLVVEAPGRDLLLVGRGLTGKLSAGIP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  213 PrsVSIRRLKADASGFAPGFVALSVlpKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDdpSALHTRLARLSATEPELGD 292
Cdd:cd11277   156 P--LTIRQLAGAQAFSSEGLGKLVV--GDFSDYNNSYVGAFAHNGYVYFLFRRRGARAQ--AEYRTYVARVCLGDTNLYS 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  293 YRELVLDCRfapkrrrrgapeGGqpYPVLRVAHSAPvgaqlatelsiaeGQEVLFGVFVTGKDGGPGVGPNSVVCAFPID 372
Cdd:cd11277   230 YVEVPLVCQ------------GG--YNLAQAAYLAP-------------GQGTLFVVFAAGQGSTPTPTDQTALCAYPLV 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  373 LLDTLIDEGVERCC-----------ESPVHPGLRRGLDFFQSPSFCPNPPGLEAlSPNTSCRHFPLLVSSSFSrvdlfng 441
Cdd:cd11277   283 ELDSAMERARRLCYtaggggpngkeEATIEYGVTSRCVNLPKDSPESYPCGDEH-TPSPIASRQPLEAEPLLT------- 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  442 lLGPvQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLyvSNFSLGDSGQPVQRD--VSRLGDHLLFASGDQVFQ 519
Cdd:cd11277   355 -LTP-PLTAVAALQEDGHTIAFLGDTQGQLHKVFLNGSAGQVY--SSQPVGPPGSAVNPDllLDATGSHLYVLTARQVTK 430

                  ...
gi 578806145  520 VPI 522
Cdd:cd11277   431 VPV 433
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1089-1314 5.13e-11

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 65.41  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYiDQAQNRIqcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMcHG 1168
Cdd:cd07873    10 LGEGTYATVYKGRS-KLTDNLV--ALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLT-LVFEYL-DK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR--DILDREYYSVQQHR 1246
Cdd:cd07873    85 DLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARakSIPTKTYSNEVVTL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1247 HARLPVKWmalesLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEYCP 1314
Cdd:cd07873   165 WYRPPDIL-----LGSTDYSTQIDMWGVGCIFYEMST-GRPLFPGSTVEEQLHFIFRILGTPTEETWP 226
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1130-1289 5.17e-11

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: 65.42  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1130 LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPYMcHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRD 1209
Cdd:cd07871    51 IREVSLLKNLKHANIVTLHDIIHTERCLTLVF-EYL-DSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1210 LAARNCMLDESFTVKVADFGLARdildreYYSVQQHRHARLPVK-WMALES--LQTYRFTTKSDVWSFGVLLWELLTrGA 1286
Cdd:cd07871   129 LKPQNLLINEKGELKLADFGLAR------AKSVPTKTYSNEVVTlWYRPPDvlLGSTEYSTPIDMWGVGCILYEMAT-GR 201

                  ...
gi 578806145 1287 PPY 1289
Cdd:cd07871   202 PMF 204
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
1089-1284 5.54e-11

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: 64.98  E-value: 5.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYH------GEYIDQAQNRIQ-----CAIKSLSRITEMQQVEAFlregllmrglNHPNVLALIGI--MLPPE 1155
Cdd:cd07863     8 IGVGAYGTVYKardphsGHFVALKSVRVQtnedgLPLSTVREVALLKRLEAF----------DHPNIVRLMDVcaTSRTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 GLPHVLLPY-MCHGDLLQFIRS--PQRNP--TVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGL 1230
Cdd:cd07863    78 RETKVTLVFeHVDQDLRTYLDKvpPPGLPaeTIKDLMR---QFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1231 ARdildreYYSVQQHRHARLPVKWM-ALESLQTYRFTTKSDVWSFGVLLWELLTR 1284
Cdd:cd07863   155 AR------IYSCQMALTPVVVTLWYrAPEVLLQSTYATPVDMWSVGCIFAEMFRR 203
IPT smart00429
ig-like, plexins, transcription factors;
568-627 5.62e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 60.13  E-value: 5.62e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    568 PPKLTEFHPHSGPLRGSTRLTLCGSNFylhpsGLVPEGTHQVTVGQSPCRPLPKDSSKLR 627
Cdd:smart00429    1 DPVITRISPTSGPVSGGTEITLCGKNL-----KSISVVFVEVGVGEAPCTFSPSSSTAIV 55
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
1089-1295 6.13e-11

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: 65.06  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeYIDQAQNRIQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd06658    30 IGEGSTGIVC---IATEKHTGKQVAVKKMD-LRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDEL-WVVMEFLEGG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPtvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyysVQQHRHA 1248
Cdd:cd06658   105 ALTDIVTHTRMNE--EQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKE----VPKRKSL 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1249 RLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPF 1295
Cdd:cd06658   179 VGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFNEPPL 224
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
1087-1289 7.29e-11

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: 64.11  E-value: 7.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhgEYIDQAQNRIQCAIKSLSRITEMQQ-VEAFL-REGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPy 1164
Cdd:cd14164     6 TTIGEGSFSKV---KLATSQKYCCKVAIKIVDRRRASPDfVQKFLpRELSILRRVNHPNIVQMFECIEVANGRLYIVME- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTV--KDLISfglQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDILDreyYS 1241
Cdd:cd14164    82 AAATDLLQKIQEVHHIPKDlaRDMFA---QMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVED---YP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1242 VQQHRHARlPVKWMALESLQTYRFTTKS-DVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14164   156 ELSTTFCG-SRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPF 202
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1087-1334 7.67e-11

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: 64.37  E-value: 7.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSrITEMQQVE--AFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd08220     6 RVVGRGAYGTVYLCRRKDDNK---LVIIKQIP-VEQMTKEErqAALNEVKVLSMLHHPNIIEYYESFLEDKAL-MIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRspQRNPTVKD---LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFT-VKVADFGLARDILDR-EY 1239
Cdd:cd08220    81 APGGTLFEYIQ--QRKGSLLSeeeILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILSSKsKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YSVqqhrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWEL--LTRGappyrhidpFDLTHFLA------QGRRLPQPE 1311
Cdd:cd08220   159 YTV-----VGTPC-YISPELCEGKPYNQKSDIWALGCVLYELasLKRA---------FEAANLPAlvlkimRGTFAPISD 223
                         250       260
                  ....*....|....*....|...
gi 578806145 1312 YCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd08220   224 RYSEELRHLILSMLHLDPNKRPT 246
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
1089-1334 8.76e-11

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 64.32  E-value: 8.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd07847     9 IGEGSYGVVF------KCRNRETGQIVAIKKFVESEDDPVIkkiaLREIRMLKQLKHPNLVNLIEVFRRKRKL-HLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNP--TVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdIL---DREY 1239
Cdd:cd07847    82 CDHTVLNELEKNPRGVPehLIKKII---WQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR-ILtgpGDDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YSVQQHRHARLPvkwmalESL-QTYRFTTKSDVWSFGVLLWELLTrGAPPY---------------------RHIDPFDL 1297
Cdd:cd07847   158 TDYVATRWYRAP------ELLvGDTQYGPPVDVWAIGCVFAELLT-GQPLWpgksdvdqlylirktlgdlipRHQQIFST 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1298 THFLAqGRRLPQPE-----------YCPDSLyQVMQQCWEADPAVRPT 1334
Cdd:cd07847   231 NQFFK-GLSIPEPEtrepleskfpnISSPAL-SFLKGCLQMDPTERLS 276
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
1087-1290 9.17e-11

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: 64.30  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeyidQAQNRIQ---CAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVL 1161
Cdd:cd05605     6 RVLGKGGFGEVC------ACQVRATgkmYACKKLekKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDAL-CLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIRSpQRNP--TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREy 1239
Cdd:cd05605    79 LTIMNGGDLKFHIYN-MGNPgfEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGE- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1240 ySVqqhrHARL-PVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd05605   157 -TI----RGRVgTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIE-GQAPFR 202
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
1086-1334 9.70e-11

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: 63.87  E-value: 9.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYhgeyidQAQNR---IQCAIK-SLSRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGIMlppEGLPHV 1160
Cdd:cd14050     6 LSKLGEGSFGEVF------KVRSRedgKLYAVKrSRSRFRGEKDRKRKLEEvERHEKLGEHPNCVRFIKAW---EEKGIL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPY-MCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDiLDREY 1239
Cdd:cd14050    77 YIQTeLCDTSLQQYCEETHSLPE-SEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-LDKED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YSVQQHRHARlpvkWMALESLQTyRFTTKSDVWSFGVLLWELLTrgappYRHIDPF-DLTHFLAQGrRLPQPEY--CPDS 1316
Cdd:cd14050   155 IHDAQEGDPR----YMAPELLQG-SFTKAADIFSLGITILELAC-----NLELPSGgDGWHQLRQG-YLPEEFTagLSPE 223
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMQQCWEADPAVRPT 1334
Cdd:cd14050   224 LRSIIKLMMDPDPERRPT 241
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
1087-1299 1.02e-10

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 64.71  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDqaqNRIQCAIKSLSR--ITEMQQVEAFLREG-LLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd05592     1 KVLGKGSFGKVMLAELKG---TNQYFAIKALKKdvVLEDDDVECTMIERrVLALASQHPFLTHLFCTFQTESHLFFVM-E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRnptvkdlisFGLQVAR--------GMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL 1235
Cdd:cd05592    77 YLNGGDLMFHIQQSGR---------FDEDRARfygaeiicGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENI 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1236 DREyysVQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFDLTH 1299
Cdd:cd05592   148 YGE---NKASTFCGTP-DYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPFHGEDEDELFW 206
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1087-1336 1.35e-10

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 63.63  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVvyhGEYIDQAQNRIQCAIKSLSRITEMQqvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMC 1166
Cdd:cd14662     6 KDIGSGNFGV---ARLMRNKETKELVAVKYIERGLKID--ENVQREIINHRSLRHPNIIRFKEVVLTPTHLA-IVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGlQVARGMEYLAEQKFVHRDLAARNCMLDESFT--VKVADFGLARdildreyySVQQ 1244
Cdd:cd14662    80 GGELFERICNAGRFSEDEARYFFQ-QLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSK--------SSVL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARLPV---KWMALESLQTYRFTTK-SDVWSFGVLLWELLTrGAPPYRhiDPFDLTHFLAQGRRLPQPEYCPDSLYQV 1320
Cdd:cd14662   151 HSQPKSTVgtpAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLV-GAYPFE--DPDDPKNFRKTIQRIMSVQYKIPDYVRV 227
                         250       260
                  ....*....|....*....|...
gi 578806145 1321 MQQC-------WEADPAVRPTFR 1336
Cdd:cd14662   228 SQDCrhllsriFVANPAKRITIP 250
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
1089-1298 1.36e-10

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: 63.81  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRIQcAIKSLSRITEMQQ-------------------------VEAFLREGLLMRGLNHPN 1143
Cdd:cd14200     8 IGKGSYGVVKLA--YNESDDKYY-AMKVLSKKKLLKQygfprrppprgskaaqgeqakplapLERVYQEIAILKKLDHVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1144 VLALIGIML-PPEGLPHVLLPYMCHGDLLQFirsPQRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCMLDESF 1221
Cdd:cd14200    85 IVKLIEVLDdPAEDNLYMVFDLLRKGPVMEV---PSDKPFSEDQARLYFRdIVLGIEYLHYQKIVHRDIKPSNLLLGDDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1222 TVKVADFGLARDIldrEYYSVQQHRHARLPVkWMALESLQTYR--FTTKS-DVWSFGVLLWeLLTRGAPPYrhIDPFDLT 1298
Cdd:cd14200   162 HVKIADFGVSNQF---EGNDALLSSTAGTPA-FMAPETLSDSGqsFSGKAlDVWAMGVTLY-CFVYGKCPF--IDEFILA 234
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1089-1282 1.54e-10

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


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 63.68  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQ---CAIKS-LSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPY 1164
Cdd:cd14049    14 LGKGGYGKVY------KVRNKLDgqyYAIKKiLIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPT-------------VKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDES-FTVKVADFGL 1230
Cdd:cd14049    88 LCELSLWDWIVERNKRPCeeefksapytpvdVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSdIHVRIGDFGL 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 A-RDILDREYYSVQQHRHARL-------PVKWMALESLQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:cd14049   168 AcPDILQDGNDSTTMSRLNGLthtsgvgTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
1084-1289 1.71e-10

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: 63.34  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1084 HSDRVIGKGHFGVVYHGEYIdqaQNRIQCAIKSLSRITE-MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLL 1162
Cdd:cd14097     4 TFGRKLGQGSFGVVIEATHK---ETQTKWAIKKINREKAgSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRM--YLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDES-------FTVKVADFGLARDIL 1235
Cdd:cd14097    79 MELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLSVQKY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1236 DREYYSVQQHrhARLPVkWMALESLQTYRFTTKSDVWSFGVLLWeLLTRGAPPY 1289
Cdd:cd14097   159 GLGEDMLQET--CGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPF 208
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
684-766 1.75e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 58.61  E-value: 1.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   684 PVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRA-VLVNGTECLLARVSEGQLLCATPPGATvASVPLSLQVGGAQ-VPGS 761
Cdd:pfam01833    1 PVITSISPSSGPASGGTTITITGSNFGTDSSDLkVTIGGTPCTVISVSSTTIVCTTPPGTS-GLVNVSVTVGGGGiSSSP 79

                   ....*
gi 578806145   762 WTFQY 766
Cdd:pfam01833   80 LTFTY 84
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
1160-1339 1.75e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 65.04  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRspQRnptVKDLISF-----GL---QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:PTZ00267  142 LIMEYGSGGDLNKQIK--QR---LKEHLPFqeyevGLlfyQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFS 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 RDILDREYYSVQQhRHARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTRGApPYRHIDPFDLTHFLAQGRRLPQPe 1311
Cdd:PTZ00267  217 KQYSDSVSLDVAS-SFCGTPY-YLAPELWERKRYSKKADMWSLGVILYELLTLHR-PFKGPSQREIMQQVLYGKYDPFP- 292
                         170       180       190
                  ....*....|....*....|....*....|
gi 578806145 1312 yCP--DSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:PTZ00267  293 -CPvsSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
1087-1284 1.76e-10

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: 64.11  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeYIDQAQNRIqcAIKSLsRITEMQQVEAFLREGLLMRGLN--HPNVLALIGIMLPPEGLP------ 1158
Cdd:cd13977     6 REVGRGSYGVVYEA-VVRRTGARV--AVKKI-RCNAPENVELALREFWALSSIQrqHPNVIQLEECVLQRDGLAqrmshg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 ------HVLLPYMC-----------------------HGDLLQFIRSpqRNPTVKDLISFGLQVARGMEYLAEQKFVHRD 1209
Cdd:cd13977    82 ssksdlYLLLVETSlkgercfdprsacylwfvmefcdGGDMNEYLLS--RRPDRQTNTSFMLQLSSALAFLHRNQIVHRD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1210 LAARNCMLDESF---TVKVADFGLAR-----DILDREYYSVQQHRHARLPVK--WMALESLQTYrFTTKSDVWSFGVLLW 1279
Cdd:cd13977   160 LKPDNILISHKRgepILKVADFGLSKvcsgsGLNPEEPANVNKHFLSSACGSdfYMAPEVWEGH-YTAKADIFALGIIIW 238

