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Conserved domains on  [gi|759191595|ref|XP_011383030|]
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angiopoietin-1 receptor isoform X3 [Pteropus vampyrus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
669-971 0e+00

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: 630.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 669 YPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHR 748
Cdd:cd05088    1 YPVLEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05088   81 GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05088  161 YVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDC 971
Cdd:cd05088  241 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDC 303
IgI_Tie2 cd20964
Immunoglobulin domain of Tie2 tyrosine kinase; a member of the I-set of IgSF domains; The ...
201-292 8.73e-57

Immunoglobulin domain of Tie2 tyrosine kinase; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain of Tie2 tyrosine kinase. The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Tie2 contains three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Tie2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


:

Pssm-ID: 409556  Cd Length: 92  Bit Score: 190.19  E-value: 8.73e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 201 MTPKIEDLPDHIEVNSGKFNPICKASGWPLPANEEMTLVKPDGTVLHPKDFNHTGHLSVATFTIHRILPPDSGVWVCSVN 280
Cdd:cd20964    1 MPPKIDDLPDHEEVNSGKFNPICKASGWPLPVNEEMTLVKPDGTVLHPKDFNHTPHRSVAEFTIHRLLPPDSGVWVCSVN 80
                         90
                 ....*....|..
gi 759191595 281 TVAGMVEKPFNI 292
Cdd:cd20964   81 TVAGMVEKPFNI 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
493-585 2.00e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 493 PPQPENIKISNITDSTAMISWTILDGysISSIIIRYKIQ--GKNEDQHIDVKIKNATITQYQLKGLEPQTVYQVDIFAEN 570
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPED--DGGPITGYVVEyrEKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                         90
                 ....*....|....*
gi 759191595 571 NIGSSNPTFSHELTT 585
Cdd:cd00063   79 GGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
397-480 2.24e-15

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.06  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRAR-VNTKA 475
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQaVNGGG 80

                  ....*
gi 759191595  476 QGEWS 480
Cdd:pfam00041  81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
298-373 7.85e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 7.85e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595  298 PKPLNaPNVIDTGHNFAVINISsEPYFGDGPIKSKKLLYKPVNHYEAWRQIQVTNEI--VTLNYLEPRTEYELCVQLV 373
Cdd:pfam00041   1 SAPSN-LTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAV 76
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
126-171 4.74e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 47.35  E-value: 4.74e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 759191595 126 NGVCHEDTGECICPPGFMGRTCEKaCELHTFGRTckercSGPEGCK 171
Cdd:cd00055   11 SGQCDPGTGQCECKPNTTGRRCDR-CAPGYYGLP-----SQGGGCQ 50
 
Name Accession Description Interval E-value
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
669-971 0e+00

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: 630.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 669 YPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHR 748
Cdd:cd05088    1 YPVLEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05088   81 GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05088  161 YVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDC 971
Cdd:cd05088  241 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDC 303
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
677-945 5.04e-125

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: 5.04e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   677 IKFQDVIGEGNFGQVLKARIK--KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKgkGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   755 IEYAPHGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:smart00221  80 MEYMPGGDLLDYLRKNR--------------PKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   835 DFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:smart00221 146 DFGLSRdlYDDDYYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPK 225
                          250       260       270
                   ....*....|....*....|....*....|...
gi 759191595   913 PLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:smart00221 226 PPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
677-945 1.40e-123

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: 376.07  E-value: 1.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  677 IKFQDVIGEGNFGQVLKARIK--KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKgeGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  755 IEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHK---------------RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKIS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  835 DFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLE 911
Cdd:pfam07714 145 DFGLSRdiyDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 759191595  912 KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:pfam07714 225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
IgI_Tie2 cd20964
Immunoglobulin domain of Tie2 tyrosine kinase; a member of the I-set of IgSF domains; The ...
201-292 8.73e-57

Immunoglobulin domain of Tie2 tyrosine kinase; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain of Tie2 tyrosine kinase. The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Tie2 contains three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Tie2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409556  Cd Length: 92  Bit Score: 190.19  E-value: 8.73e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 201 MTPKIEDLPDHIEVNSGKFNPICKASGWPLPANEEMTLVKPDGTVLHPKDFNHTGHLSVATFTIHRILPPDSGVWVCSVN 280
Cdd:cd20964    1 MPPKIDDLPDHEEVNSGKFNPICKASGWPLPVNEEMTLVKPDGTVLHPKDFNHTPHRSVAEFTIHRLLPPDSGVWVCSVN 80
                         90
                 ....*....|..
gi 759191595 281 TVAGMVEKPFNI 292
Cdd:cd20964   81 TVAGMVEKPFNI 92
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
681-952 1.11e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 130.13  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARikKDGLRMDAAIKRMKEYASKDDH--RDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:COG0515   13 RLLGRGGMGVVYLAR--DLRLGRPVALKVLRPELAADPEarERFRREARALARL-NHPNIVRVYDVGEEDGRPYLVMEYV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:COG0515   90 EGESLADLLRRRG----------------PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRGQEVYVKKTMGRLP--VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRL---EKP 913
Cdd:COG0515  154 ARALGGATLTQTGTVVgtPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPppsELR 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERP-SFAQILVSLNRMLEER 952
Cdd:COG0515  233 PDLPPALDAIVLRALAKDPEERYqSAAELAAALRAVLRSL 272
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
493-585 2.00e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 493 PPQPENIKISNITDSTAMISWTILDGysISSIIIRYKIQ--GKNEDQHIDVKIKNATITQYQLKGLEPQTVYQVDIFAEN 570
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPED--DGGPITGYVVEyrEKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                         90
                 ....*....|....*
gi 759191595 571 NIGSSNPTFSHELTT 585
Cdd:cd00063   79 GGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
397-480 2.24e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.06  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRAR-VNTKA 475
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQaVNGGG 80

                  ....*
gi 759191595  476 QGEWS 480
Cdd:pfam00041  81 EGPPS 85
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
683-942 2.40e-15

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 78.26  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDD---HRDFAG----------ELEVLCKLgHHPNIINLLGACEHRG 749
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTG--KIVAIKKVKIIEISNDvtkDRQLVGmcgihfttlrELKIMNEI-KHENIMGLVDVYVEGD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYApHGNLldflrkSRVLETDPAFAIANSTASTLssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:PTZ00024  94 FINLVMDIM-ASDL------KKVVDRKIRLTESQVKCILL---QIL-------NGLNVLHKWYFMHRDLSPANIFINSKG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSR--GQEVYVKKTMG-------------------RLPVRWMAIESLNYSVyttnsDVWSYGVLLWE----- 883
Cdd:PTZ00024 157 ICKIADFGLARryGYPPYSDTLSKdetmqrreemtskvvtlwyRAPELLMGAEKYHFAV-----DMWSVGCIFAElltgk 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 884 --------------IVSLGGTP-------------YCGMTCAElyeklPQGYRLEKPLNCDDEVyDLMRQCWREKPYERP 936
Cdd:PTZ00024 232 plfpgeneidqlgrIFELLGTPnednwpqakklplYTEFTPRK-----PKDLKTIFPNASDDAI-DLLQSLLKLNPLERI 305