                  ....*
gi 578806145 1280 ELLTR 1284
Cdd:cd13977   239 AMVER 243
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
1089-1289 2.03e-10

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: 63.28  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVV-----------YHGEYIDQAQnriqcaIKSLSRITEMQQVEaflREGLLMRGLNHPNVLALIGIMlppEGL 1157
Cdd:cd14105    13 LGSGQFAVVkkcrekstgleYAAKFIKKRR------SKASRRGVSREDIE---REVSILRQVLHPNIITLHDVF---ENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1158 PHV--LLPYMCHGDLLQFIrSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFT----VKVADFGLA 1231
Cdd:cd14105    81 TDVvlILELVAGGELFDFL-AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1232 RDILDReyysvQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14105   160 HKIEDG-----NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPF 211
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1193-1334 2.16e-10

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: 63.21  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1193 VARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFG--------LARDILDREYYsvqqhrharlpvkwMALESLQTYR 1264
Cdd:cd06621   114 VLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGvsgelvnsLAGTFTGTSYY--------------MAPERIQGGP 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1265 FTTKSDVWSFGVLLWEL-------LTRGAPPyrhIDPFDLTHFLAqgrRLPQPEY--CPD-------SLYQVMQQCWEAD 1328
Cdd:cd06621   180 YSITSDVWSLGLTLLEVaqnrfpfPPEGEPP---LGPIELLSYIV---NMPNPELkdEPEngikwseSFKDFIEKCLEKD 253

                  ....*.
gi 578806145 1329 PAVRPT 1334
Cdd:cd06621   254 GTRRPG 259
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1089-1283 2.51e-10

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: 63.06  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidqaqnRIQC-------AIKSL-SRITEMQQVEAfLREGLLMRGLN-HPNVLALIGIMLPPeglPH 1159
Cdd:cd07831     7 IGEGTFSEVL----------KAQSrktgkyyAIKCMkKHFKSLEQVNN-LREIQALRRLSpHPNILRLIEVLFDR---KT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCH---GDLLQFIRSpQRNP----TVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESfTVKVADFGLAR 1232
Cdd:cd07831    73 GRLALVFElmdMNLYELIKG-RKRPlpekRVK---NYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1233 DILDR----EYYSVQQHRharlpvkwmALESLQTY-RFTTKSDVWSFGVLLWELLT 1283
Cdd:cd07831   148 GIYSKppytEYISTRWYR---------APECLLTDgYYGPKMDIWAVGCVFFEILS 194
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1089-1284 2.62e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 63.30  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:PLN00009   10 IGEGTYGVVY------KARDRVTNETIALKKIRLEQEDEGVpstaIREISLLKEMQHGNIVRLQDVVHSEKRL-YLVFEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 McHGDLLQFIRSP---QRNPTVkdLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF-TVKVADFGLARDIldreYY 1240
Cdd:PLN00009   83 L-DLDLKKHMDSSpdfAKNPRL--IKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTnALKLADFGLARAF----GI 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1241 SVQQHRHARLPVKWMALESLQTYR-FTTKSDVWSFGVLLWELLTR 1284
Cdd:PLN00009  156 PVRTFTHEVVTLWYRAPEILLGSRhYSTPVDIWSVGCIFAEMVNQ 200
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1089-1334 2.88e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 62.82  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHgeyIDQAQNRIQCAIK--SLSRIT--EMQQVEaflREGLLMRGLNHPNVLALIGiMLPPEGLPHVLLPY 1164
Cdd:cd14086     9 LGKGAFSVVRR---CVQKSTGQEFAAKiiNTKKLSarDHQKLE---REARICRLLKHPNIVRLHD-SISEEGFHYLVFDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFI--RSPQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARDILDRey 1239
Cdd:cd14086    82 VTGGELFEDIvaREFYSEADASHCIQ---QILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGD-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 ysvQQHRH--ARLPVkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGR-RLPQPEY---C 1313
Cdd:cd14086   157 ---QQAWFgfAGTPG-YLSPEVLRKDPYGKPVDIWACGVILYILLV-GYPPFWDEDQHRLYAQIKAGAyDYPSPEWdtvT 231
                         250       260
                  ....*....|....*....|.
gi 578806145 1314 PDSlYQVMQQCWEADPAVRPT 1334
Cdd:cd14086   232 PEA-KDLINQMLTVNPAKRIT 251
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1089-1336 2.93e-10

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 63.54  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEY----IDQAQNRIQCAIKSLSRitemqqvEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPY 1164
Cdd:cd06650    13 LGAGNGGVVFKVSHkpsgLVMARKLIHLEIKPAIR-------NQIIRELQVLHECNSPYIVGFYGAFYS-DGEISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQ 1243
Cdd:cd06650    85 MDGGSLDQVLKKAGRIPE-QILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRharlpvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPpyrhIDPFDlthflaqGRRLPQPEYCPdslyqVMQQ 1323
Cdd:cd06650   164 GTR------SYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYP----IPPPD-------AKELELMFGCQ-----VEGD 221
                         250
                  ....*....|...
gi 578806145 1324 CWEADPAVRPTFR 1336
Cdd:cd06650   222 AAETPPRPRTPGR 234
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1089-1289 3.30e-10

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: 62.50  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVY------HGEYIdqaqnriqcAIKSL--SRITEMQQVEAFLRE-GLLMRGLNHPNVLALIGIMLPPEGLpH 1159
Cdd:cd05611     4 ISKGAFGSVYlakkrsTGDYF---------AIKVLkkSDMIAKNQVTNVKAErAIMMIQGESPYVAKLYYSFQSKDYL-Y 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRS--PQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR 1237
Cdd:cd05611    74 LVMEYLNGGDCASLIKTlgGLPEDWAKQYIA---EVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1238 EyysvQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05611   151 R----HNKKFVGTP-DYLAPETILGVGDDKMSDWWSLGCVIFEFLF-GYPPF 196
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
1087-1283 3.73e-10

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: 63.26  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeyIDQaQNRIQCAIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLP-----PEGLP--- 1158
Cdd:cd07854    11 RPLGCGSNGLVFSA--VDS-DCDKRVAVKKIV-LTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPsgsdlTEDVGslt 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 -----HVLLPYMcHGDLLQFIrspQRNPTVKDLIS-FGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLA 1231
Cdd:cd07854    87 elnsvYIVQEYM-ETDLANVL---EQGPLSEEHARlFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1232 RdILDREyYSVQQHRHARLPVKWMALES--LQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:cd07854   163 R-IVDPH-YSHKGYLSEGLVTKWYRSPRllLSPNNYTKAIDMWAAGCIFAEMLT 214
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
1089-1334 4.22e-10

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 62.23  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQN--RIQCAIK--SLSRITEmQQVEAFLRE-GLLMRGLNHPNVLALIGI-MLPPEGLPHVLL 1162
Cdd:cd14131     9 LGKGGSSKVY------KVLNpkKKIYALKrvDLEGADE-QTLQSYKNEiELLKKLKGSDRIIQLYDYeVTDEDDYLYMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYmCHGDLLQFIRspQRNPTVKD---LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFtVKVADFGLARDILDrey 1239
Cdd:cd14131    82 EC-GEIDLATILK--KKRPKPIDpnfIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR-LKLIDFGIAKAIQN--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YSVQQHRHARL-PVKWMALESLQ----------TYRFTTKSDVWSFGVLLWELlTRGAPPYRHIdpfdlTHFLAQGRRLP 1308
Cdd:cd14131   155 DTTSIVRDSQVgTLNYMSPEAIKdtsasgegkpKSKIGRPSDVWSLGCILYQM-VYGKTPFQHI-----TNPIAKLQAII 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578806145 1309 QPEY-------CPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14131   229 DPNHeiefpdiPNPDLIDVMKRCLQRDPKKRPS 261
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
1087-1290 4.47e-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: 62.68  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMC 1166
Cdd:cd05632     8 RVLGKGGFGEVCACQ-VRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALC-LVLTIMN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLlQFIRSPQRNPTVKD--LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYsvqq 1244
Cdd:cd05632    86 GGDL-KFHIYNMGNPGFEEerALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESI---- 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1245 hRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYR 1290
Cdd:cd05632   161 -RGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMI-EGQSPFR 204
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
1089-1229 5.39e-10

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 58.99  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQcaikSLSRITEMQQVEAFLREGLLMR-----GLNHPNVL-------ALIGIMlppEG 1156
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAV----KIGDDVNNEEGEDLESEMDILRrlkglELNIPKVLvtedvdgPNILLM---EL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1157 LPHVLLPymchgDLLQFIRSPQrnptvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFG 1229
Cdd:cd13968    74 VKGGTLI-----AYTQEEELDE-----KDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
1087-1290 6.32e-10

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 61.93  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPYMC 1166
Cdd:cd05631     6 RVLGKGGFGEVCACQ-VRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVL-TIMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLlQFIRSPQRNPTVKD--LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYsvqq 1244
Cdd:cd05631    84 GGDL-KFHIYNMGNPGFDEqrAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETV---- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578806145 1245 hRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYR 1290
Cdd:cd05631   159 -RGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMI-QGQSPFR 202
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
1089-1334 8.23e-10

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 61.18  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIdQAQNRIQCAIKSLSRITEMQ-QVEAFLRegllmrglnHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd13995    12 IPRGAFGKVYLAQDT-KTKKRMACKLIPVEQFKPSDvEIQACFR---------HENIAELYGALLWEETV-HLFMEAGEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRS--PQRNptvKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVaDFGLARDILDREYYSvqqh 1245
Cdd:cd13995    81 GSVLEKLEScgPMRE---FEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVP---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1246 RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY-----RHIDPFDLTHFLAQGRRLPQ-PEYCPDSLYQ 1319
Cdd:cd13995   153 KDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQT-GSPPWvrrypRSAYPSYLYIIHKQAPPLEDiAQDCSPAMRE 231
                         250
                  ....*....|....*
gi 578806145 1320 VMQQCWEADPAVRPT 1334
Cdd:cd13995   232 LLEAALERNPNHRSS 246
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
1132-1283 8.41e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 62.70  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1132 EGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYmcHGDLLQFIrSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLA 1211
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRY--KTDLYCYL-AAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIK 209
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1212 ARNCMLDESFTVKVADFGLA---RDILDREYYSVQQHRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:PHA03212  210 AENIFINHPGDVCLGDFGAAcfpVDINANKYYGWAGTIATNAP------ELLARDPYGPAVDIWSAGIVLFEMAT 278
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
1192-1289 8.48e-10

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: 61.46  E-value: 8.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1192 QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE--YYSVQQHRHARLPVK---------WMALESL 1260
Cdd:cd05579   101 EIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRqiKLSIQKKSNGAPEKEdrrivgtpdYLAPEIL 180
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578806145 1261 --QTYRFTtkSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05579   181 lgQGHGKT--VDWWSLGVILYEFLV-GIPPF 208
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
1089-1334 8.74e-10

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 61.08  E-value: 8.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQC----AIKSLSRITEMQQVEAFLREGLLMRGLNhpNVLALIGIMLPPEglpHVL--L 1162
Cdd:cd14019     9 IGEGTFSSVYKAEDKLHDLYDRNKgrlvALKHIYPTSSPSRILNELECLERLGGSN--NVSGLITAFRNED---QVVavL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPqrnpTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDILDREyys 1241
Cdd:cd14019    84 PYIEHDDFRDFYRKM----SLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQREEDRP--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 vQQH------RHARLPvkwmalESLQTY-RFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLthfLAQ-----GRrlpq 1309
Cdd:cd14019   157 -EQRapragtRGFRAP------EVLFKCpHQTTAIDIWSAGVILLSILSGRFPFFFSSDDIDA---LAEiatifGS---- 222
                         250       260
                  ....*....|....*....|....*
gi 578806145 1310 peycpDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14019   223 -----DEAYDLLDKLLELDPSKRIT 242
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
1187-1333 9.78e-10

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 61.18  E-value: 9.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1187 ISFGL-QVARGMEYL-AEQKFVHRDLAARNCMLDESFTVKVADFGLARDI-------LDREYYSVQQHRHARLPVKWMAL 1257
Cdd:cd14011   116 IKYGLlQISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSeqatdqfPYFREYDPNLPPLAQPNLNYLAP 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1258 ESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFD-LTHFLAQGRRLPQP--EYCPDSLYQVMQQCWEADPAVRP 1333
Cdd:cd14011   196 EYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLsYKKNSNQLRQLSLSllEKVPEELRDHVKTLLNVTPEVRP 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
1088-1233 1.02e-09

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 61.23  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYhgeyidQAQNRI---QCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd14046    13 VLGKGAFGQVV------KVRNKLdgrYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANL-YIQMEY 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVkDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARD 1233
Cdd:cd14046    86 CEKSTLRDLIDSGLFQDTD-RLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATS 153
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1088-1287 1.07e-09

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: 61.24  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGeyidqaQNRIQCAIKSLSRItEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd07844     7 KLGEGSYATVYKG------RSKLTGQLVALKEI-RLEHEEGApftaIREASLLKDLKHANIVTLHDIIHTKKTLTLVF-E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMcHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARdildreYYSVQ 1243
Cdd:cd07844    79 YL-DTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR------AKSVP 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1244 QHRHARLPVK-WmaleslqtYR----------FTTKSDVWSFGVLLWELLTrGAP 1287
Cdd:cd07844   152 SKTYSNEVVTlW--------YRppdvllgsteYSTSLDMWGVGCIFYEMAT-GRP 197
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
1088-1334 1.18e-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: 61.40  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVY---HGEyidqaqNRIQCAIKS--LSRITEMQ--QVEAFLREGLLMRGLNHPNVLALIGiMLPPEGLPHV 1160
Cdd:cd14094    10 VIGKGPFSVVRrciHRE------TGQQFAVKIvdVAKFTSSPglSTEDLKREASICHMLKHPHIVELLE-TYSSDGMLYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDL-LQFIRSPQRNPTVKDLIS--FGLQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARDI 1234
Cdd:cd14094    83 VFEFMDGADLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 LDreyysVQQHRHARLPV-KWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPfDLTHFLAQGR---RLPQP 1310
Cdd:cd14094   163 GE-----SGLVAGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTKE-RLFEGIIKGKykmNPRQW 235
                         250       260
                  ....*....|....*....|....
gi 578806145 1311 EYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14094   236 SHISESAKDLVRRMLMLDPAERIT 259
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
1089-1290 1.19e-09

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: 60.43  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyiDQAQNRIQCAIKSLSRiTEMQQVEAFL--REGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd14075    10 LGSGNFSQVKLG---IHQLTKEKVAIKILDK-TKLDQKTQRLlsREISSMEKLHHPNIIRLYEVVETLSKL-HLVMEYAS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFI--RSPQRNPTVKDLISfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGlardildreyYSVQQ 1244
Cdd:cd14075    85 GGELYTKIstEGKLSESEAKPLFA---QIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFG----------FSTHA 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1245 HRHARL-------PvkWMALESLQ-TYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd14075   152 KRGETLntfcgspP--YAAPELFKdEHYIGIYVDIWALGVLLYFMVT-GVMPFR 202
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
1088-1337 1.26e-09

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 60.92  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYidQAQNriqCAIKSLSRITEMQQV-EAFLREGLLMRglnHPNVLALIGIMLPPEGLPHVLL---P 1163
Cdd:cd14143     2 SIGKGRFGEVWRGRW--RGED---VAVKIFSSREERSWFrEAEIYQTVMLR---HENILGFIAADNKDNGTWTQLWlvsD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIrspQRNP-TVKDLISFGLQVARG-----MEYLAEQ---KFVHRDLAARNCMLDESFTVKVADFGLARDi 1234
Cdd:cd14143    74 YHEHGSLFDYL---NRYTvTVEGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDLKSKNILVKKNGTCCIADLGLAVR- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 LDREYYSVQQHRHARLPVK-WMALE----SLQTYRFTT--KSDVWSFGVLLWELLTR----GAP-----PYRHIDPFDLT 1298
Cdd:cd14143   150 HDSATDTIDIAPNHRVGTKrYMAPEvlddTINMKHFESfkRADIYALGLVFWEIARRcsigGIHedyqlPYYDLVPSDPS 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1299 ------HFLAQGRRLPQPEYCPDS-----LYQVMQQCWEADPAVR-PTFRV 1337
Cdd:cd14143   230 ieemrkVVCEQKLRPNIPNRWQSCealrvMAKIMRECWYANGAARlTALRI 280
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1130-1294 1.26e-09

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 60.61  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1130 LREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPYMCHG-DLLQFIRSPQRNpTVKDLISFGLQVARGMEYLAEQKFVHR 1208
Cdd:cd14111    47 LQEYEILKSLHHERIMALHEAYITPRYL--VLIAEFCSGkELLHSLIDRFRY-SEDDVVGYLVQILQGLEYLHGRRVLHL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1209 DLAARNCMLDESFTVKVADFGLARDIldrEYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPP 1288
Cdd:cd14111   124 DIKPDNIMVTNLNAIKIVDFGSAQSF---NPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLS-GRSP 199

                  ....*.
gi 578806145 1289 YRHIDP 1294
Cdd:cd14111   200 FEDQDP 205
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
1191-1338 1.32e-09

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 60.90  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1191 LQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDILDreyySVQQHRHARLPvKWMALE----SLQTYRF 1265
Cdd:cd06617   110 VSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVD----SVAKTIDAGCK-PYMAPErinpELNQKGY 184
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1266 TTKSDVWSFGVLLWELLTrGAPPY-RHIDPFDLTHFLAQGR--RLPQPEYCPDSLYQVmQQCWEADPAVRPTFRVL 1338
Cdd:cd06617   185 DVKSDVWSLGITMIELAT-GRFPYdSWKTPFQQLKQVVEEPspQLPAEKFSPEFQDFV-NKCLKKNYKERPNYPEL 258
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
1087-1291 1.38e-09

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: 60.81  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMC 1166
Cdd:cd05630     6 RVLGKGGFGEVCACQ-VRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALC-LVLTLMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDL-LQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyysvQQH 1245
Cdd:cd05630    84 GGDLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPE------GQT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1246 RHARL-PVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd05630   158 IKGRVgTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFQQ 203
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
1089-1296 1.39e-09

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 61.60  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRiQCAIKSLSRITEMQ-QVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLP-----HVLL 1162
Cdd:cd07875    32 IGSGAQGIVCAA--YDAILER-NVAIKKLSRPFQNQtHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEefqdvYIVM 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMcHGDLLQFIRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI---LDREY 1239
Cdd:cd07875   109 ELM-DANLCQVIQMELDHERMSYLL---YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAgtsFMMTP 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1240 YSVQqhRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLTRGA--PPYRHIDPFD 1296
Cdd:cd07875   185 YVVT--RYYRAP------EVILGMGYKENVDIWSVGCIMGEMIKGGVlfPGTDHIDQWN 235
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
1088-1297 1.44e-09

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 61.17  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEyiDQAQNRIQcAIKSLSRITEMQQ--VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYM 1165
Cdd:cd05616     7 VLGKGSFGKVMLAE--RKGTDELY-AVKILKKDVVIQDddVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQR--NPTVkdlISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARD-ILDreyySV 1242
Cdd:cd05616    84 NGGDLMYHIQQVGRfkEPHA---VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEnIWD----GV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1243 QQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDL 1297
Cdd:cd05616   157 TTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDEL 209
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
1192-1334 1.47e-09

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 60.36  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1192 QVARGMEYLAEQKFVHRDLAARNCML--DESFTVKVADFGLARDILDREYYSVQQhRHARLPvkwmalESLQTYRFTTKS 1269
Cdd:cd14133   110 QILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCFLTQRLYSYIQS-RYYRAP------EVILGLPYDEKI 182
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1270 DVWSFGVLLWELLTrGAPPYRHIDPFDL------------THFLAQGRrlpqpeyCPDSLY-QVMQQCWEADPAVRPT 1334
Cdd:cd14133   183 DMWSLGCILAELYT-GEPLFPGASEVDQlariigtigippAHMLDQGK-------ADDELFvDFLKKLLEIDPKERPT 252
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
1087-1334 1.80e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 60.44  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQQV-EAFLREGLLMRglnHPNVLALIGIMLPPEGLP---HVLL 1162
Cdd:cd14220     1 RQIGKGRYGEVWMGKWRGE-----KVAVKVFFTTEEASWFrETEIYQTVLMR---HENILGFIAADIKGTGSWtqlYLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNptVKDLISFGLQVARGMEYLAEQKF--------VHRDLAARNCMLDESFTVKVADFGLARDi 1234
Cdd:cd14220    73 DYHENGSLYDFLKCTTLD--TRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVK- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1235 LDREYYSVQQHRHARLPVK-WMALESLQT------YRFTTKSDVWSFGVLLWELLTRGAP---------PYRHIDPF--- 1295
Cdd:cd14220   150 FNSDTNEVDVPLNTRVGTKrYMAPEVLDEslnknhFQAYIMADIYSFGLIIWEMARRCVTggiveeyqlPYYDMVPSdps 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1296 --DLTHFLAQGRRLP------QPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14220   230 yeDMREVVCVKRLRPtvsnrwNSDECLRAVLKLMSECWAHNPASRLT 276
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
1087-1309 1.83e-09

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: 60.79  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPY 1164
Cdd:cd05595     1 KLLGKGTFGKVI---LVREKATGRYYAMKILRKevIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVM-EY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLqFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysVQQ 1244
Cdd:cd05595    77 ANGGELF-FHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDG---ATM 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1245 HRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYR--HIDPFDLthFLAQGRRLPQ 1309
Cdd:cd05595   153 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqdHERLFEL--ILMEEIRFPR 216
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1089-1338 2.35e-09

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 60.07  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVY---H---GEYIdqAQNRIQCAIKSLSRITEMQQVEAflreglLMRGLNHPNVLALIGIMLPpEGLPHVLL 1162
Cdd:cd06616    14 IGRGAFGTVNkmlHkpsGTIM--AVKRIRSTVDEKEQKRLLMDLDV------VMRSSDCPYIVKFYGALFR-EGDCWICM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYM--CHGDLLQFIRSPQRNPTVKDLIS-FGLQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDILDre 1238
Cdd:cd06616    85 ELMdiSLDKFYKYVYEVLDSVIPEEILGkIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 yySVQQHRHA--RlpvKWMALESLQTYR----FTTKSDVWSFGVLLWELLTrGAPPYRHIDP-FDLTHFLAQGrrlPQPE 1311
Cdd:cd06616   163 --SIAKTRDAgcR---PYMAPERIDPSAsrdgYDVRSDVWSLGITLYEVAT-GKFPYPKWNSvFDQLTQVVKG---DPPI 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578806145 1312 YCPDSLYQV-------MQQCWEADPAVRPTFRVL 1338
Cdd:cd06616   234 LSNSEEREFspsfvnfVNLCLIKDESKRPKYKEL 267
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1089-1289 2.39e-09

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: 59.99  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVyhgEYIDQAQNRIQCAIKSLSRitEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGlpHVLLPYMC-H 1167
Cdd:cd14113    15 LGRGRFSVV---KKCDQRGTKRAVATKFVNK--KLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTS--YILVLEMAdQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF---TVKVADFGLARDiLDREYYSVQQ 1244
Cdd:cd14113    88 GRLLDYVVR-WGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAVQ-LNTTYYIHQL 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1245 HRHArlpvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14113   166 LGSP----EFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPF 205
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
1087-1296 2.45e-09

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 60.81  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeyIDQAQNrIQCAIKSLSRITEMQ-QVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHV----L 1161
Cdd:cd07876    27 KPIGSGAQGIVCAA--FDTVLG-INVAVKKLSRPFQNQtHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFqdvyL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR----DILDR 1237
Cdd:cd07876   104 VMELMDANLCQVIHMELDHERMSYLL---YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARtactNFMMT 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1238 EYYSVQQHRharlpvkwmALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPYRHIDPFD 1296
Cdd:cd07876   181 PYVVTRYYR---------APEVILGMGYKENVDIWSVGCIMGELV-KGSVIFQGTDHID 229
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
1087-1293 2.61e-09

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 60.51  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNriqCAIKSLSRITEMQQ--VEAFlREGLLMRGLNHPNVLALIGIMLPPEGLP-----H 1159
Cdd:cd07850     6 KPIGSGAQGIVCAAYDTVTGQN---VAIKKLSRPFQNVThaKRAY-RELVLMKLVNHKNIIGLLNVFTPQKSLEefqdvY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHgDLLQFIrspQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR---DILD 1236
Cdd:cd07850    82 LVMELMDA-NLCQVI---QMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARtagTSFM 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 REYYSVQqhRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLtRGA---PPYRHID 1293
Cdd:cd07850   158 MTPYVVT--RYYRAP------EVILGMGYKENVDIWSVGCIMGEMI-RGTvlfPGTDHID 208
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
1087-1289 2.84e-09

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 60.37  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidQAQNRIQcAIKSLSRITEMQQVEA---FLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd05603     1 KVIGKGSFGKVLLAKR--KCDGKFY-AVKVLQKKTILKKKEQnhiMAERNVLLKNLKHPFLVGLHYSFQTSEKL-YFVLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQ--RNPTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYS 1241
Cdd:cd05603    77 YVNGGELFFHLQRERcfLEPRAR---FYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1242 VQqhrHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPY 1289
Cdd:cd05603   154 ST---FCGTP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPF 196
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
1087-1289 2.96e-09

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: 60.11  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSR--ITEMQQVEAFLR-EGLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd05584     2 KVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKasIVRNQKDTAHTKaERNILEAVKHPFIVDLHYAFQTGGKL-YLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLlqFIRSPQRNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSv 1242
Cdd:cd05584    81 YLSGGEL--FMHLEREGIFMEDTACFYLaEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVT- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1243 qqHRHARlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05584   158 --HTFCG-TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPF 200
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1087-1325 3.85e-09

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: 59.49  E-value: 3.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyidQAQNRIQCAIKSL--SRItEMQQVEAFLREGLLMRG-LNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd14117    12 RPLGKGKFGNVYLAR---EKQSKFIVALKVLfkSQI-EKEGVEHQLRREIEIQShLRHPNILRLYNYFHDRKRI-YLILE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIR-----SPQRNPTVKDlisfglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGlardildre 1238
Cdd:cd14117    87 YAPRGELYKELQkhgrfDEQRTATFME------ELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG--------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 yYSVQQHRHARLP----VKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPP---------YRHIDPFDLTH--FLAQ 1303
Cdd:cd14117   152 -WSVHAPSLRRRTmcgtLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLV-GMPPfesashtetYRRIVKVDLKFppFLSD 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 578806145 1304 GR--------RLPQPEYCPdsLYQVMQQCW 1325
Cdd:cd14117   230 GSrdliskllRYHPSERLP--LKGVMEHPW 257
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
1089-1334 4.05e-09

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 59.76  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAqnriqCAIKSLSRITEmqqvEAFLREG-----LLMRglnHPNVLALIGI-MLPPEGLPHVLL 1162
Cdd:cd14142    13 IGKGRYGEVWRGQWQGES-----VAVKIFSSRDE----KSWFRETeiyntVLLR---HENILGFIASdMTSRNSCTQLWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 --PYMCHGDLLQFIrspQRNP-TVKDLISFGLQVARGMEYLAEQKF--------VHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd14142    81 itHYHENGSLYDYL---QRTTlDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADLGLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1232 ------RDILDREyysvqqhRHARLPVK-WMAL----ESLQTYRFTT--KSDVWSFGVLLWELLTRGA---------PPY 1289
Cdd:cd14142   158 vthsqeTNQLDVG-------NNPRVGTKrYMAPevldETINTDCFESykRVDIYAFGLVLWEVARRCVsggiveeykPPF 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1290 RHIDPFDLThFLAQGRRLPQPEYCPD------------SLYQVMQQCWEADPAVRPT 1334
Cdd:cd14142   231 YDVVPSDPS-FEDMRKVVCVDQQRPNipnrwssdptltAMAKLMKECWYQNPSARLT 286
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
1087-1291 4.25e-09

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: 59.68  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRI-TEMQQVEAFLREGLLMRGL----NHPNVLALIGIMLPPEGLPHVL 1161
Cdd:cd14223     6 RIIGRGGFGEVYGCRKADTGK---MYAMKCLDKKrIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKLSFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 lPYMCHGDLlQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE-YY 1240
Cdd:cd14223    83 -DLMNGGDL-HYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKpHA 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1241 SVQQHrharlpvKWMALESLQT-YRFTTKSDVWSFGVLLWELLtRGAPPYRH 1291
Cdd:cd14223   161 SVGTH-------GYMAPEVLQKgVAYDSSADWFSLGCMLFKLL-RGHSPFRQ 204
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1089-1281 4.43e-09

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 59.68  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEY----IDQAQNRIQCAIKSLSRitemqqvEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPY 1164
Cdd:cd06649    13 LGAGNGGVVTKVQHkpsgLIMARKLIHLEIKPAIR-------NQIIRELQVLHECNSPYIVGFYGAFYS-DGEISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQ 1243
Cdd:cd06649    85 MDGGSLDQVLKEAKRIPE-EILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFV 163
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 578806145 1244 QHRharlpvKWMALESLQTYRFTTKSDVWSFGVLLWEL 1281
Cdd:cd06649   164 GTR------SYMSPERLQGTHYSVQSDIWSMGLSLVEL 195
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1159-1400 4.62e-09

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: 59.93  E-value: 4.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPYMCHGDLlqFIRSPQRNPTVKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR 1237
Cdd:cd05614    81 HLILDYVSGGEL--FTHLYQRDHFSEDEVRFySGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTE 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1238 EyysvqQHRHARL--PVKWMALESLQTYRFTTKS-DVWSFGVLLWELLTrGAPPyrhidpfdlthFLAQGRRLPQPEycp 1314
Cdd:cd05614   159 E-----KERTYSFcgTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLT-GASP-----------FTLEGEKNTQSE--- 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1315 dslyqVMQQCWEADPAvrptFRVLVGEVEQivsALLGDHYVQLPATYMNLGPSTSHEMNvrpEQPQFSPMPGNVRRPRPL 1394
Cdd:cd05614   219 -----VSRRILKCDPP----FPSFIGPVAR---DLLQKLLCKDPKKRLGAGPQGAQEIK---EHPFFKGLDWEALALRKV 283