                 ....*.
gi 759191595 937 SFAQIL 942
Cdd:PTZ00024 306 SAKEAL 311
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
493-575 1.59e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.57  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   493 PPQPENIKISNITDSTAMISWTILDGYSISSIIIRYKIQGKNEDQHIDVKIKNATITQYQLKGLEPQTVYQVDIFAENNI 572
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                   ...
gi 759191595   573 GSS 575
Cdd:smart00060  81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
494-578 3.49e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  494 PQPENIKISNITDSTAMISWTILDGYS--ISSIIIRYKIQGKNE-DQHIDVKiknATITQYQLKGLEPQTVYQVDIFAEN 570
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNSGEpWNEITVP---GTTTSVTLTGLKPGTEYEVRVQAVN 77

                  ....*...
gi 759191595  571 NIGSSNPT 578
Cdd:pfam00041  78 GGGEGPPS 85
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
681-840 2.04e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.43  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKArikKDgLRMD--AAIKRMK-EYASKDD-HRDF------AGELEvlcklghHPNIINLLGACEHRGY 750
Cdd:NF033483  13 ERIGRGGMAEVYLA---KD-TRLDrdVAVKVLRpDLARDPEfVARFrreaqsAASLS-------HPNIVSVYDVGEDGGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRVLetdpafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:NF033483  82 PYIVMEYVDGRTLKDYIREHGPL----------------SPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR 145
                        170
                 ....*....|
gi 759191595 831 AKIADFGLSR 840
Cdd:NF033483 146 VKVTDFGIAR 155
fn3 pfam00041
Fibronectin type III domain;
298-373 7.85e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 7.85e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595  298 PKPLNaPNVIDTGHNFAVINISsEPYFGDGPIKSKKLLYKPVNHYEAWRQIQVTNEI--VTLNYLEPRTEYELCVQLV 373
Cdd:pfam00041   1 SAPSN-LTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAV 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
397-487 1.07e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRAR-VNTKA 475
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGGG 81
                         90
                 ....*....|..
gi 759191595 476 QGEWSEDLTAWT 487
Cdd:cd00063   82 ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
397-475 7.45e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 7.45e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595   397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRARVNTKA 475
Cdd:smart00060   2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
126-171 4.74e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 47.35  E-value: 4.74e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 759191595 126 NGVCHEDTGECICPPGFMGRTCEKaCELHTFGRTckercSGPEGCK 171
Cdd:cd00055   11 SGQCDPGTGQCECKPNTTGRRCDR-CAPGYYGLP-----SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
126-170 5.21e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 44.22  E-value: 5.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 759191595   126 NGVCHEDTGECICPPGFMGRTCEKaCELHTFGRTckercsgPEGC 170
Cdd:smart00180  10 SGTCDPDTGQCECKPNVTGRRCDR-CAPGYYGDG-------PPGC 46
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
223-294 8.40e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 8.40e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595   223 CKASGWPLPaneEMTLVKPDGTVLHPKD-FNHTGHLSVATFTIHRILPPDSGVWVCSVNTVAGMVEKPFNISV 294
Cdd:smart00410  16 CEASGSPPP---EVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
669-971 0e+00

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: 630.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 669 YPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHR 748
Cdd:cd05088    1 YPVLEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05088   81 GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05088  161 YVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDC 971
Cdd:cd05088  241 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDC 303
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
681-950 0e+00

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: 592.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd05047   81 GNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd05047  161 GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 921 YDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd05047  241 YDLMRQCWREKPYERPSFAQILVSLNRMLE 270
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
674-970 0e+00

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: 568.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 674 WNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd05089    1 WEDIKFEDVIGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05089   81 AIEYAPYGNLLDFLRKSRVLETDPAFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKP 913
Cdd:cd05089  161 ADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGID 970
Cdd:cd05089  241 RNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKAYVNMALFENFTYAGID 297
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
681-945 2.94e-132

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: 398.84  E-value: 2.94e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIK-KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHhPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKgGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGH-PNVVRLLGVCTEEEPLYLVMEYME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAFaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd00192   80 GGDLLDFLRKSRPVFPSPEP-------STLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNC 916
Cdd:cd00192  153 RdiyDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENC 232
                        250       260
                 ....*....|....*....|....*....
gi 759191595 917 DDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd00192  233 PDELYELMLSCWQLDPEDRPTFSELVERL 261
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
677-945 5.04e-125

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: 5.04e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   677 IKFQDVIGEGNFGQVLKARIK--KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKgkGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   755 IEYAPHGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:smart00221  80 MEYMPGGDLLDYLRKNR--------------PKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   835 DFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:smart00221 146 DFGLSRdlYDDDYYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPK 225
                          250       260       270
                   ....*....|....*....|....*....|...
gi 759191595   913 PLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:smart00221 226 PPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
677-945 9.84e-125

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 378.80  E-value: 9.84e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   677 IKFQDVIGEGNFGQVLKARIK--KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKgkGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   755 IEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:smart00219  80 MEYMEGGDLLSYLRKNR---------------PKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   835 DFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:smart00219 145 DFGLSRdlYDDDYYRKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQ 224
                          250       260       270
                   ....*....|....*....|....*....|...
gi 759191595   913 PLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:smart00219 225 PPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
677-945 1.40e-123

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: 376.07  E-value: 1.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  677 IKFQDVIGEGNFGQVLKARIK--KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKgeGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  755 IEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHK---------------RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKIS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  835 DFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLE 911
Cdd:pfam07714 145 DFGLSRdiyDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 759191595  912 KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:pfam07714 225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
683-949 4.78e-112

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: 347.10  E-value: 4.78e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARI----KKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05053   20 LGEGAFGQVVKAEAvgldNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVVVEYA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05053  100 SKGNLREFLRARRPPGEEASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLN 915
Cdd:cd05053  180 ARDihhIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMEKPQN 259
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 916 CDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05053  260 CTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRIL 293
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
683-949 8.74e-87

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: 281.08  E-value: 8.74e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKAR---IKKDglRMD----AAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd05099   20 LGEGCFGQVVRAEaygIDKS--RPDqtvtVAVKMLKDNATDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPLYVIV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05099   98 EYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIAD 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRGQ---EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:cd05099  178 FGLARGVhdiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEELFKLLREGHRMDK 257
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 913 PLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05099  258 PSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
682-952 5.64e-86