                  ....*.
gi 578806145 1395 SEPPRP 1400
Cdd:cd05614   284 NPPFRP 289
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
1087-1334 4.65e-09

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: 58.85  E-value: 4.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhGEYIDQAQNRiQCAIKSLSRITEMQQ-VEAFL-REGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPY 1164
Cdd:cd14163     6 KTIGEGTYSKV--KEAFSKKHQR-KVAIKIIDKSGGPEEfIQRFLpRELQIVERLDHKNIIHVYEMLESADGKIYLVMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFgLQVARGMEYLAEQKFVHRDLAARNCMLdESFTVKVADFGLARdILDREYYSVQQ 1244
Cdd:cd14163    83 AEDGDVFDCVLHGGPLPEHRAKALF-RQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAK-QLPKGGRELSQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1245 HRHARlpVKWMALESLQTYRF-TTKSDVWSFGVLLWELLTRGAPpyrhIDPFDLTHFLAQ---GRRLPQ----PEYCPDS 1316
Cdd:cd14163   160 TFCGS--TAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLP----FDDTDIPKMLCQqqkGVSLPGhlgvSRTCQDL 233
                         250
                  ....*....|....*...
gi 578806145 1317 LYQVMqqcwEADPAVRPT 1334
Cdd:cd14163   234 LKRLL----EPDMVLRPS 247
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1089-1281 4.66e-09

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: 59.62  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYiDQAQNRIqcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMcHG 1168
Cdd:cd07872    14 LGEGTYATVFKGRS-KLTENLV--ALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLT-LVFEYL-DK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR-DILDREYYSVQQHRH 1247
Cdd:cd07872    89 DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaKSVPTKTYSNEVVTL 168
                         170       180       190
                  ....*....|....*....|....*....|....
gi 578806145 1248 ARLPVKWMalesLQTYRFTTKSDVWSFGVLLWEL 1281
Cdd:cd07872   169 WYRPPDVL----LGSSEYSTQIDMWGVGCIFFEM 198
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
569-683 4.91e-09

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 54.77  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  569 PKLTEFHPHSGPLRGSTRLTLCGSNFYlhpsglvPEGTHQVTV-GQSPCRPLPKDSSKLrpvprkdfveefECELEPLGT 647
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFG-------SGSNLRVTFgGGVPCSVLSVSSTAI------------VCTTPPYAN 61
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 578806145  648 QAVGPTNVSLTVTNmppgkhfrVDGTSVLRGFSFME 683
Cdd:cd00102    62 PGPGPVEVTVDRGN--------GGITSSPLTFTYVP 89
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
1087-1287 5.34e-09

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: 59.54  E-value: 5.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSR--ITEMQQVEAFLREG-LLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGR---LYAVKVLKKdvILQDDDVECTMTEKrILSLARNHPFLTQLYCCFQTPDRLFFVM-E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLIsFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdreYYSVQ 1243
Cdd:cd05590    77 FVNGGDLMFHIQKSRRFDEARARF-YAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGI---FNGKT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1244 QHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAP 1287
Cdd:cd05590   153 TSTFCGTP-DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAP 195
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1087-1291 5.46e-09

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: 59.69  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRI-TEMQQVEAFLREGLLMRGL----NHPNVLALIGIMLPPEGLPHVL 1161
Cdd:cd05633    11 RIIGRGGFGEVYGCRKADTGK---MYAMKCLDKKrIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 lPYMCHGDLlQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE-YY 1240
Cdd:cd05633    88 -DLMNGGDL-HYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKpHA 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1241 SVQQHrharlpvKWMALESLQT-YRFTTKSDVWSFGVLLWELLtRGAPPYRH 1291
Cdd:cd05633   166 SVGTH-------GYMAPEVLQKgTAYDSSADWFSLGCMLFKLL-RGHSPFRQ 209
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
1089-1282 6.05e-09

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 59.72  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRiQCAIKSLSRITEMQ-QVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHV----LLP 1163
Cdd:cd07874    25 IGSGAQGIVCAA--YDAVLDR-NVAIKKLSRPFQNQtHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEFqdvyLVM 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR----DILDREY 1239
Cdd:cd07874   102 ELMDANLCQVIQMELDHERMSYLL---YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARtagtSFMMTPY 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1240 YSVQQHRharlpvkwmALESLQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:cd07874   179 VVTRYYR---------APEVILGMGYKENVDIWSVGCIMGEMV 212
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
1088-1289 6.06e-09

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: 59.63  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQ--VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYM 1165
Cdd:cd05615    17 VLGKGSFGKVMLAERKGSDE---LYAIKILKKDVVIQDddVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFI------RSPQRnptvkdlISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARD-ILDre 1238
Cdd:cd05615    94 NGGDLMYHIqqvgkfKEPQA-------VFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEhMVE-- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1239 yySVQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05615   165 --GVTTRTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPF 211
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1073-1291 7.98e-09

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 59.32  E-value: 7.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1073 DVLIPHERVVTHSD----RVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLA 1146
Cdd:cd05593     3 DASTTHHKRKTMNDfdylKLLGKGTFGKVI---LVREKASGKYYAMKILKKevIIAKDEVAHTLTESRVLKNTRHPFLTS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1147 LIGIMLPPEGLPHVLlPYMCHGDLLqFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVA 1226
Cdd:cd05593    80 LKYSFQTKDRLCFVM-EYVNGGELF-FHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1227 DFGLARD-ILDreyySVQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRH 1291
Cdd:cd05593   158 DFGLCKEgITD----AATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 218
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1135-1295 9.63e-09

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: 58.13  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1135 LMRGLNHPNVLALIGIMLPPEGLphVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN 1214
Cdd:cd14106    61 LELCKDCPRVVNLHEVYETRSEL--ILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQN 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1215 CMLDESFT---VKVADFGLARDILDREyysvqQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrgappyrH 1291
Cdd:cd14106   139 ILLTSEFPlgdIKLCDFGISRVIGEGE-----EIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLT-------G 206

                  ....
gi 578806145 1292 IDPF 1295
Cdd:cd14106   207 HSPF 210
pknD PRK13184
serine/threonine-protein kinase PknD;
1087-1344 1.14e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 59.78  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGeYIDQAQNRIqcaikSLSRITE-MQQVE----AFLREGLLMRGLNHPNVLALIGIMlpPEGLP-HV 1160
Cdd:PRK13184    8 RLIGKGGMGEVYLA-YDPVCSRRV-----ALKKIREdLSENPllkkRFLREAKIAADLIHPGIVPVYSIC--SDGDPvYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIRSPQR----------NPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGL 1230
Cdd:PRK13184   80 TMPYIEGYTLKSLLKSVWQkeslskelaeKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 A------RDILDREYYSVQQHRHARLPV--------KWMALESLQTYRFTTKSDVWSFGVLLWELLTRgAPPYRHIDpfd 1296
Cdd:PRK13184  160 AifkkleEEDLLDIDVDERNICYSSMTIpgkivgtpDYMAPERLLGVPASESTDIYALGVILYQMLTL-SFPYRRKK--- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1297 lthflaqGRRLPQPEYCPD------------SLYQVMQQCWEADPAVR-PTFRVLVGEVEQ 1344
Cdd:PRK13184  236 -------GRKISYRDVILSpievapyreippFLSQIAMKALAVDPAERySSVQELKQDLEP 289
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1089-1289 1.18e-08

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 57.66  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAqNRIQCAIKSLSRitEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd14115     1 IGRGRFSIVK--KCLHKA-TRKDVAVKFVSK--KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSY-ILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSpqRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCMLDESF---TVKVADFGLARDIldreyySVQQ 1244
Cdd:cd14115    75 RLLDYLMN--HDELMEEKVAFYIRdIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQI------SGHR 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1245 HRHARL--PvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14115   147 HVHHLLgnP-EFAAPEVIQGTPVSLATDIWSIGVLTYVMLS-GVSPF 191
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1088-1325 1.18e-08

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 57.55  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIdqaQNRIQCAIKSLSR-----ITEMQQVEAFLREGLLMR----GLNHPNVLALIGIMLPPEGLP 1158
Cdd:cd14101     7 LLGKGGFGTVYAGHRI---SDGLQVAIKQISRnrvqqWSKLPGVNPVPNEVALLQsvggGPGHRGVIRLLDWFEIPEGFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVL-LPYMCHgDLLQFIrsPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDIL 1235
Cdd:cd14101    84 LVLeRPQHCQ-DLFDYI--TERGALDESLArRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 DREYYSVQQHRhARLPVKWMALESLQTYRFTtksdVWSFGVLLWELLTRGAPPYRHID-----PFDLTHFLAQGRRL--- 1307
Cdd:cd14101   161 DSMYTDFDGTR-VYSPPEWILYHQYHALPAT----VWSLGILLYDMVCGDIPFERDTDilkakPSFNKRVSNDCRSLirs 235
                         250       260
                  ....*....|....*....|.
gi 578806145 1308 ---PQPEYCPdSLYQVMQQCW 1325
Cdd:cd14101   236 claYNPSDRP-SLEQILLHPW 255
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1087-1287 1.29e-08

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 57.78  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQ----AQNRIQCAIKSLSRITEMQQVEAFLReglLMRGLNHPNVLALIGIMLP-PEGLPHVL 1161
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTgrelAAKQVQFDPESPETSKEVSALECEIQ---LLKNLQHERIVQYYGCLRDrAEKTLTIF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHG---DLLQFIRSPQRNPTVKdlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDiLDRE 1238
Cdd:cd06651    90 MEYMPGGsvkDQLKAYGALTESVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR-LQTI 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1239 YYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAP 1287
Cdd:cd06651   165 CMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 213
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
1126-1291 1.37e-08

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 57.75  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1126 VEAFLREGLLMRGLN-HPNVLALIGIMLPPEGLPHVLlPYMCHGDLLQFIRS------PQRNPTVKDLISfglqvarGME 1198
Cdd:cd14093    52 REATRREIEILRQVSgHPNIIELHDVFESPTFIFLVF-ELCRKGELFDYLTEvvtlseKKTRRIMRQLFE-------AVE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1199 YLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSvqqhrhaRL---PvKWMALESLQTYRF------TTKS 1269
Cdd:cd14093   124 FLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLR-------ELcgtP-GYLAPEVLKCSMYdnapgyGKEV 195
                         170       180
                  ....*....|....*....|..
gi 578806145 1270 DVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd14093   196 DMWACGVIMYTLLA-GCPPFWH 216
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
1088-1291 1.53e-08

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 57.45  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSL--SRItEMQQVEAF-LRE----GLLMRGLNHPNVLALIGIMLPPEGLPHV 1160
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGK---MYAMKCLdkKRI-KMKQGETLaLNErimlSLVSTGGDCPFIVCMTYAFQTPDKLCFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LlPYMCHGDLlQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDRE-Y 1239
Cdd:cd05606    77 L-DLMNGGDL-HYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKpH 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1240 YSVQQHrharlpvKWMALESLQT-YRFTTKSDVWSFGVLLWELLtRGAPPYRH 1291
Cdd:cd05606   155 ASVGTH-------GYMAPEVLQKgVAYDSSADWFSLGCMLYKLL-KGHSPFRQ 199
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
1113-1295 1.61e-08

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: 57.73  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1113 AIKSLSrITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHGDLLQFIRSPQRNPtvKDLISFGLQ 1192
Cdd:cd06657    49 AVKKMD-LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDEL-WVVMEFLEGGALTDIVTHTRMNE--EQIAAVCLA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1193 VARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIlDREyysVQQHRHARLPVKWMALESLQTYRFTTKSDVW 1272
Cdd:cd06657   125 VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKE---VPRRKSLVGTPYWMAPELISRLPYGPEVDIW 200
                         170       180
                  ....*....|....*....|...
gi 578806145 1273 SFGVLLWELLTrGAPPYRHIDPF 1295
Cdd:cd06657   201 SLGIMVIEMVD-GEPPYFNEPPL 222
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
1089-1283 1.82e-08

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: 57.20  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriqcAIKSLSRITEMQ---QVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYM 1165
Cdd:cd14160     1 IGEGEIFEVYRVRIGNRSY-----AVKLFKQEKKMQwkkHWKRFLSELEVLLLFQHPNILELAAYFTETEKFC-LVYPYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLlqFIRSPQRNPTV----KDLISFGLQVARGMEYLAEQK---FVHRDLAARNCMLDESFTVKVADFGLA--RDILD 1236
Cdd:cd14160    75 QNGTL--FDRLQCHGVTKplswHERINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALAhfRPHLE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1237 REYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:cd14160   153 DQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT 199
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
1089-1289 2.03e-08

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 57.18  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIQCAIKSLSRITEMQQVEaflREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMCHG 1168
Cdd:cd14104     8 LGRGQFGIVH--RCVETSSKKTYMAKFVKVKGADQVLVK---KEISILNIARHRNILRLHESFESHEELV-MIFEFISGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN--CMLDESFTVKVADFGLARDIldreyYSVQQHR 1246
Cdd:cd14104    82 DIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENiiYCTRRGSYIKIIEFGQSRQL-----KPGDKFR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1247 HARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14104   157 LQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPF 198
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1088-1334 2.74e-08

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: 56.57  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEyiDQAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGImLPPEGLPHVLLPYMCH 1167
Cdd:cd14167    10 VLGTGAFSEVVLAE--EKRTQKL-VAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDI-YESGGHLYLIMQLVSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLlqFIRSPQRN-PTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCM---LDESFTVKVADFGLARdildREYYSVQ 1243
Cdd:cd14167    86 GEL--FDRIVEKGfYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK----IEGSGSV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYrhIDPFDLTHFlaqgRRLPQPEYCPDSLY----- 1318
Cdd:cd14167   160 MSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPF--YDENDAKLF----EQILKAEYEFDSPYwddis 231
                         250       260
                  ....*....|....*....|
gi 578806145 1319 ----QVMQQCWEADPAVRPT 1334
Cdd:cd14167   232 dsakDFIQHLMEKDPEKRFT 251
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1160-1283 2.75e-08

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: 57.06  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 VLLPYMCHGDLLQFIRSPQRNPTvKDLISFGLQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDILDRE 1238
Cdd:cd06615    76 ICMEHMDGGSLDQVLKKAGRIPE-NILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM 154
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1239 YYSVQQHRharlpvKWMALESLQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:cd06615   155 ANSFVGTR------SYMSPERLQGTHYTVQSDIWSLGLSLVEMAI 193
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
1088-1334 3.22e-08

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: 56.66  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQVEAF-LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd07846     8 LVGEGSYGMVMKCRHKETGQ---IVAIKKFLESEDDKMVKKIaMREIKMLKQLRHENLVNLIEVFRRKKRW-YLVFEFVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 H---GDLLQFIRSPQRNPTVKDLisfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD-----RE 1238
Cdd:cd07846    84 HtvlDDLEKYPNGLDESRVRKYL----FQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgevyTD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYSVQQHRHARLPVKwmaleslqTYRFTTKSDVWSFGVLLWELLTrGAPPY---------------------RHIDPFDL 1297
Cdd:cd07846   160 YVATRWYRAPELLVG--------DTKYGKAVDVWAVGCLVTEMLT-GEPLFpgdsdidqlyhiikclgnlipRHQELFQK 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1298 THfLAQGRRLPQ-----------PEYCPDSLyQVMQQCWEADPAVRPT 1334
Cdd:cd07846   231 NP-LFAGVRLPEvkeveplerryPKLSGVVI-DLAKKCLHIDPDKRPS 276
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1089-1334 3.27e-08

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: 56.59  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLsRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYmCHG 1168
Cdd:cd06645    19 IGSGTYGDVYKARNVNTGE---LAAIKVI-KLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL-WICMEF-CGG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreYYSVQQHRHA 1248
Cdd:cd06645    93 GSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQI----TATIAKRKSF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1249 RLPVKWMALESLQTYR---FTTKSDVWSFGVLLWElLTRGAPPYRHIDP----FDLTHFLAQGRRLPQPEYCPDSLYQVM 1321
Cdd:cd06645   169 IGTPYWMAPEVAAVERkggYNQLCDIWAVGITAIE-LAELQPPMFDLHPmralFLMTKSNFQPPKLKDKMKWSNSFHHFV 247
                         250
                  ....*....|...
gi 578806145 1322 QQCWEADPAVRPT 1334
Cdd:cd06645   248 KMALTKNPKKRPT 260
IPT smart00429
ig-like, plexins, transcription factors;
769-860 4.03e-08

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 52.04  E-value: 4.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145    769 DPVVLSISPNCGYI--NSHITICGQHLTSAWHLVLSFHDGlraveSRQCERQL--PEQQLCRLPEYvvrdPQGWVAGNLS 844
Cdd:smart00429    1 DPVITRISPTSGPVsgGTEITLCGKNLKSISVVFVEVGVG-----EAPCTFSPssSTAIVCKTPPY----HNIPGSVPVR 71
                            90
                    ....*....|....*.
gi 578806145    845 ARGDGAAGFTLPGFRF 860
Cdd:smart00429   72 TVGLRNGGVPSSPQPF 87
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1087-1376 5.25e-08

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 56.16  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQ---VEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLP 1163
Cdd:cd05613     6 KVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQKaktAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLHLILD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLISFGlQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyysVQ 1243
Cdd:cd05613    86 YINGGELFTHLSQRERFTENEVQIYIG-EIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDE---NE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLPVKWMALESLQ--TYRFTTKSDVWSFGVLLWELLTRGAPpyrhidpfdlthFLAQGRRLPQPEycpdslyqVM 1321
Cdd:cd05613   162 RAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASP------------FTVDGEKNSQAE--------IS 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1322 QQCWEADPavrPTFRVLVGEVEQIVSALLgdhyVQLPATYMNLGPSTSHEMNVRP 1376
Cdd:cd05613   222 RRILKSEP---PYPQEMSALAKDIIQRLL----MKDPKKRLGCGPNGADEIKKHP 269
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1193-1338 5.34e-08

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: 56.23  E-value: 5.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1193 VARGMEYLAE-QKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyySVQQHRHARLPVkWMALESLQTYRFTT---K 1268
Cdd:cd06618   123 IVKALHYLKEkHGVIHRDVKPSNILLDESGNVKLCDFGISGRLVD----SKAKTRSAGCAA-YMAPERIDPPDNPKydiR 197
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1269 SDVWSFGVLLWELLTrGAPPYRHID-PFD-LTHFLAQGR-RLP-----QPEYCpdslyQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06618   198 ADVWSLGISLVELAT-GQFPYRNCKtEFEvLTKILNEEPpSLPpnegfSPDFC-----SFVDLCLTKDHRYRPKYREL 269
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
1139-1337 5.60e-08

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 56.35  E-value: 5.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1139 LNHPNVLALigiMLPPEGLPH------VLLPYMChgDLLQFIRSPQRNPTVKDLISfgLQVARGMEYLAEQKFVHRDLAA 1212
Cdd:cd14018    94 EDYPDVLPA---RLNPSGLGHnrtlflVMKNYPC--TLRQYLWVNTPSYRLARVMI--LQLLEGVDHLVRHGIAHRDLKS 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1213 RNCMLDESFT----VKVADFG--LARDI----LDREYYSVQQHRHARLpvkwMALESLQTY--RFT----TKSDVWSFGV 1276
Cdd:cd14018   167 DNILLELDFDgcpwLVIADFGccLADDSiglqLPFSSWYVDRGGNACL----MAPEVSTAVpgPGVvinySKADAWAVGA 242
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1277 LLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRV 1337
Cdd:cd14018   243 IAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRVSARV 303
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
1088-1289 6.82e-08

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: 56.04  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAqnRIQcAIKSL--SRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYM 1165
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTS--RIY-ALKTIrkAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKL-YLVLAFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPTVKDLIsFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyySVQQH 1245
Cdd:cd05585    77 NGGELFHHLQREGRFDLSRARF-YTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKD---DDKTN 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1246 RHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05585   153 TFCGTP-EYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPF 194
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
1086-1289 7.82e-08

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: 55.11  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRiTEMQQVEA--FLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd14074     8 EETLGRGHFAVVKLARHVFTGE---KVAVKVIDK-TKLDDVSKahLFQEVRCMKLVQHPNVVRLYEVIDTQTKL-YLILE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF-TVKVADFGLArdildREYYSV 1242
Cdd:cd14074    83 LGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFS-----NKFQPG 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1243 QQHRHARLPVKWMALESL--QTYRfTTKSDVWSFGVLLWeLLTRGAPPY 1289
Cdd:cd14074   158 EKLETSCGSLAYSAPEILlgDEYD-APAVDIWSLGVILY-MLVCGQPPF 204
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
1087-1290 1.05e-07

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 55.27  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidQAQNRIQcAIKSLS--RITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPY 1164
Cdd:cd05608     7 RVLGKGGFGEVSACQM--RATGKLY-ACKKLNkkRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVM-TI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRS-PQRNPTVKD--LISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREyys 1241
Cdd:cd05608    83 MNGGDLRYHIYNvDEENPGFQEprACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQ--- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578806145 1242 VQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELL-TRGapPYR 1290
Cdd:cd05608   160 TKTKGYAGTP-GFMAPELLLGEEYDYSVDYFTLGVTLYEMIaARG--PFR 206
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
1089-1291 1.07e-07

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: 54.95  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEM--QQVEAFLREGllmrglNHPNVLALIGImLPPEGLPHVLLPYMC 1166
Cdd:cd14091     8 IGKGSYSVCKRCIHKATGK---EYAVKIIDKSKRDpsEEIEILLRYG------QHPNIITLRDV-YDDGNSVYLVTELLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML-DESF---TVKVADFGLARdildreyysv 1242
Cdd:cd14091    78 GGELLDRILR-QKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGdpeSLRICDFGFAK---------- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1243 qQHRHAR----LP---VKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd14091   147 -QLRAENgllmTPcytANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFAS 200
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1087-1335 1.15e-07

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 54.55  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYIdqaQNRIQCAIKSL--SRITEMQQVEAFLR---EGLLMRGLN---HPNVLALIGIMLPPEGLP 1158
Cdd:cd14005     6 DLLGKGGFGTVYSGVRI---RDGLPVAVKFVpkSRVTEWAMINGPVPvplEIALLLKASkpgVPGVIRLLDWYERPDGFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVL-LPYMCHgDLLQFIrspqrnpTVKDLISFGL------QVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGL 1230
Cdd:cd14005    83 LIMeRPEPCQ-DLFDFI-------TERGALSENLariifrQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 ArDILDREYYSVQQHRHARLPVKWmalesLQTYRFTTKS-DVWSFGVLLWELLTrGAPPYRHIDpfDLTHFLAQGRRLPQ 1309
Cdd:cd14005   155 G-ALLKDSVYTDFDGTRVYSPPEW-----IRHGRYHGRPaTVWSLGILLYDMLC-GDIPFENDE--QILRGNVLFRPRLS 225
                         250       260
                  ....*....|....*....|....*.
gi 578806145 1310 PEYCpdslyQVMQQCWEADPAVRPTF 1335
Cdd:cd14005   226 KECC-----DLISRCLQFDPSKRPSL 246
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1088-1339 1.16e-07

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 54.59  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIdqaQNRIQCAIKSLS--RITEMQQVEAFLR---EGLLMR--GLNHPNVLALIGIMLPPEGLPHV 1160
Cdd:cd14100     7 LLGSGGFGSVYSGIRV---ADGAPVAIKHVEkdRVSEWGELPNGTRvpmEIVLLKkvGSGFRGVIRLLDWFERPDSFVLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQFIrsPQRNPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDILDRE 1238
Cdd:cd14100    84 LERPEPVQDLFDFI--TERGALPEELArSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKDTV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYSVQQHRhARLPVKWmalesLQTYRFTTKS-DVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLPQPEycpdsl 1317
Cdd:cd14100   162 YTDFDGTR-VYSPPEW-----IRFHRYHGRSaAVWSLGILLYDMVC-GDIPFEHDEEIIRGQVFFRQRVSSECQ------ 228
                         250       260
                  ....*....|....*....|..
gi 578806145 1318 yQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd14100   229 -HLIKWCLALRPSDRPSFEDIQ 249
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
1089-1289 1.16e-07

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: 54.64  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVV-----------YHGEYIDQAQNriqcaiKSLSRITEMQQVEaflREGLLMRGLNHPNVLALIGIMlppEGL 1157
Cdd:cd14194    13 LGSGQFAVVkkcrekstglqYAAKFIKKRRT------KSSRRGVSREDIE---REVSILKEIQHPNVITLHEVY---ENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1158 PHVLL--PYMCHGDLLQFIrSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML-DESFT---VKVADFGLA 1231
Cdd:cd14194    81 TDVILilELVAGGELFDFL-AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLlDRNVPkprIKIIDFGLA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1232 RDI-LDREYYSVqqhrhARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14194   160 HKIdFGNEFKNI-----FGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPF 211
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1089-1282 1.18e-07

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: 54.80  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNRIQCAIKSLSRItEMQQVEAfLREGLLMRGLNHPNVLALIGIMLPPEGLPH--------- 1159
Cdd:cd14047    14 IGSGGFGQVF------KAKHRIDGKTYAIKRV-KLNNEKA-EREVKALAKLDHPNIVRYNGCWDGFDYDPEtsssnssrs 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1160 ---VLLPYM--CH-GDLLQFI--RSPQRNPTVKDLISFgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd14047    86 ktkCLFIQMefCEkGTLESWIekRNGEKLDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1232 RDIldREYYSVQQHRHARlpvKWMALESLQTYRFTTKSDVWSFGVLLWELL 1282
Cdd:cd14047   165 TSL--KNDGKRTKSKGTL---SYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
1089-1289 1.19e-07

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: 54.63  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIQCA--IKSLSriteMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPHVL--LPY 1164
Cdd:cd14191    10 LGSGKFGQVF--RLVEKKTKKVWAGkfFKAYS----AKEKENIRQEISIMNCLHHPKLVQCVDAF---EEKANIVmvLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARN--CMLDESFTVKVADFGLARDIldreyysv 1242
Cdd:cd14191    81 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTKIKLIDFGLARRL-------- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1243 qqHRHARLPV-----KWMALESLQTYRFTTKSDVWSFGVLLWeLLTRGAPPY 1289
Cdd:cd14191   153 --ENAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPF 201
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1088-1335 1.20e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 54.58  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSL--SRITEMQQVEAFL--REGLLMR--GLNHPNVLALIGIMLPPEGLPHVL 1161
Cdd:cd14102     7 VLGSGGFGTVYAGSRIADGL---PVAVKHVvkERVTEWGTLNGVMvpLEIVLLKkvGSGFRGVIKLLDWYERPDGFLIVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFI--RSPQRNPTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLD-ESFTVKVADFGLARDILDRE 1238
Cdd:cd14102    84 ERPEPVKDLFDFIteKGALDEDTAR---GFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKDTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1239 YYSVQQHRhARLPVKWmalesLQTYRFTTKS-DVWSFGVLLWELLtrgappYRHIdPFDLTHFLAQGRRLPQPEYCPDSl 1317
Cdd:cd14102   161 YTDFDGTR-VYSPPEW-----IRYHRYHGRSaTVWSLGVLLYDMV------CGDI-PFEQDEEILRGRLYFRRRVSPEC- 226
                         250
                  ....*....|....*...
gi 578806145 1318 YQVMQQCWEADPAVRPTF 1335
Cdd:cd14102   227 QQLIKWCLSLRPSDRPTL 244
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
1123-1334 1.54e-07

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: 54.99  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1123 MQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQ-VARGMEYLA 1201
Cdd:cd08216    40 KEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDL-YVVTPLMAYGSCRDLLKTHFPEGLPELAIAFILRdVLNALEYIH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1202 EQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVK---WMALE----SLQTYrfTTKSDVWSF 1274
Cdd:cd08216   119 SKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVVHDFPKSSEKnlpWLSPEvlqqNLLGY--NEKSDIYSV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1275 GVLLWEL---------------LT---RGAPPyrhiDPFDLTHFLAQGRRLPQPEYCP-------------------DSL 1317
Cdd:cd08216   197 GITACELangvvpfsdmpatqmLLekvRGTTP----QLLDCSTYPLEEDSMSQSEDSStehpnnrdtrdipyqrtfsEAF 272
                         250
                  ....*....|....*..
gi 578806145 1318 YQVMQQCWEADPAVRPT 1334
Cdd:cd08216   273 HQFVELCLQRDPELRPS 289
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
1089-1283 1.74e-07

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: 54.46  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidqaQNRIQCAIKSLSRI--TEMQQVEAFLR-EGLLMRGLNHPNVLALIGIMLppEGLPHVLL-PY 1164
Cdd:cd14157     1 ISEGTFADIYKGY-----RHGKQYVIKRLKETecESPKSTERFFQtEVQICFRCCHPNILPLLGFCV--ESDCHCLIyPY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDL---LQfiRSPQRNP---TVKDLISFGLqvARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLardildrE 1238
Cdd:cd14157    74 MPNGSLqdrLQ--QQGGSHPlpwEQRLSISLGL--LKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGL-------R 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1239 YYSVQQHRhARLPVKWMALESLQTY---------RFTTKSDVWSFGVLLWELLT 1283
Cdd:cd14157   143 LCPVDKKS-VYTMMKTKVLQISLAYlpedfvrhgQLTEKVDIFSCGVVLAEILT 195
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
1124-1289 2.02e-07

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: 54.25  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1124 QQVEAFLREGllmrglNHPNVLALIGIMlpPEG-LPHVLLPYMCHGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAE 1202
Cdd:cd14178    45 EEIEILLRYG------QHPNIITLKDVY--DDGkFVYLVMELMRGGELLDRILR-QKCFSEREASAVLCTITKTVEYLHS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1203 QKFVHRDLAARNCM-LDESF---TVKVADFGLARDILDREYYSVQQHRHArlpvKWMALESLQTYRFTTKSDVWSFGVLL 1278
Cdd:cd14178   116 QGVVHRDLKPSNILyMDESGnpeSIRICDFGFAKQLRAENGLLMTPCYTA----NFVAPEVLKRQGYDAACDIWSLGILL 191
                         170
                  ....*....|.
gi 578806145 1279 WELLTrGAPPY 1289
Cdd:cd14178   192 YTMLA-GFTPF 201
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1077-1309 2.09e-07