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: 278.00  E-value: 5.64e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKA---RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05045    7 TLGEGEFGKVVKAtafRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQV-NHPHVIKLYGACSQDGPLLLIVEYA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPAFAIANSTAST--------LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05045   86 KYGSLRSFLRESRKVGPSYLGSDGNRNSSYldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQG 907
Cdd:cd05045  166 MKISDFGLSRDvyeEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFNLLKTG 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 908 YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEER 952
Cdd:cd05045  246 YRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMMVKS 290
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
683-949 1.71e-83

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: 272.27  E-value: 1.71e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKAR---IKKDGLR--MDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd05101   32 LGEGCFGQVVMAEavgIDKDKPKeaVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEY 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd05101  112 ASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05101  192 LARdinNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA 271
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05101  272 NCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
683-945 1.96e-83

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: 269.70  E-value: 1.96e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDN--TEVAVKTCRETLPPDLKRKFLQEARIL-KQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd05041   80 LLTFLRKK---------------GARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 843 E--VY-VKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDE 919
Cdd:cd05041  145 EdgEYtVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEA 224
                        250       260
                 ....*....|....*....|....*.
gi 759191595 920 VYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05041  225 VYRLMLQCWAYDPENRPSFSEIYNEL 250
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
665-949 3.10e-83

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: 270.90  E-value: 3.10e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 665 DPTIYPV-LDW----NDIKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHP 736
Cdd:cd05055   20 DPTQLPYdLKWefprNNLSFGKTLGAGAFGKVVEATaygLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLGNHE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 737 NIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHR 816
Cdd:cd05055  100 NIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKR--------------ESFLTLEDLLSFSYQVAKGMAFLASKNCIHR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 817 DLAARNILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYC 893
Cdd:cd05055  166 DLAARNVLLTHGKIVKICDFGLARdimNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYP 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 894 GMTC-AELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05055  246 GMPVdSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
683-970 1.42e-82

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: 270.35  E-value: 1.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKAR---IKKD--GLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd05100   20 LGEGCFGQVVMAEaigIDKDkpNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd05100  100 ASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05100  180 LARdvhNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKT--YVNTTL-YEKFTYAGID 970
Cdd:cd05100  260 NCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTSTdeYLDLSVpFEQYSPGCPD 318
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
683-939 1.31e-81

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: 264.53  E-value: 1.31e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdglRMDAAIKRMKEYASKDDhrDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd05034    3 LGAGQFGEVWMGVWNG---TTKVAVKTLKPGTMSPE--AFLQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVTELMSKGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd05034   77 LLDYLR--------------TGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 843 E--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd05034  143 EddEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDEL 222
                        250
                 ....*....|....*....
gi 759191595 921 YDLMRQCWREKPYERPSFA 939
Cdd:cd05034  223 YDIMLQCWKKEPEERPTFE 241
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
683-949 2.37e-81

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: 266.11  E-value: 2.37e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARI-----KKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd05098   21 LGEGCFGQVVLAEAigldkDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd05098  101 ASKGNLREYLQARRPPGMEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRGQ---EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05098  181 LARDIhhiDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPS 260
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05098  261 NCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIV 295
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
683-950 9.11e-78

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: 254.58  E-value: 9.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIK-KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLyLAIEYAPHG 761
Cdd:cd05060    3 LGHGNFGSVRKGVYLmKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQL-DHPCIVRLIGVCKGEPLM-LVMELAPLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRVletdpafaIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR- 840
Cdd:cd05060   81 PLLKYLKKRRE--------IPVSDLKELAHQ--------VAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRa 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 ---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCD 917
Cdd:cd05060  145 lgaGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECP 224
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 918 DEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd05060  225 QEIYSIMLSCWKYRPEDRPTFSELESTFRRDPE 257
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
677-941 5.16e-77

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: 253.95  E-value: 5.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGAC-EHRGYLY 752
Cdd:cd05054    9 LKLGKPLGRGAFGKVIQASafgIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGACtKPGGPLM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSR---VLETD-------PAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARN 822
Cdd:cd05054   89 VIVEFCKFGNLSNYLRSKReefVPYRDkgardveEEEDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAE 899
Cdd:cd05054  169 ILLSENNVVKICDFGLARdiyKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQMDE 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 900 -LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05054  249 eFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSEL 291
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
675-947 2.38e-76

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: 250.73  E-value: 2.38e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLrmdaAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:cd05039    6 KDLKLGELIGKGEFGDVMLGDYRGQKV----AVKCLKDDSTAAQA--FLAEASVMTTL-RHPNLVQLLGVVLEGNGLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRkSRvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd05039   79 TEYMAKGSLVDYLR-SR-------------GRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRgqEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05039  145 DFGLAK--EASSNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPE 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNR 947
Cdd:cd05039  223 GCPPEVYKVMKNCWELDPAKRPTFKQLREKLEH 255
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
672-938 6.34e-73

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: 241.54  E-value: 6.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDglrMDAAIKRMKeyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd05068    5 IDRKSLKLLRKLGSGQFGEVWEGLWNNT---TPVAVKTLK--PGTMDPEDFLREAQIMKKL-RHPKLIQLYAVCTLEEPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05068   79 YIITELMKHGSLLEYLQGK---------------GRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNIC 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05068  144 KVADFGLARvikVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGY 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd05068  224 RMPCPPNCPPQLYDIMLECWKADPMERPTF 253
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
676-941 6.22e-72

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: 239.58  E-value: 6.22e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARI---KKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd05048    6 AVRFLEELGEGAFGKVYKGELlgpSSEESAISVAIKTLKENASPKTQQDFRREAELMSDL-QHPNIVCLLGVCTKEQPQC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLrKSRVLETDPAFAIANS-TASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05048   85 MLFEYMAHGDLHEFL-VRHSPHSDVGVSSDDDgTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRgqEVY-------VKKTMgrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKL 904
Cdd:cd05048  164 KISDFGLSR--DIYssdyyrvQSKSL--LPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMI 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 905 PQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05048  240 RSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
672-945 2.17e-71

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: 238.01  E-value: 2.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQV---LKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHR 748
Cdd:cd05032    3 LPREKITLIRELGQGSFGMVyegLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVM-KEFNCHHVVRLLGVVSTG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRVLETDpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05032   82 QPTLVVMELMAKGDLKSYLRSRRPEAEN------NPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAED 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLP 905
Cdd:cd05032  156 LTVKIGDFGMTRDiyeTDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVI 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 906 QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05032  236 DGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSL 275
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
672-949 2.49e-71

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: 237.27  E-value: 2.49e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLR-MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY 750
Cdd:cd05033    1 IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKeIDVAIKTLKSGYSDKQRLDFLTEASIMGQF-DHPNVIRLEGVVTKSRP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05033   80 VMIVTEYMENGSLDKFLREND---------------GKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRGQE----VYVKKTmGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 906
Cdd:cd05033  145 CKVSDFGLSRRLEdseaTYTTKG-GKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVED 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 907 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05033  224 GYRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKMI 266
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
672-948 2.73e-71