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 54.65  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1077 PHERVVTHSD---RVIGKGHFGVVYHGEyiDQAQNRIQcAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIM 1151
Cdd:cd05594    18 PKHKVTMNDFeylKLLGKGTFGKVILVK--EKATGRYY-AMKILKKevIVAKDEVAHTLTENRVLQNSRHPFLTALKYSF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1152 LPPEGLPHVLlPYMCHGDLLqFIRSPQRNPTVKDLISFGLQVARGMEYL-AEQKFVHRDLAARNCMLDESFTVKVADFGL 1230
Cdd:cd05594    95 QTHDRLCFVM-EYANGGELF-FHLSRERVFSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1231 ARD-ILDreyySVQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYR--HIDPFDLthFLAQGRRL 1307
Cdd:cd05594   173 CKEgIKD----GATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqdHEKLFEL--ILMEEIRF 245

                  ..
gi 578806145 1308 PQ 1309
Cdd:cd05594   246 PR 247
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
1089-1283 2.33e-07

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 54.30  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQcaikSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHG 1168
Cdd:cd07867    10 VGRGTYGHVYKAKRKDGKDEKEY----ALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIR---------SPQRNP--TVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARd 1233
Cdd:cd07867    86 DLWHIIKfhraskankKPMQLPrsMVKSLL---YQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR- 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1234 ILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKS-DVWSFGVLLWELLT 1283
Cdd:cd07867   162 LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLT 212
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
1085-1334 2.35e-07

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: 53.82  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1085 SDRVIGKGHFG-VVYHGEYidqaQNRiQCAIKslsRITeMQQVEAFLRE-GLLMRGLNHPNVLALIGIMLPPEGLphvll 1162
Cdd:cd13982     5 SPKVLGYGSEGtIVFRGTF----DGR-PVAVK---RLL-PEFFDFADREvQLLRESDEHPNVIRYFCTEKDRQFL----- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 pYM----CHGDLLQFIRSPqrnPTVKDLISFGL-------QVARGMEYLAEQKFVHRDLAARNCMLDESFT-----VKVA 1226
Cdd:cd13982    71 -YIalelCAASLQDLVESP---RESKLFLRPGLepvrllrQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMIS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1227 DFGLARDiLDREYYSVQQHRHARLPVKWMALESL---QTYRFTTKSDVWSFGVLLWELLTRGAPPYRhiDPFD-----LT 1298
Cdd:cd13982   147 DFGLCKK-LDVGRSSFSRRSGVAGTSGWIAPEMLsgsTKRRQTRAVDIFSLGCVFYYVLSGGSHPFG--DKLEreaniLK 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578806145 1299 HFLAQGRRLPQPEYCPDsLYQVMQQCWEADPAVRPT 1334
Cdd:cd13982   224 GKYSLDKLLSLGEHGPE-AQDLIERMIDFDPEKRPS 258
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
1118-1289 2.47e-07

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: 54.26  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1118 SRITEMQQVEAFLREGllmrglNHPNVLALIGIMLPPEGLpHVLLPYMCHGDLLQFIRSpQRNPTVKDLISFGLQVARGM 1197
Cdd:cd14176    55 SKRDPTEEIEILLRYG------QHPNIITLKDVYDDGKYV-YVVTELMKGGELLDKILR-QKFFSEREASAVLFTITKTV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1198 EYLAEQKFVHRDLAARNCM-LDESF---TVKVADFGLARDILDREYYSVQQHRHArlpvKWMALESLQTYRFTTKSDVWS 1273
Cdd:cd14176   127 EYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLLMTPCYTA----NFVAPEVLERQGYDAACDIWS 202
                         170
                  ....*....|....*.
gi 578806145 1274 FGVLLWELLTrGAPPY 1289
Cdd:cd14176   203 LGVLLYTMLT-GYTPF 217
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
1089-1339 2.60e-07

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: 53.54  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd14078    11 IGSGGFAKVKLATHILTGE---KVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKI-FMVLEYCPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSpqrnptvKDLIS------FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA---RDILDREY 1239
Cdd:cd14078    87 ELFDYIVA-------KDRLSedearvFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCakpKGGMDHHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1240 YSVqqhrhARLPVkWMALESLQ--TYrFTTKSDVWSFGVLLWELLTrGAPP---------YRHIdpfdlthflaQGRRLP 1308
Cdd:cd14078   160 ETC-----CGSPA-YAAPELIQgkPY-IGSEADVWSMGVLLYALLC-GFLPfdddnvmalYRKI----------QSGKYE 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578806145 1309 QPEYCPDSLYQVMQQCWEADPAVRPTFRVLV 1339
Cdd:cd14078   222 EPEWLSPSSKLLLDQMLQVDPKKRITVKELL 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
1131-1280 3.07e-07

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 54.06  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1131 REGLLMRGLNHPNVLALIGiMLPPEGLPHVLLPYMCHGDLlqfirSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDL 1210
Cdd:PLN00034  121 REIEILRDVNHPNVVKCHD-MFDHNGEIQVLLEFMDGGSL-----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDI 194
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1211 AARNCMLDESFTVKVADFGLAR---DILDREYYSVQQhrharlpVKWMALESLQTYRFTTK-----SDVWSFGVLLWE 1280
Cdd:PLN00034  195 KPSNLLINSAKNVKIADFGVSRilaQTMDPCNSSVGT-------IAYMSPERINTDLNHGAydgyaGDIWSLGVSILE 265
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
1089-1283 3.27e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 53.91  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQcaikSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHG 1168
Cdd:cd07868    25 VGRGTYGHVYKAKRKDGKDDKDY----ALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DL---LQFIRSPQRNPT--------VKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARd 1233
Cdd:cd07868   101 DLwhiIKFHRASKANKKpvqlprgmVKSLL---YQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR- 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1234 ILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKS-DVWSFGVLLWELLT 1283
Cdd:cd07868   177 LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLT 227
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
1088-1297 3.30e-07

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 53.94  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLSR--ITEMQQVEAFLREgllmrglnhPNVLALIGimLPP----------- 1154
Cdd:cd05587     3 VLGKGSFGKVMLAERKGTDE---LYAIKILKKdvIIQDDDVECTMVE---------KRVLALSG--KPPfltqlhscfqt 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1155 -EGLPHVLlPYMCHGDLLQFIrspQRNPTVKDLIS--FGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA 1231
Cdd:cd05587    69 mDRLYFVM-EYVNGGDLMYHI---QQVGKFKEPVAvfYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1232 RD-ILDreyySVQQHRHARLPvKWMALESLqTYRFTTKS-DVWSFGVLLWELLTrGAPPYRHIDPFDL 1297
Cdd:cd05587   145 KEgIFG----GKTTRTFCGTP-DYIAPEII-AYQPYGKSvDWWAYGVLLYEMLA-GQPPFDGEDEDEL 205
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
1089-1334 4.00e-07

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


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 53.51  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQaqnriQCAIKSLSRITEMQQV-EAFLREGLLMRglnHPNVLALIGIMLPPEG---LPHVLLPY 1164
Cdd:cd14219    13 IGKGRYGEVWMGKWRGE-----KVAVKVFFTTEEASWFrETEIYQTVLMR---HENILGFIAADIKGTGswtQLYLITDY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPtvKDLISFGLQVARGMEYLAEQKF--------VHRDLAARNCMLDESFTVKVADFGLARDILD 1236
Cdd:cd14219    85 HENGSLYDYLKSTTLDT--KAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNILVKKNGTCCIADLGLAVKFIS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1237 rEYYSVQQHRHARLPVK-WMALESLQT------YRFTTKSDVWSFGVLLWELLTRGA----------PPYRHI--DPF-- 1295
Cdd:cd14219   163 -DTNEVDIPPNTRVGTKrYMPPEVLDEslnrnhFQSYIMADMYSFGLILWEVARRCVsggiveeyqlPYHDLVpsDPSye 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1296 DLTHFLAQGRRLP------QPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:cd14219   242 DMREIVCIKRLRPsfpnrwSSDECLRQMGKLMTECWAHNPASRLT 286
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
1162-1332 4.64e-07

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 53.12  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIRSPQRNPTV---------------------------KDLISFGLQVARGMEYLAEQ----------K 1204
Cdd:cd14141    43 LPGMKHENILQFIGAEKRGTNLdvdlwlitafhekgsltdylkanvvswNELCHIAQTMARGLAYLHEDipglkdghkpA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1205 FVHRDLAARNCMLDESFTVKVADFGLArdiLDREYYSVQQHRHARLPV-KWMALESLQ-TYRFTTKS----DVWSFGVLL 1278
Cdd:cd14141   123 IAHRDIKSKNVLLKNNLTACIADFGLA---LKFEAGKSAGDTHGQVGTrRYMAPEVLEgAINFQRDAflriDMYAMGLVL 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806145 1279 WELLTR----GAPPYRHIDPF-----------DLTHFLAQGRRLPQPEYCPDS------LYQVMQQCWEADPAVR 1332
Cdd:cd14141   200 WELASRctasDGPVDEYMLPFeeevgqhpsleDMQEVVVHKKKRPVLRECWQKhagmamLCETIEECWDHDAEAR 274
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1185-1287 4.84e-07

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: 53.00  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1185 DLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESF---TVKVADFGLARDIldreyYSVQQHRHARLPVKWMALESLQ 1261
Cdd:cd14198   111 DIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKI-----GHACELREIMGTPEYLAPEILN 185
                          90       100
                  ....*....|....*....|....*.
gi 578806145 1262 TYRFTTKSDVWSFGVLLWELLTRGAP 1287
Cdd:cd14198   186 YDPITTATDMWNIGVIAYMLLTHESP 211
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1087-1289 4.85e-07

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 53.86  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhgEYIDQAQNRIQCAIKSLSRITEMQQVEA--FLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd05622    79 KVIGRGAFGEV---QLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYL-YMVMEY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRS---PQRNPTVkdlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDiLDREYYs 1241
Cdd:cd05622   155 MPGGDLVNLMSNydvPEKWARF-----YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK-MNKEGM- 227
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1242 VQQHRHARLPvKWMALESLQTY----RFTTKSDVWSFGVLLWELLTRGAPPY 1289
Cdd:cd05622   228 VRCDTAVGTP-DYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFY 278
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
1089-1280 5.55e-07

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: 52.81  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIqcAIKSL--------SRITEMQQVEaFLREgllMRGLNHPNVLALIGIMlPPEGLPHV 1160
Cdd:cd14052     8 IGSGEFSQVYKVSERVPTGKVY--AVKKLkpnyagakDRLRRLEEVS-ILRE---LTLDGHDNIVQLIDSW-EYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1161 LLPYMCHGDLLQF-----IRSPQRNPTVKDLIsfgLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLA---- 1231
Cdd:cd14052    81 QTELCENGSLDVFlselgLLGRLDEFRVWKIL---VELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwp 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806145 1232 --RDIL---DREYysvqqhrharlpvkwMALESLQTYRFTTKSDVWSFGVLLWE 1280
Cdd:cd14052   158 liRGIEregDREY---------------IAPEILSEHMYDKPADIFSLGLILLE 196
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1089-1338 5.68e-07

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: 52.93  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIQcAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPpEGLPHVLLPYMCHG 1168
Cdd:cd06622     9 LGKGNYGSVY--KVLHRPTGVTM-AMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFI-EGAVYMCMEYMDAG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKD--LISFGLQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDI---LDREYYSV 1242
Cdd:cd06622    85 SLDKLYAGGVATEGIPEdvLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLvasLAKTNIGC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1243 QQHrhaRLPVKWMALESLQTYRFTTKSDVWSFGVLLWElLTRGAPPYrhiDPFDLTHFLAQGR--------RLPqPEYCP 1314
Cdd:cd06622   165 QSY---MAPERIKSGGPNQNPTYTVQSDVWSLGLSILE-MALGRYPY---PPETYANIFAQLSaivdgdppTLP-SGYSD 236
                         250       260
                  ....*....|....*....|....
gi 578806145 1315 DSlYQVMQQCWEADPAVRPTFRVL 1338
Cdd:cd06622   237 DA-QDFVAKCLNKIPNRRPTYAQL 259
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
1088-1287 5.76e-07

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: 52.69  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQnriQCAIKSLSRITEMQQV-EAFLREGLLMRGLNHPNVLALiGIMLPPEGLPHVLLPYMc 1166
Cdd:cd07848     8 VVGEGAYGVVLKCRHKETKE---IVAIKKFKDSEENEEVkETTLRELKMLRTLKQENIVEL-KEAFRRRGKLYLVFEYV- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDI---LDREYYSVQ 1243
Cdd:cd07848    83 EKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLsegSNANYTEYV 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578806145 1244 QHRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWElLTRGAP 1287
Cdd:cd07848   163 ATRWYRSP------ELLLGAPYGKAVDMWSVGCILGE-LSDGQP 199
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
1163-1349 6.33e-07

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 52.73  E-value: 6.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVK---------------------------DLISFGLQVARGMEYLAEQ-----------K 1204
Cdd:cd14140    44 PGMKHENLLQFIAAEKRGSNLEmelwlitafhdkgsltdylkgnivswnELCHIAETMARGLSYLHEDvprckgeghkpA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1205 FVHRDLAARNCMLDESFTVKVADFGLArdiLDREYYSVQQHRHARLPV-KWMALESLQ-TYRFTTKS----DVWSFGVLL 1278
Cdd:cd14140   124 IAHRDFKSKNVLLKNDLTAVLADFGLA---VRFEPGKPPGDTHGQVGTrRYMAPEVLEgAINFQRDSflriDMYAMGLVL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1279 WELLTR----GAPPYRHIDPF-----------DLTHFLAQGRRLP--------QPEYCpdSLYQVMQQCWEADPAVRPTf 1335
Cdd:cd14140   201 WELVSRckaaDGPVDEYMLPFeeeigqhpsleDLQEVVVHKKMRPvfkdhwlkHPGLA--QLCVTIEECWDHDAEARLS- 277
                         250
                  ....*....|....
gi 578806145 1336 rvlVGEVEQIVSAL 1349
Cdd:cd14140   278 ---AGCVEERISQI 288
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
1089-1303 8.19e-07

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: 52.13  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidQAQNRIQCAIKSLsritemqQVEAFLREGLLM-RGLNHPNVLALIGIMlpPEGlPHVLL--PYM 1165
Cdd:cd13991    14 IGRGSFGEVHRME---DKQTGFQCAVKKV-------RLEVFRAEELMAcAGLTSPRVVPLYGAV--REG-PWVNIfmDLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQRNPtvKDL-ISFGLQVARGMEYLAEQKFVHRDLAARNCML-DESFTVKVADFGLArDILDREYYSVQ 1243
Cdd:cd13991    81 EGGSLGQLIKEQGCLP--EDRaLHYLGQALEGLEYLHSRKILHGDVKADNVLLsSDGSDAFLCDFGHA-ECLDPDGLGKS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1244 QHRHARLP--VKWMALESLQTYRFTTKSDVWSFGVLLWELL------TR------------GAPPYRHIDPfDLTHFLAQ 1303
Cdd:cd13991   158 LFTGDYIPgtETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLngchpwTQyysgplclkianEPPPLREIPP-SCAPLTAQ 236
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1087-1289 9.08e-07