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: 236.93  E-value: 2.73e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDhrDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd05052    3 IERTDITMKHKLGGGQYGEVYEGVWKKYNLTV--AVKTLKEDTMEVE--EFLKEAAVMKEI-KHPNLVQLLGVCTREPPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRksrvlETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05052   78 YIITEFMPYGNLLDYLR-----ECNR---------EELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05052  144 KVADFGLSRlmTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYR 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd05052  224 MERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
665-949 3.86e-71

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: 240.90  E-value: 3.86e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 665 DPTIYPVLD-W----NDIKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHP 736
Cdd:cd05106   23 DPTQLPYNEkWefprDNLQFGKTLGAGAFGKVVEATafgLGKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLGQHK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 737 NIINLLGACEHRGYLYLAIEYAPHGNLLDFLRK-------------------------------------------SRVL 773
Cdd:cd05106  103 NIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKkaetflnfvmalpeisetssdyknitlekkyirsdsgfssqgsDTYV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 774 ETDPAFAIANSTASTLSSQQ-----------LLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd05106  183 EMRPVSSSSSQSSDSKDEEDtedswpldlddLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARdi 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 -GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTC-AELYEKLPQGYRLEKPLNCDD 918
Cdd:cd05106  263 mNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILVnSKFYKMVKRGYQMSRPDFAPP 342
                        330       340       350
                 ....*....|....*....|....*....|.
gi 759191595 919 EVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05106  343 EIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
681-941 4.57e-71

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: 236.06  E-value: 4.57e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKdglRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05085    2 ELLGKGNFGEVYKGTLKD---KTPVAVKTCKEDLPQELKIKFLSEARIL-KQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd05085   78 GDFLSFLRKKK---------------DELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDD 918
Cdd:cd05085  143 QEDdgVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPE 222
                        250       260
                 ....*....|....*....|...
gi 759191595 919 EVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05085  223 DIYKIMQRCWDYNPENRPKFSEL 245
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
672-945 6.58e-71

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 235.81  E-value: 6.58e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKdglRMDAAIKRMKEYASKDDhrDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd05059    1 IDPSELTFLKELGSGQFGVVHLGKWRG---KIDVAIKMIKEGSMSED--DFIEEAKVMMKL-SHPKLVQLYGVCTKQRPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSRVLetdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05059   75 FIVTEYMANGCLLNYLRERRGK---------------FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRG--QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05059  140 KVSDFGLARYvlDDEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYR 219
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05059  220 LYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
675-947 5.04e-70

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: 234.92  E-value: 5.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVL--KARIKKDGLRMD------------AAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIIN 740
Cdd:cd05051    5 EKLEFVEKLGEGQFGEVHlcEANGLSDLTSDDfigndnkdepvlVAVKMLRPDASKNAREDFLKEVKIMSQL-KDPNIVR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 741 LLGACEHRGYLYLAIEYAPHGNLLDFLRKsRVLETDPAFAIAnstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAA 820
Cdd:cd05051   84 LLGVCTRDEPLCMIVEYMENGDLNQFLQK-HEAETQGASATN---SKTLSYGTLLYMATQIASGMKYLESLNFVHRDLAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 821 RNILVGENYVAKIADFGLSRgqEVYVK---KTMGR--LPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGG-TPYCG 894
Cdd:cd05051  160 RNCLVGPNYTIKIADFGMSR--NLYSGdyyRIEGRavLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKeQPYEH 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 895 MTCAELYEKLPQGYR-------LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNR 947
Cdd:cd05051  238 LTDEQVIENAGEFFRddgmevyLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQR 297
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
675-947 1.47e-69

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 233.19  E-value: 1.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARikKDGLRMD-----AAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRG 749
Cdd:cd05050    5 NNIEYVRDIGQGAFGRVFQAR--APGLLPYepftmVAVKMLKEEASADMQADFQREAALMAEF-DHPNIVKLLGVCAVGK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHGNLLDFLRK------SRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNI 823
Cdd:cd05050   82 PMCLLFEYMAYGDLNEFLRHrspraqCSLSHSTSSARKCGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL 900
Cdd:cd05050  162 LVGENMVVKIADFGLSRniySADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEEV 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 901 YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNR 947
Cdd:cd05050  242 IYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
676-946 3.12e-69

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: 231.97  E-value: 3.12e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd05049    6 TIVLKRELGEGAFGKVFLGEcynLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNL-QHENIVKFYGVCTEGDPLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSrvlETDPAFAIANSTAST-LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05049   85 MVFEYMEHGDLNKFLRSH---GPDAAFLASEDSAPGeLTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRgqEVYVK-------KTMgrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKL 904
Cdd:cd05049  162 KIGDFGMSR--DIYSTdyyrvggHTM--LPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECI 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 905 PQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd05049  238 TQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
683-951 9.59e-69

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 230.66  E-value: 9.59e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMK-EYASKDDHRDFAGElEVLCKLGHHPNIINLLGAC----EHRGYL--YLAI 755
Cdd:cd05075    8 LGEGEFGSVMEGQLNQDDSVLKVAVKTMKiAICTRSEMEDFLSE-AVCMKEFDHPNVMRLIGVClqntESEGYPspVVIL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRVLETdPAFaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05075   87 PFMKHGDLHSFLLYSRLGDC-PVY---------LPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:cd05075  157 FGLSKkiyNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQ 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 913 PLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEE 951
Cdd:cd05075  237 PPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
677-945 1.25e-68

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: 232.59  E-value: 1.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGAC-EHRGYLY 752
Cdd:cd14207    9 LKLGKSLGRGAFGKVVQASafgIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGACtKSGGPLM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSR---VLETDPAFAI------------------------ANSTAST----------------- 788
Cdd:cd14207   89 VIVEYCKYGNLSNYLKSKRdffVTNKDTSLQEelikekkeaeptggkkkrlesvtsSESFASSgfqedkslsdveeeeed 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 789 --------LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG---QEVYVKKTMGRLPVRW 857
Cdd:cd14207  169 sgdfykrpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDiykNPDYVRKGDARLPLKW 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 858 MAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAE-LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERP 936
Cdd:cd14207  249 MAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIDEdFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERP 328

                 ....*....
gi 759191595 937 SFAQILVSL 945
Cdd:cd14207  329 RFSELVERL 337
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
683-945 1.36e-68

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 228.96  E-value: 1.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrmDAAIKRMKEYASKDDH-RDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd13999    1 IGSGSFGEVYKGKWRGT----DVAIKKLKVEDDNDELlKEFRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd13999   76 SLYDLLHKKK---------------IPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 QEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAEL-YEKLPQGYRLEKPLNCDDE 919
Cdd:cd13999  141 KNSTTEKMTGVVgTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIaAAVVQKGLRPPIPPDCPPE 219
                        250       260
                 ....*....|....*....|....*.
gi 759191595 920 VYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd13999  220 LSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
683-941 3.61e-68

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: 228.28  E-value: 3.61e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPV--AVKSCRETLPPDLKAKFLQEARIL-KQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd05084   81 FLTFLR---------------TEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 843 E--VYVKKT-MGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDE 919
Cdd:cd05084  146 EdgVYAATGgMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDE 225
                        250       260
                 ....*....|....*....|..
gi 759191595 920 VYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05084  226 VYRLMEQCWEYDPRKRPSFSTV 247
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
671-950 7.83e-68

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: 228.28  E-value: 7.83e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIKFQDVIGEGNFGQVLKARIKK-DGLRMDAAIKRMK-EYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHR 748
Cdd:cd14204    3 MIDRNLLSLGKVLGEGEFGSVMEGELQQpDGTNHKVAVKTMKlDNFSQREIEEFLSEAACM-KDFNHPNVIRLLGVCLEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYL-----AIEYAPHGNLLDFLRKSRvLETDPAFaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNI 823
Cdd:cd14204   82 GSQRIpkpmvILPFMKYGDLHSFLLRSR-LGSGPQH---------VPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNC 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL 900
Cdd:cd14204  152 MLRDDMTVCVADFGLSKkiySGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 901 YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd14204  232 YDYLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLE 281
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
683-946 7.97e-68

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: 228.04  E-value: 7.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIK---KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05036   14 LGQGAFGEVYEGTVSgmpGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKF-NHPNIVRCIGVCFQRLPRFILLELMA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADF 836
Cdd:cd05036   93 GGDLKSFLRENRPRPEQP---------SSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLtckGPGRVAKIGDF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKP 913
Cdd:cd05036  164 GMARDiyrADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRMDPP 243
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd05036  244 KNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
682-949 1.30e-67

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: 227.42  E-value: 1.30e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKK-DGLRMDAAIKRMK-EYASKDDHRDFAGEleVLC-KLGHHPNIINLLGAC---EHRGYL---Y 752
Cdd:cd05035    6 ILGEGEFGSVMEAQLKQdDGSQLKVAVKTMKvDIHTYSEIEEFLSE--AACmKDFDHPNVMRLIGVCftaSDLNKPpspM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRvLETDPAFaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05035   84 VILPFMKHGDLHSYLLYSR-LGGLPEK---------LPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05035  154 VADFGLSRkiySGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNR 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05035  234 LKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
683-946 9.71e-67

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: 224.62  E-value: 9.71e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdglRMDAAIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd05148   14 LGSGYFGEVWEGLWKN---RVRVAIKILKS-DDLLKQQDFQKEVQALKRL-RHKHLISLFAVCSVGEPVYIITELMEKGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd05148   89 LLAFLR--------------SPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARli 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQEVYVKKTMgRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd05148  155 KEDVYLSSDK-KIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEI 233
                        250       260
                 ....*....|....*....|....*.
gi 759191595 921 YDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd05148  234 YKIMLECWAAEPEDRPSFKALREELD 259
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
677-941 1.62e-66

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: 224.57  E-value: 1.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKAR--IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACE--HRGYLY 752
Cdd:cd05038    6 LKFIKQLGEGHFGSVELCRydPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTL-DHEYIVKYKGVCEspGRRSLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05038   85 LIMEYLPSGSLRDYLQRHR---------------DQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSR----GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLG--------------GTPYCG 894
Cdd:cd05038  150 ISDFGLAKvlpeDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqsppalflrmiGIAQGQ 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 895 MTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05038  230 MIVTRLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
665-942 4.54e-66

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: 226.71  E-value: 4.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 665 DPTIYPV-LDW----NDIKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHP 736
Cdd:cd05104   20 DPTQLPYdHKWefprDRLRFGKTLGAGAFGKVVEATaygLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLGNHI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 737 NIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRV-------------------------------------------- 772
Cdd:cd05104  100 NIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDsficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvv 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 773 ---------------LETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd05104  180 ptkadkrrgvrsgsyVDQDVTSEILEEDELALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFG 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTC-AELYEKLPQGYRLEKP 913
Cdd:cd05104  260 LARdirNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVdSKFYKMIKEGYRMDSP 339
                        330       340
                 ....*....|....*....|....*....
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd05104  340 EFAPSEMYDIMRSCWDADPLKRPTFKQIV 368
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
672-945 4.97e-66

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: 222.52  E-value: 4.97e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDhrDFAGELEVLCKLGHhPNIINLLGACEHRGYL 751
Cdd:cd05112    1 IDPSELTFVQEIGSGQFGLVHLGYWLNK---DKVAIKTIREGAMSEE--DFIEEAEVMMKLSH-PKLVQLYGVCLEQAPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05112   75 CLVFEFMEHGCLSDYLRTQR---------------GLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRG--QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05112  140 KVSDFGMTRFvlDDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFR 219
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05112  220 LYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
671-948 8.21e-66

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 221.67  E-value: 8.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIKFQDVIGEGNFGQVLKARIkkdgLRMDAAIKRMKEYASKddhRDFAGELEVLCKLgHHPNIINLLGACEHRGy 750
Cdd:cd05083    2 LLNLQKLTLGEIIGEGEFGAVLQGEY----MGQKVAVKNIKCDVTA---QAFLEETAVMTKL-QHKNLVRLLGVILHNG- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLR-KSRVLetdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd05083   73 LYIVMELMSKGNLVNFLRsRGRAL---------------VPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSRGQEVYVKKTmgRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05083  138 VAKISDFGLAKVGSMGVDNS--RLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYR 215
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd05083  216 MEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLEKE 254
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
682-952 1.50e-65

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: 224.09  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGAC-EHRGYLYLAIEY 757
Cdd:cd05102   14 VLGHGAFGKVVEASafgIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLGACtKPNGPLMVIVEF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSR-------------------VLE-----------TDPAFAIANSTAST--------------LSSQQ 793
Cdd:cd05102   94 CKYGNLSNFLRAKRegfspyrersprtrsqvrsMVEavradrrsrqgSDRVASFTESTSSTnqprqevddlwqspLTMED 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 794 LLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTT 870
Cdd:cd05102  174 LICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDiykDPDYVRKGSARLPLKWMAPESIFDKVYTT 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 871 NSDVWSYGVLLWEIVSLGGTPYCGMTCAELY-EKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05102  254 QSDVWSFGVLLWEIFSLGASPYPGVQINEEFcQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLVEILGDLL 333

                 ...
gi 759191595 950 EER 952
Cdd:cd05102  334 QEN 336
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
683-946 1.73e-65