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 52.49  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidQAQNRIQcAIKSLSR--ITEMQQVEAFLREG-LLMRGLNHPNVLALIGIMLPPEGLPHVLlP 1163
Cdd:cd05591     1 KVLGKGSFGKVMLAER--KGTDEVY-AIKVLKKdvILQDDDVDCTMTEKrILALAAKHPFLTALHSCFQTKDRLFFVM-E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLL-QFIRSPQRNPTVKDLisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARD-ILDreyyS 1241
Cdd:cd05591    77 YVNGGDLMfQIQRARKFDEPRARF--YAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILN----G 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1242 VQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05591   151 KTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 196
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
1089-1289 9.24e-07

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: 52.34  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVyhGEYIDQAQNrIQCAIKSL--SRITEMQQVEAFLREGllmrglNHPNVLALIGIMLPPEGLpHVLLPYMC 1166
Cdd:cd14175     9 IGVGSYSVC--KRCVHKATN-MEYAVKVIdkSKRDPSEEIEILLRYG------QHPNIITLKDVYDDGKHV-YLVTELMR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCM-LDESF---TVKVADFGLARDI------LD 1236
Cdd:cd14175    79 GGELLDKILR-QKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGnpeSLRICDFGFAKQLraenglLM 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1237 REYYSVQqhrharlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14175   158 TPCYTAN----------FVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPF 199
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
1165-1308 1.23e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a 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: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 52.34  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARDILDREY 1239
Cdd:cd14229    82 MLEQNLYDFLKQNKFSPLPLKVIRPILQqVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSKTVC 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1240 YSVQQHRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLP 1308
Cdd:cd14229   162 STYLQSRYYRAP------EIILGLPFCEAIDMWSLGCVIAELFL-GWPLYPGALEYDQIRYISQTQGLP 223
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
1088-1334 1.25e-06

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: 51.99  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIdqaqnriqcaiKSLSRITEMQQVEAFL----------REGLLMRGLNHPNVLALIGIMLPPEGL 1157
Cdd:cd14055     2 LVGKGRFAEVWKAKLK-----------QNASGQYETVAVKIFPyeeyaswkneKDIFTDASLKHENILQFLTAEERGVGL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1158 PH---VLLPYMCHGDLLQFIRspqRNP-TVKDLISFGLQVARGMEYL-AE------QKF--VHRDLAARNCMLDESFTVK 1224
Cdd:cd14055    71 DRqywLITAYHENGSLQDYLT---RHIlSWEDLCKMAGSLARGLAHLhSDrtpcgrPKIpiAHRDLKSSNILVKNDGTCV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1225 VADFGLARDiLD-----REYYSVQQHRHARlpvkWMA---LES---LQTYRFTTKSDVWSFGVLLWELLTR-----GAPP 1288
Cdd:cd14055   148 LADFGLALR-LDpslsvDELANSGQVGTAR----YMApeaLESrvnLEDLESFKQIDVYSMALVLWEMASRceasgEVKP 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1289 YRhiDPF--------------DLthfLAQGRRLPQpeyCPDS---------LYQVMQQCWEADPAVRPT 1334
Cdd:cd14055   223 YE--LPFgskvrerpcvesmkDL---VLRDRGRPE---IPDSwlthqgmcvLCDTITECWDHDPEARLT 283
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1089-1289 1.33e-06

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: 51.44  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVyhgEYIDQAQNRIQCAIKSLSRITEMQQveAFLREGLLMRGLNHPNVLALIGIMLPPEGLphVLLPYMCHG 1168
Cdd:cd14108    10 IGRGAFSYL---RRVKEKSSDLSFAAKFIPVRAKKKT--SARRELALLAELDHKSIVRFHDAFEKRRVV--IIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIrspQRNPTV--KDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFT--VKVADFGLARDILDREyysvQQ 1244
Cdd:cd14108    83 ELLERI---TKRPTVceSEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNE----PQ 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1245 HRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14108   156 YCKYGTP-EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLT-GISPF 198
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
1089-1286 1.38e-06

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 51.76  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyiDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPN----VLALIGIMLPPEGLPHVLLPY 1164
Cdd:cd07837     9 IGEGTYGKVYKAR--DKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIyivrLLDVEHVEENGKPLLYLVFEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 McHGDLLQFIRSPQR---NPTVKDLI-SFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTV-KVADFGLARDILdrey 1239
Cdd:cd07837    87 L-DTDLKKFIDSYGRgphNPLPAKTIqSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGRAFT---- 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1240 YSVQQHRHARLPVKWMALES-LQTYRFTTKSDVWSFGVLLWELLTRGA 1286
Cdd:cd07837   162 IPIKSYTHEIVTLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMSRKQP 209
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1159-1289 1.40e-06

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: 51.63  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPYMCHGDLlqFIRSPQRNPTVKDLISF-GLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIL-- 1235
Cdd:cd05583    75 HLILDYVNGGEL--FTHLYQREHFTESEVRIyIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpg 152
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1236 --DREYYSVQQhrharlpVKWMALESLQT----YRFTTksDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05583   153 enDRAYSFCGT-------IEYMAPEVVRGgsdgHDKAV--DWWSLGVLTYELLT-GASPF 202
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
1197-1291 1.44e-06

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 51.45  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1197 MEYLAEQKFVHRDLAARNCMLDESFTVKVADFGlardildreyYSVQQHRHARL-----PVKWMALESLQTYR------F 1265
Cdd:cd14182   123 ICALHKLNIVHRDLKPENILLDDDMNIKLTDFG----------FSCQLDPGEKLrevcgTPGYLAPEIIECSMddnhpgY 192
                          90       100
                  ....*....|....*....|....*.
gi 578806145 1266 TTKSDVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd14182   193 GKEVDMWSTGVIMYTLLA-GSPPFWH 217
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
526-568 1.48e-06

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 46.55  E-value: 1.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578806145   526 GCRHFLTCGRCLRAWhFMGCGWC--GNMCGQQKECPG------SWQQDH--CP 568
Cdd:pfam01437    1 RCSQYTSCSSCLAAR-DPYCGWCssEGRCVRRSACGApegnceEWEQASskCP 52
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1087-1289 1.60e-06

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: 51.94  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEYidQAQNRIQcAIKSLSR--ITEMQQVEAFLRE-GLLMRGLNHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd05602    13 KVIGKGSFGKVLLARH--KSDEKFY-AVKVLQKkaILKKKEEKHIMSErNVLLKNVKHPFLVGLHFSFQTTDKL-YFVLD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQ--RNPTVKdliSFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyYS 1241
Cdd:cd05602    89 YINGGELFYHLQRERcfLEPRAR---FYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE---PN 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578806145 1242 VQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05602   163 GTTSTFCGTP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEMLY-GLPPF 208
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1088-1289 1.60e-06

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: 51.22  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEyiDQAQNRIqCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCH 1167
Cdd:cd14083    10 VLGTGAFSEVVLAE--DKATGKL-VAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHL-YLVMELVTG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1168 GDLlqFIRSPQR-NPTVKD---LISfglQVARGMEYLAEQKFVHRDLAARN---CMLDESFTVKVADFGLARdILDREYY 1240
Cdd:cd14083    86 GEL--FDRIVEKgSYTEKDashLIR---QVLEAVDYLHSLGIVHRDLKPENllyYSPDEDSKIMISDFGLSK-MEDSGVM 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1241 SVqqhrhARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14083   160 ST-----ACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLC-GYPPF 202
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1193-1340 1.75e-06

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: 51.42  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1193 VARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILD---REYYSVQqhrharlpvKWMALESLQTYRFTTKS 1269
Cdd:cd06619   104 VVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNsiaKTYVGTN---------AYMAPERISGEQYGIHS 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1270 DVWSFGVLLWELLTrGAPPYRHID-------PFDLTHFLAQGR--RLPQPEYCPdSLYQVMQQCWEADPAVRPTFRVLVG 1340
Cdd:cd06619   175 DVWSLGISFMELAL-GRFPYPQIQknqgslmPLQLLQCIVDEDppVLPVGQFSE-KFVHFITQCMRKQPKERPAPENLMD 252
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
1088-1291 1.82e-06

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 51.60  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGeyIDQAQNRIQCA-IKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLL 1162
Cdd:cd14040    13 LLGRGGFSEVYKA--FDLYEQRYAAVkIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDTDTFCTVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYmCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQK--FVHRDLAARNCMLDESFT---VKVADFGLARdILDR 1237
Cdd:cd14040    91 EY-CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-IMDD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1238 EYYSVQ--------QHRHARLPVKWMALESlQTYRFTTKSDVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd14040   169 DSYGVDgmdltsqgAGTYWYLPPECFVVGK-EPPKISNKVDVWSVGVIFFQCLY-GRKPFGH 228
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
526-568 2.30e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 45.61  E-value: 2.30e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578806145    526 GCRHFLTCGRCLRAWHFmGCGWC--GNMCGQQKECPGS---WQQDHCP 568
Cdd:smart00423    1 RCSKYTSCSECLLARDP-YCAWCssQGRCTSGERCDSRrqnWLSGGCP 47
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1087-1289 2.47e-06

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: 51.12  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhgeyIDQAQNRIQC-AIKSLSR---ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLL 1162
Cdd:cd05604     2 KVIGKGSFGKVL----LAKRKRDGKYyAVKVLQKkviLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKL-YFVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFIRSPQRNPTVKDLIsFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDReyySV 1242
Cdd:cd05604    77 DFVNGGELFFHLQRERSFPEPRARF-YAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISN---SD 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1243 QQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLtRGAPPY 1289
Cdd:cd05604   153 TTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPF 197
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
1088-1291 2.49e-06

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 51.21  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQaQNRIQCAIKSLSRITEMQQVEAF----LREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLP 1163
Cdd:cd14041    13 LLGRGGFSEVYKAFDLTE-QRYVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YmCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQK--FVHRDLAARNCMLDESFT---VKVADFGLARDILDRE 1238
Cdd:cd14041    92 Y-CEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTAcgeIKITDFGLSKIMDDDS 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806145 1239 YYSVQQHR--------HARLPVKWMALESlQTYRFTTKSDVWSFGVLLWELLTrGAPPYRH 1291
Cdd:cd14041   171 YNSVDGMEltsqgagtYWYLPPECFVVGK-EPPKISNKVDVWSVGVIFYQCLY-GRKPFGH 229
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
1181-1283 2.72e-06

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 51.04  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1181 PTVKDLISfglQVARGMEYLAEQ-KFVHRDLAARNCMLDES-FTVKVADFGLARDIlDREYYSVQQHRHARlpvkwmALE 1258
Cdd:cd14136   119 PLVKKIAR---QVLQGLDYLHTKcGIIHTDIKPENVLLCISkIEVKIADLGNACWT-DKHFTEDIQTRQYR------SPE 188
                          90       100
                  ....*....|....*....|....*
gi 578806145 1259 SLQTYRFTTKSDVWSFGVLLWELLT 1283
Cdd:cd14136   189 VILGAGYGTPADIWSTACMAFELAT 213
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
1087-1290 3.32e-06

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: 50.67  E-value: 3.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYhGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMlppEGLPHVLL--PY 1164
Cdd:cd05607     8 RVLGKGGFGEVC-AVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAF---ETKTHLCLvmSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRS-PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldREYYSVQ 1243
Cdd:cd05607    84 MNGGDLKYHIYNvGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV--KEGKPIT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1244 QHRHARlpvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYR 1290
Cdd:cd05607   162 QRAGTN---GYMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPFR 204
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
1089-1287 3.35e-06

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: 50.62  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDqaqNRIQCAIKSLSRItemqQVEAFLREGLLMRGLN-HPNVLALIGI-MLPPEGLPHVLLPYMC 1166
Cdd:cd14132    26 IGRGKYSEVFEGINIG---NNEKVVIKVLKPV----KKKKIKREIKILQNLRgGPNIVKLLDVvKDPQSKTPSLIFEYVN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1167 HGDLLQFIrspqrnPTVKDL-ISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESF-TVKVADFGLArdildrEYYSVQ 1243
Cdd:cd14132    99 NTDFKTLY------PTLTDYdIRYYMyELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWGLA------EFYHPG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1244 QH-------RHARLPvkwmalESLQTYRFTTKS-DVWSFGVLLWELLTRGAP 1287
Cdd:cd14132   167 QEynvrvasRYYKGP------ELLVDYQYYDYSlDMWSLGCMLASMIFRKEP 212
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
1087-1289 3.36e-06

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 51.16  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhgeyidqAQNRIQC-----AIKSLSRITEMQQVE-AFLRE--GLLMRGlnHPNVLALIGIMLPPEGLP 1158
Cdd:cd05624    78 KVIGRGAFGEV--------AVVKMKNteriyAMKILNKWEMLKRAEtACFREerNVLVNG--DCQWITTLHYAFQDENYL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1159 HVLLPYMCHGDLLQFIrSPQRNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDR 1237
Cdd:cd05624   148 YLVMDYYVGGDLLTLL-SKFEDKLPEDMARFYIgEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDD 226
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578806145 1238 EyySVQQHRHARLPvKWMALESLQTY-----RFTTKSDVWSFGVLLWELLTRGAPPY 1289
Cdd:cd05624   227 G--TVQSSVAVGTP-DYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFY 280
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
1089-1320 4.43e-06

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: 50.00  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQAQNRIQCAI--KSLSRiTEMQQveaFLREGLLMRGLNHPNVLAL-----------IGIMLPPE 1155
Cdd:cd14033     9 IGRGSFKTVYRGLDTETTVEVAWCELqtRKLSK-GERQR---FSEEVEMLKGLQHPNIVRFydswkstvrghKCIILVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1156 glphvllpYMCHGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQ--KFVHRDLAARNCMLD-ESFTVKVADFGLAr 1232
Cdd:cd14033    85 --------LMTSGTLKTYLKR-FREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGLA- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1233 dildreyySVQQHRHARLPV---KWMALESLQTyRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRlpq 1309
Cdd:cd14033   155 --------TLKRASFAKSVIgtpEFMAPEMYEE-KYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIK--- 222
                         250
                  ....*....|.
gi 578806145 1310 peycPDSLYQV 1320
Cdd:cd14033   223 ----PDSFYKV 229
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
1089-1287 4.48e-06

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: 50.63  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGeyIDQAQNRIqCAIK----SLSRITEMQQVeafLREGLLMRGLN-HPNVLALIGIMLPPEGLP-HVLL 1162
Cdd:cd07852    15 LGKGAYGIVWKA--IDKKTGEV-VALKkifdAFRNATDAQRT---FREIMFLQELNdHPNIIKLLNVIRAENDKDiYLVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMcHGDLLQFIRSPQRNPTVKDLISFglQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSV 1242
Cdd:cd07852    89 EYM-ETDLHAVIRANILEDIHKQYIMY--QLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDE 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1243 QQ-------HRHARLPvkwmalESL-QTYRFTTKSDVWSFGVLLWELLtRGAP 1287
Cdd:cd07852   166 NPvltdyvaTRWYRAP------EILlGSTRYTKGVDMWSVGCILGEML-LGKP 211
PHA02988 PHA02988
hypothetical protein; Provisional
1114-1334 4.52e-06