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: 221.14  E-value: 1.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKAR---IKKDGL-RMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05044    3 LGSGAFGEVFEGTakdILGDGSgETKVAVKTLRKGATDQEKAEFLKEAHLMSNF-KHPNILKLLGVCLDNDPQYIILELM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE-NY---VAKIA 834
Cdd:cd05044   82 EGGDLLSYLRAARPTAFTP---------PLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkDYrerVVKIG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLE 911
Cdd:cd05044  153 DFGLARDiykNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLD 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd05044  233 QPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
677-950 1.78e-65

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: 224.09  E-value: 1.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRG-YLY 752
Cdd:cd05103    9 LKLGKPLGRGAFGQVIEADafgIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGgPLM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSR----VLET-DPAF-------------------AIANSTAST-------------------- 788
Cdd:cd05103   89 VIVEFCKFGNLSAYLRSKRsefvPYKTkGARFrqgkdyvgdisvdlkrrldSITSSQSSAssgfveekslsdveeeeagq 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 789 -------LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG---QEVYVKKTMGRLPVRWM 858
Cdd:cd05103  169 edlykdfLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDiykDPDYVRKGDARLPLKWM 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 859 AIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELY-EKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPS 937
Cdd:cd05103  249 APETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFcRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPT 328
                        330
                 ....*....|...
gi 759191595 938 FAQILVSLNRMLE 950
Cdd:cd05103  329 FSELVEHLGNLLQ 341
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
682-945 4.61e-65

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: 220.94  E-value: 4.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIK-KDGLRMDAAIKRMK-EYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHR---GYLYLAIE 756
Cdd:cd05074   16 MLGKGEFGSVREAQLKsEDGSFQKVAVKMLKaDIFSSSDIEEFLREAACM-KEFDHPNVIKLIGVSLRSrakGRLPIPMV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAP---HGNLLDFLRKSRVLEtDPAfaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05074   95 ILPfmkHGDLHTFLLMSRIGE-EPF---------TLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRL 910
Cdd:cd05074  165 ADFGLSKkiySGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLIKGNRL 244
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05074  245 KQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQL 279
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
677-956 4.93e-63

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: 214.97  E-value: 4.93e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKA--RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHhPNIINLLGACEHRgYLYLA 754
Cdd:cd05057    9 LEKGKVLGSGAFGTVYKGvwIPEGEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDH-PHLVRLLGICLSS-QVQLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd05057   87 TQLMPLGCLLDYVRNHR---------------DNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKIT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLE 911
Cdd:cd05057  152 DFGLAKlldVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLP 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYV 956
Cdd:cd05057  232 QPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMARDPQRYL 276
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
672-953 4.97e-63

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: 214.59  E-value: 4.97e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKA-RIKKDGLRMDAAIKRMKEYASKDDHRDFAGElEVLCKLGHHPNIINLLGACEHRGy 750
Cdd:cd05056    3 IQREDITLGRCIGEGQFGDVYQGvYMSPENEKIAVAVKTCKNCTSPSVREKFLQE-AYIMRQFDHPHIVKLIGVITENP- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05056   81 VWIVMELAPLGELRSYLQVNK---------------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05056  146 VKLGDFGLSRymEDESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGE 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERK 953
Cdd:cd05056  226 RLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
672-941 1.32e-62

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: 212.92  E-value: 1.32e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKkdGLRMdaAIKRMKEYASKddhRDFAGELEVLCKLgHHPNIINLLGA-CEHRGY 750
Cdd:cd05082    3 LNMKELKLLQTIGKGEFGDVMLGDYR--GNKV--AVKCIKNDATA---QAFLAEASVMTQL-RHSNLVQLLGViVEEKGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRkSRvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05082   75 LYIVTEYMAKGSLVDYLR-SR-------------GRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRgqEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRL 910
Cdd:cd05082  141 AKVSDFGLTK--EASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKM 218
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05082  219 DAPDGCPPAVYDVMKNCWHLDAAMRPSFLQL 249
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
683-949 3.13e-62

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: 216.80  E-value: 3.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKAriKKDGLR-----MDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd05107   45 LGSGAFGRVVEA--TAHGLShsqstMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNIVNLLGACTKGGPIYIITEY 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFL-------------------------------RKSRV---LETDPAF------------------------ 779
Cdd:cd05107  123 CRYGDLVDYLhrnkhtflqyyldknrddgslisggstplsqRKSHVslgSESDGGYmdmskdesadyvpmqdmkgtvkya 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 780 ------------------------AIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05107  203 diessnyespydqylpsapertrrDTLINESPALSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICD 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL-YEKLPQGYRLE 911
Cdd:cd05107  283 FGLARDimrDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQfYNAIKRGYRMA 362
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05107  363 KPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
672-945 1.26e-61

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: 210.12  E-value: 1.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKdglRMDAAIKRMKEYASKDDhrDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd05113    1 IDPKDLTFLKELGTGQFGVVKYGKWRG---QYDVAIKMIKEGSMSED--EFIEEAKVMMNL-SHEKLVQLYGVCTKQRPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05113   75 FIITEYMANGCLLNYLR---------------EMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRG--QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05113  140 KVSDFGLSRYvlDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLR 219
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05113  220 LYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNI 255
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
682-944 1.73e-61

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: 210.02  E-value: 1.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKAR-IKKDGLRMDAAIKRMKEYASKDDHRDFAGElEVLCKLGHHPNIINLLGAC-EHRGYLYLAIEYAP 759
Cdd:cd05058    2 VIGKGHFGCVYHGTlIDSDGQKIHCAVKSLNRITDIEEVEQFLKE-GIIMKDFSHPNVLSLLGIClPSEGSPLVVLPYMK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKsrvlETDpafaiaNSTAstlssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05058   81 HGDLRNFIRS----ETH------NPTV-----KDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RgqEVYVK-------KTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:cd05058  146 R--DIYDKeyysvhnHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQ 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 913 PLNCDDEVYDLMRQCWREKPYERPSFAQiLVS 944
Cdd:cd05058  224 PEYCPDPLYEVMLSCWHPKPEMRPTFSE-LVS 254
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
672-949 7.62e-61

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: 208.57  E-value: 7.62e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLR-MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY 750
Cdd:cd05066    1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKReIPVAIKTLKAGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTRSKP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSrvletDPAFAIAnstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05066   80 VMIVTEYMENGSLDAFLRKH-----DGQFTVI----------QLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSR----GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 906
Cdd:cd05066  145 CKVSDFGLSRvledDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEE 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 907 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05066  225 GYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
677-947 8.21e-60

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 205.97  E-value: 8.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVI-----GEGNFGQVLKAR---IKKDGLRMDAAIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHR 748
Cdd:cd05092    2 IKRRDIVlkwelGEGAFGKVFLAEchnLLPEQDKMLVAVKALKE-ATESARQDFQREAELLTVL-QHQHIVRFYGVCTEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRK----SRVLETDPAFAIANstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL 824
Cdd:cd05092   80 EPLIMVFEYMRHGDLNRFLRShgpdAKILDGGEGQAPGQ-----LTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 825 VGENYVAKIADFGLSRgqEVYVK---KTMGR--LPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAE 899
Cdd:cd05092  155 VGQGLVVKIGDFGMSR--DIYSTdyyRVGGRtmLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTE 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 759191595 900 LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNR 947
Cdd:cd05092  233 AIECITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
672-949 1.50e-59

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: 204.72  E-value: 1.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLR-MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY 750
Cdd:cd05065    1 IDVSCVKIEEVIGAGEFGEVCRGRLKLPGKReIFVAIKTLKSGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSrvletDPAFAIAnstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05065   80 VMIITEFMENGALDSFLRQN-----DGQFTVI----------QLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRGQE------VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKL 904
Cdd:cd05065  145 CKVSDFGLSRFLEddtsdpTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAI 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 905 PQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05065  225 EQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
682-945 1.69e-59

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: 209.11  E-value: 1.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05105   44 ILGSGAFGKVVEGTaygLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYC 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSR--VLETDPA--------FAIANSTAST---------------------------------------- 788
Cdd:cd05105  124 FYGDLVNYLHKNRdnFLSRHPEkpkkdldiFGINPADESTrsyvilsfenkgdymdmkqadttqyvpmleikeaskysdi 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 789 ------------------------------LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05105  204 qrsnydrpasykgsndsevknllsddgsegLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGL 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTC-AELYEKLPQGYRLEKPL 914
Cdd:cd05105  284 ARDimhDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMIVdSTFYNKIKSGYRMAKPD 363
                        330       340       350
                 ....*....|....*....|....*....|....
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSF---AQILVSL 945
Cdd:cd05105  364 HATQEVYDIMVKCWNSEPEKRPSFlhlSDIVESL 397
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
675-949 4.96e-59

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: 203.28  E-value: 4.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDA-AIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYL 753
Cdd:cd05063    5 SHITKQKVIGAGEFGEVFRGILKMPGRKEVAvAIKTLKPGYTEKQRQDFLSEASIMGQFSHH-NIIRLEGVVTKFKPAMI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRksrvlETDPAFaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05063   84 ITEYMENGALDKYLR-----DHDGEF----------SSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTM----GRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05063  149 SDFGLSRVLEDDPEGTYttsgGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFR 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05063  229 LPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
677-945 1.28e-58

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: 202.68  E-value: 1.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKAR-IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC-EHRGYLYLA 754
Cdd:cd05043    8 VTLSDLLQEGTFGRIFHGIlRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGL-SHQNLLPILHVCiEDGEKPMVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd05043   87 YPYMNWGNLKLFLQQCRLSEA--------NNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKIT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRGQEVYVKKTMG---RLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLE 911
Cdd:cd05043  159 DNALSRDLFPMDYHCLGdneNRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLA 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05043  239 QPINCPDELFAVMACCWALDPEERPSFQQLVQCL 272
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
678-942 2.69e-57

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 197.75  E-value: 2.69e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLV--AIKVIKKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   758 APHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:smart00220  79 CEGGDLFDLLKKRG----------------RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   838 LSR--GQEVYVKKTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM-TCAELYEKLPQGYR--LEK 912
Cdd:smart00220 143 LARqlDPGEKLTTFVGTPE--YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDdQLLELFKKIGKPKPpfPPP 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 759191595   913 PLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:smart00220 220 EWDISPEAKDLIRKLLVKDPEKRLTAEEAL 249
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
683-941 4.78e-57

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: 197.18  E-value: 4.78e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKK-DGLRMDAAIKRMKE--YASKDDHRDFAGELEVLCKLgHHPNIINLLG-ACEHRgyLYLAIEYA 758
Cdd:cd05040    3 LGDGSFGVVRRGEWTTpSGKVIQVAVKCLKSdvLSQPNAMDDFLKEVNAMHSL-DHPNLIRLYGvVLSSP--LMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRvletdPAFAIanstaSTLSsqqllHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05040   80 PLGSLLDRLRKDQ-----GHFLI-----STLC-----DYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SR----GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQ-GYRLEKP 913
Cdd:cd05040  145 MRalpqNEDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDKeGERLERP 224
                        250       260
                 ....*....|....*....|....*...
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05040  225 DDCPQDIYNVMLQCWAHKPADRPTFVAL 252
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
682-945 5.19e-57

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 198.07  E-value: 5.19e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHR---DFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05046   12 TLGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDENlqsEFRRELDMFRKL-SHKNVVRLLGLCREAEPHYMILEYT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVletdpafAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05046   91 DLGDLKQFLRATKS-------KDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SR---GQEvYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQG-YRLEKPL 914
Cdd:cd05046  164 SKdvyNSE-YYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGkLELPVPE 242
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05046  243 GCPSRLYKLMTRCWAVNPKDRPSFSELVSAL 273
IgI_Tie2 cd20964
Immunoglobulin domain of Tie2 tyrosine kinase; a member of the I-set of IgSF domains; The ...
201-292 8.73e-57

Immunoglobulin domain of Tie2 tyrosine kinase; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain of Tie2 tyrosine kinase. The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Tie2 contains three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Tie2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409556  Cd Length: 92  Bit Score: 190.19  E-value: 8.73e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 201 MTPKIEDLPDHIEVNSGKFNPICKASGWPLPANEEMTLVKPDGTVLHPKDFNHTGHLSVATFTIHRILPPDSGVWVCSVN 280
Cdd:cd20964    1 MPPKIDDLPDHEEVNSGKFNPICKASGWPLPVNEEMTLVKPDGTVLHPKDFNHTPHRSVAEFTIHRLLPPDSGVWVCSVN 80
                         90
                 ....*....|..
gi 759191595 281 TVAGMVEKPFNI 292
Cdd:cd20964   81 TVAGMVEKPFNI 92
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
675-938 3.00e-56

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: 195.49  E-value: 3.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLgACEHRGYLYLA 754
Cdd:cd05067    7 ETLKLVERLGAGQFGEVWMGYYNGH---TKVAIKSLKQGSMSPDA--FLAEANLMKQL-QHQRLVRLY-AVVTQEPIYII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd05067   80 TEYMENGSLVDFLK--------------TPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRGQEV--YVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 912
Cdd:cd05067  146 DFGLARLIEDneYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPR 225
                        250       260
                 ....*....|....*....|....*.
gi 759191595 913 PLNCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd05067  226 PDNCPEELYQLMRLCWKERPEDRPTF 251
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
677-945 5.40e-56

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: 195.23  E-value: 5.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGlrMD----AAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd05090    7 VRFMEELGECAFGKIYKGHLYLPG--MDhaqlVAIKTLKDYNNPQQWNEFQQEASLMTEL-HHPNIVCLLGVVTQEQPVC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFL-RKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05090   84 MLFEFMNQGDLHEFLiMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05090  164 KISDLGLSReiySSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQ 243
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05090  244 LLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
677-938 1.82e-55