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 50.13  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1114 IKSLSRITEmqqveaflREGLLMRGLNHPNVLALIGIMLP-PEGLPH--VLLPYMCHGDLLQFIRSpQRNPTVKDLISFG 1190
Cdd:PHA02988   58 HKVLIDITE--------NEIKNLRRIDSNNILKIYGFIIDiVDDLPRlsLILEYCTRGYLREVLDK-EKDLSFKTKLDMA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1191 LQVARGMEYLAEQ-KFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHrhARLPVKwMALESLQTYrfTTKS 1269
Cdd:PHA02988  129 IDCCKGLYNLYKYtNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFM--VYFSYK-MLNDIFSEY--TIKD 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806145 1270 DVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLA-QGRRLPQPEYCPDSLYQVMQQCWEADPAVRPT 1334
Cdd:PHA02988  204 DIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIInKNNSLKLPLDCPLEIKCIVEACTSHDSIKRPN 268
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1135-1289 5.26e-06

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: 49.89  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1135 LMRGLNHPNVLALIGIMLPPEGLpHVLLPYMCHGDLlqFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAAR 1213
Cdd:cd14169    54 VLRRINHENIVSLEDIYESPTHL-YLAMELVTGGEL--FDRIIERGSyTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPE 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1214 NCMLDESF---TVKVADFGLARdILDREYYSVQQHRHArlpvkWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14169   131 NLLYATPFedsKIMISDFGLSK-IEAQGMLSTACGTPG-----YVAPELLEQKPYGKAVDVWAIGVISYILLC-GYPPF 202
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
1088-1289 5.57e-06

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: 50.00  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFG---VVyhgeyIDQAQNRIqCAIKSLSRItEM---QQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLpHVL 1161
Cdd:cd05601     8 VIGRGHFGevqVV-----KEKATGDI-YAMKVLKKS-ETlaqEEVSFFEEERDIMAKANSPWITKLQYAFQDSENL-YLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1162 LPYMCHGDLLQFIrSPQRNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldreyy 1240
Cdd:cd05601    80 MEYHPGGDLLSLL-SRYDDIFEESMARFYLaELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKL------ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806145 1241 SVQQHRHARLPV---KWMALESLQTYRFTTKS------DVWSFGVLLWELLTrGAPPY 1289
Cdd:cd05601   153 SSDKTVTSKMPVgtpDYIAPEVLTSMNGGSKGtygvecDWWSLGIVAYEMLY-GKTPF 209
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
1089-1289 6.62e-06

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 49.88  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEYIDQaqNRIQcAIKSLSR--ITEMQQVEAFLRE-GLLMRGL--NHPNVLALIGIMLPPEGLpHVLLP 1163
Cdd:cd05586     1 IGKGTFGQVYQVRKKDT--RRIY-AMKVLSKkvIVAKKEVAHTIGErNILVRTAldESPFIVGLKFSFQTPTDL-YLVTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLLQFIRSPQRNPtvKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLAR-DILDREYYS 1241
Cdd:cd05586    77 YMSGGELFWHLQKEGRFS--EDRAKFYIaELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKaDLTDNKTTN 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1242 VQQHrharlPVKWMALESLQTYR-FTTKSDVWSFGVLLWELLTRGAPPY 1289
Cdd:cd05586   155 TFCG-----TTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFY 198
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
1177-1294 7.18e-06

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 49.18  E-value: 7.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1177 PQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARDILDREYYSVQQHRHA---R 1249
Cdd:cd14017    90 PRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGLARQYTNKDGEVERPPRNAagfR 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1250 LPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDP 1294
Cdd:cd14017   170 GTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVT-GQLPWRKLKD 213
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1089-1289 8.12e-06

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: 49.12  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgEYIDQAQNRIQCAiKSLSRITEMQQvEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPhVLLPYMCHG 1168
Cdd:cd14114    10 LGTGAFGVVH--RCTERATGNNFAA-KFIMTPHESDK-ETVRKEIQIMNQLHHPKLINLHDAFEDDNEMV-LILEFLSGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLD--ESFTVKVADFGLARDILDREYYSVQQHr 1246
Cdd:cd14114    85 ELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKESVKVTTG- 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578806145 1247 harlPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14114   164 ----TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLS-GLSPF 201
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
1086-1339 8.19e-06

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: 49.20  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYhgeYIDQAQNRIQCAIKSLSrITEMQQVEAFLREGLLMRGL-NHPNVLALIG--IMLPPEGLPHVLL 1162
Cdd:cd14037     8 EKYLAEGGFAHVY---LVKTSNGGNRAALKRVY-VNDEHDLNVCKREIEIMKRLsGHKNIVGYIDssANRSGNGVYEVLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 --PYMCHGDLLQFIRspQRnptvkdlISFGLQ--------------VARgMEYLaEQKFVHRDLAARNCMLDESFTVKVA 1226
Cdd:cd14037    84 lmEYCKGGGVIDLMN--QR-------LQTGLTeseilkifcdvceaVAA-MHYL-KPPLIHRDLKVENVLISDSGNYKLC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1227 DFGLARDILDR-----EYYSVQQ--HRHARLPVKwmALESLQTYR---FTTKSDVWSFGVLLWELLTrgappyrHIDPFD 1296
Cdd:cd14037   153 DFGSATTKILPpqtkqGVTYVEEdiKKYTTLQYR--APEMIDLYRgkpITEKSDIWALGCLLYKLCF-------YTTPFE 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1297 LTHFLA-QGRRLPQPEYCP--DSLYQVMQQCWEADPAVRPT-FRVLV 1339
Cdd:cd14037   224 ESGQLAiLNGNFTFPDNSRysKRLHKLIRYMLEEDPEKRPNiYQVSY 270
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
1086-1287 9.60e-06

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: 48.95  E-value: 9.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1086 DRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSlSRITEMQQvEAFLREGLLMRGLNHPNVLALIG---IMLPPEGLPHVLL 1162
Cdd:cd14031    15 DIELGRGAFKTVYKGLDTETWVEVAWCELQD-RKLTKAEQ-QRFKEEAEMLKGLQHPNIVRFYDsweSVLKGKKCIVLVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1163 PYMCHGDLLQFI-RSPQRNPTVkdLISFGLQVARGMEYLAEQK--FVHRDLAARNCMLD-ESFTVKVADFGLArdILDRE 1238
Cdd:cd14031    93 ELMTSGTLKTYLkRFKVMKPKV--LRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLMRT 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578806145 1239 YYSvqqhRHARLPVKWMALESLQTYrFTTKSDVWSFGVLLWELLTRGAP 1287
Cdd:cd14031   169 SFA----KSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYP 212
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
1205-1289 1.17e-05

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: 49.24  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1205 FVHRDLAARNCMLDESFTVKVADFGLA---RDILDREYYsvQQHRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWEL 1281
Cdd:cd05598   122 FIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYY--LAHSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEM 198

                  ....*...
gi 578806145 1282 LTrGAPPY 1289
Cdd:cd05598   199 LV-GQPPF 205
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
1134-1289 1.32e-05

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: 48.86  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1134 LLMRGLNHPNVLALIGIMlpPEG-LPHVLLPYMCHGDLLQFIRSpQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAA 1212
Cdd:cd14177    50 ILMRYGQHPNIITLKDVY--DDGrYVYLVTELMKGGELLDRILR-QKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKP 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1213 RNCM-LDESF---TVKVADFGLARDILDREYYSVQQHRHArlpvKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPP 1288
Cdd:cd14177   127 SNILyMDDSAnadSIRICDFGFAKQLRGENGLLLTPCYTA----NFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTP 201

                  .
gi 578806145 1289 Y 1289
Cdd:cd14177   202 F 202
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1088-1289 1.37e-05

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: 48.45  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1088 VIGKGHFGVVYHGEYIDQAQN-RIQCAIKS-LSRITEMQQVEAFLREgllmrgLNHPNVLALIGIMlppEGLPH--VLLP 1163
Cdd:cd14166    10 VLGSGAFSEVYLVKQRSTGKLyALKCIKKSpLSRDSSLENEIAVLKR------IKHENIVTLEDIY---ESTTHyyLVMQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1164 YMCHGDLlqFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML---DESFTVKVADFGLARdildrey 1239
Cdd:cd14166    81 LVSGGEL--FDRILERGVyTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK------- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1240 ysVQQH---RHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTrGAPPY 1289
Cdd:cd14166   152 --MEQNgimSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLC-GYPPF 201
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
1132-1280 1.45e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 49.12  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1132 EGLLMRGLNHPNVLALIGIMlPPEGLPHVLLPYMcHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLA 1211
Cdd:PHA03211  210 EARLLRRLSHPAVLALLDVR-VVGGLTCLVLPKY-RSDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIK 287
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1212 ARNCMLDESFTVKVADFGLArdILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWE 1280
Cdd:PHA03211  288 TENVLVNGPEDICLGDFGAA--CFARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFE 354
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
1165-1308 1.91e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 48.55  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARDILDREY 1239
Cdd:cd14228    97 MLEQNLYDFLKQNKFSPlPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSKAVC 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1240 YSVQQHRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLP 1308
Cdd:cd14228   177 STYLQSRYYRAP------EIILGLPFCEAIDMWSLGCVIAELFL-GWPLYPGASEYDQIRYISQTQGLP 238
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1089-1289 1.96e-05

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 48.28  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYHGEyidQAQNRIQCAIKSLSRITEMQQVEAFLreGLLMRgLNHPNVLALIGIMLPPEGLpHVLLPYMCHG 1168
Cdd:cd14085    11 LGRGATSVVYRCR---QKGTQKPYAVKKLKKTVDKKIVRTEI--GVLLR-LSHPNIIKLKEIFETPTEI-SLVLELVTGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1169 DLlqFIRSPQRNP-TVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCM---LDESFTVKVADFGLARdILDREyysVQQ 1244
Cdd:cd14085    84 EL--FDRIVEKGYySERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSK-IVDQQ---VTM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578806145 1245 HRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPY 1289
Cdd:cd14085   158 KTVCGTP-GYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFY 201
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1089-1294 2.03e-05

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: 48.10  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1089 IGKGHFGVVYhgeyidQAQNrIQCAIKSLSRITEMQQVEAF---LREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPYm 1165
Cdd:cd06646    17 VGSGTYGDVY------KARN-LHTGELAAVKIIKLEPGDDFsliQQEIFMVKECKHCNIVAYFGSYLSREKL-WICMEY- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1166 CHGDLLQFIRSPQrNPTVKDLISFGL-QVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILdreyYSVQQ 1244
Cdd:cd06646    88 CGGGSLQDIYHVT-GPLSELQIAYVCrETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKIT----ATIAK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578806145 1245 HRHARLPVKWMALESLQTYR---FTTKSDVWSFGVLLWElLTRGAPPYRHIDP 1294
Cdd:cd06646   163 RKSFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGITAIE-LAELQPPMFDLHP 214
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1087-1289 2.16e-05

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: 48.46  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVyhgEYIDQAQNRIQCAIKSLSRITEMQQVEA--FLREGLLMRGLNHPNVLALIGIMLPPEGLpHVLLPY 1164
Cdd:cd05621    58 KVIGRGAFGEV---QLVRHKASQKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFCAFQDDKYL-YMVMEY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRS---PQRNPTVkdlisFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDIldREYYS 1241
Cdd:cd05621   134 MPGGDLVNLMSNydvPEKWAKF-----YTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKM--DETGM 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578806145 1242 VQQHRHARLPvKWMALESLQTY----RFTTKSDVWSFGVLLWELLTRGAPPY 1289
Cdd:cd05621   207 VHCDTAVGTP-DYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFY 257
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
1087-1291 2.30e-05

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: 48.12  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1087 RVIGKGHFGVVYHGEyiDQAQNRIQcAIKSLSR--ITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLlPY 1164
Cdd:cd05571     1 KVLGKGTFGKVILCR--EKATGELY-AIKILKKevIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVM-EY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLqFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDreyYSVQQ 1244
Cdd:cd05571    77 VNGGELF-FHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEIS---YGATT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578806145 1245 HRHARLPvKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRH 1291
Cdd:cd05571   153 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNR 198
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
1165-1308 2.32e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 48.16  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145 1165 MCHGDLLQFIRSPQRNPTVKDLISFGLQ-VARGMEYLAEQKFVHRDLAARNCML----DESFTVKVADFGLARDILDREY 1239
Cdd:cd14227    97 MLEQNLYDFLKQNKFSPLPLKYIRPILQqVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASHVSKAVC 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806145 1240 YSVQQHRHARLPvkwmalESLQTYRFTTKSDVWSFGVLLWELLTrGAPPYRHIDPFDLTHFLAQGRRLP 1308
Cdd:cd14227   177 STYLQSRYYRAP------EIILGLPFCEAIDMWSLGCVIAELFL-GWPLYPGASEYDQIRYISQTQGLP 238
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
770-862 9.44e-05

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 42.45  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  770 PVVLSISPNCGYIN--SHITICGQHLTSAWHLVLSFHDGLRAVESRQCERQLpeqqLCRLPEYvvrDPQGWVAGNLSARG 847
Cdd:cd00102     1 PVITSISPSSGPVSggTEVTITGSNFGSGSNLRVTFGGGVPCSVLSVSSTAI----VCTTPPY---ANPGPGPVEVTVDR 73
                          90
                  ....*....|....*.
gi 578806145  848 DGAAGFTLP-GFRFLP 862
Cdd:cd00102    74 GNGGITSSPlTFTYVP 89
IPT_PCSR cd00603
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
770-860 1.05e-04

IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238337 [Multi-domain]  Cd Length: 90  Bit Score: 42.44  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145  770 PVVLSISPNCGYI--NSHITICGQHLTSAWHLVLSFhdglraVESRQCE--RQLPEQQLCRLPEYVvrdPQGWVAGNLSA 845
Cdd:cd00603     1 PVITSISPSSGPLsgGTRLTITGSNLGSGSPRVRVT------VGGVPCKvlNVSSTEIVCRTPAAA---TPGEGPVEVTV 71
                          90
                  ....*....|....*
gi 578806145  846 RGDGAAGFTLPGFRF 860
Cdd:cd00603    72 DGANVSARVLSNTTF 86
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
569-661 1.29e-04

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 42.05  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806145   569 PKLTEFHPHSGPLRGSTRLTLCGSNFylhpsGLVPEGThQVTVGQSPCRPLPKDSSKLRpvprkdfveefeCELEPLgtq 648
Cdd:pfam01833    1 PVITSISPSSGPASGGTTITITGSNF-----GTDSSDL-KVTIGGTPCTVISVSSTTIV------------CTTPPG--- 59
                           90
                   ....*....|...
gi 578806145   649 AVGPTNVSLTVTN 661
Cdd:pfam01833   60 TSGLVNVSVTVGG 72
 
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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