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: 193.33  E-value: 1.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDglrMDAAIKRMKeyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd05072    9 IKLVKKLGAGQFGEVWMGYYNNS---TKVAVKTLK--PGTMSVQAFLEEANLMKTL-QHDKLVRLYAVVTKEEPIYIITE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd05072   83 YMAKGSLLDFLK--------------SDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05072  149 GLARVIEdnEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRME 228
                        250       260
                 ....*....|....*....|....
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd05072  229 NCPDELYDIMKTCWKEKAEERPTF 252
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
683-951 1.47e-54

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: 191.34  E-value: 1.47e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKArIKKDGLRMDA----AIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05061   14 LGQGSFGMVYEG-NARDIIKGEAetrvAVKTVNESASLRERIEFLNEASVMKGFTCH-HVVRLLGVVSKGQPTLVVMELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPAfaiaNSTASTLssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05061   92 AHGDLKSYLRSLRPEAENNP----GRPPPTL--QEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLN 915
Cdd:cd05061  166 TRDiyeTDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDN 245
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 916 CDDEVYDLMRQCWREKPYERPSFAQILvslnRMLEE 951
Cdd:cd05061  246 CPERVTDLMRMCWQFNPKMRPTFLEIV----NLLKD 277
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
672-950 3.96e-54

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: 189.30  E-value: 3.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVlkaRIKKDGLRMDAAIKRMKEYASKDDhrDFAGELEVLCKLGHhPNIINLLGACEHRGYL 751
Cdd:cd05114    1 INPSELTFMKELGSGLFGVV---RLGKWRAQYKVAIKAIREGAMSEE--DFIEEAKVMMKLTH-PKLVQLYGVCTQQKPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05114   75 YIVTEFMENGCLLNYLRQRR---------------GKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRG--QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd05114  140 KVSDFGMTRYvlDDQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHR 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd05114  220 LYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTITEIAE 260
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
683-945 4.90e-54

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: 189.02  E-value: 4.90e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRD-FAGELEVLCKLgHHPNIINLLGACEHRGYLyLAIEYAPHG 761
Cdd:cd05116    3 LGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDeLLREANVMQQL-DNPYIVRMIGICEAESWM-LVMEMAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRvletdpafaiaNSTASTLSsqQLLHfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd05116   81 PLNKFLQKNR-----------HVTEKNIT--ELVH---QVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 ----QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCD 917
Cdd:cd05116  145 lradENYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCP 224
                        250       260
                 ....*....|....*....|....*...
gi 759191595 918 DEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05116  225 PEMYDLMKLCWTYDVDERPGFAAVELRL 252
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
675-957 1.18e-53

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 189.10  E-value: 1.18e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd05093    5 HNIVLKRELGEGAFGKVFLAEcynLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSrvlETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05093   83 IMVFEYMKHGDLNKFLRAH---GPDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd05093  160 KIGDFGMSRdvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVN 957
Cdd:cd05093  240 VLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLD 288
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
671-956 1.30e-53

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: 189.85  E-value: 1.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIKFQDVIGEGNFGQVLKARIKKDG--LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACeHR 748
Cdd:cd05108    3 ILKETEFKKIKVLGSGAFGTVYKGLWIPEGekVKIPVAIKELREATSPKANKEILDEAYVMASV-DNPHVCRLLGIC-LT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV-GE 827
Cdd:cd05108   81 STVQLITQLMPFGCLLDYVREHK---------------DNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVkTP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVaKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKL 904
Cdd:cd05108  146 QHV-KITDFGLAKllgAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSIL 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 905 PQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYV 956
Cdd:cd05108  225 EKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYL 276
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
683-941 1.61e-53

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: 187.85  E-value: 1.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHhPNIINLLGACEHRGyLYLAIEYAPHGN 762
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDN-PYIVRMIGVCEAEA-LMLVMEMASGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRvlETDPAFAIAnstastlssqQLLHfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG- 841
Cdd:cd05115   90 LNKFLSGKK--DEITVSNVV----------ELMH---QVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 ---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDD 918
Cdd:cd05115  155 gadDSYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPP 234
                        250       260
                 ....*....|....*....|...
gi 759191595 919 EVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05115  235 EMYALMSDCWIYKWEDRPNFLTV 257
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
677-941 4.01e-53

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: 187.83  E-value: 4.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIK--------------KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLL 742
Cdd:cd05096    7 LLFKEKLGEGQFGEVHLCEVVnpqdlptlqfpfnvRKGRPLLVAVKILRPDANKNARNDFLKEVKILSRL-KDPNIIRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 743 GACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTAS---TLSSQQLLHFAADVARGMDYLSQKQFIHRDLA 819
Cdd:cd05096   86 GVCVDEDPLCMITEYMENGDLNQFLSSHHLDDKEENGNDAVPPAHclpAISYSSLLHVALQIASGMKYLSSLNFVHRDLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 820 ARNILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSL-GGTPYCGM 895
Cdd:cd05096  166 TRNCLVGENLTIKIADFGMSRnlyAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKEQPYGEL 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 896 TCAELYEKLPQGYR-------LEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05096  246 TDEQVIENAGEFFRdqgrqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
677-945 6.62e-53

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: 187.12  E-value: 6.62e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQV-------LKARIKKD-------GLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLL 742
Cdd:cd05095    7 LTFKEKLGEGQFGEVhlceaegMEKFMDKDfalevseNQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDPNIIRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 743 GACEHRGYLYLAIEYAPHGNLLDFLrkSRVLETDPAFAIANStaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARN 822
Cdd:cd05095   86 AVCITDDPLCMITEYMENGDLNQFL--SRQQPEGQLALPSNA--LTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSL-GGTPYCGMTCA 898
Cdd:cd05095  162 CLVGKNYTIKIADFGMSRnlySGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPYSQLSDE 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759191595 899 ELYEKLPQGYR-------LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05095  242 QVIENTGEFFRdqgrqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLL 295
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
671-956 6.80e-53

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: 186.38  E-value: 6.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIKFQDVIGEGNFGQVLKARIKKDG--LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHhPNIINLLGACeHR 748
Cdd:cd05109    3 ILKETELKKVKVLGSGAFGTVYKGIWIPDGenVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGS-PYVCRLLGIC-LT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05109   81 STVQLVTQLMPYGCLLDYVRENK---------------DRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRGQEVYVKKTM---GRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLP 905
Cdd:cd05109  146 NHVKITDFGLARLLDIDETEYHadgGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLE 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 906 QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYV 956
Cdd:cd05109  226 KGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMARDPSRFV 276
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
672-941 2.03e-52

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: 185.22  E-value: 2.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARI--KKDGLRMDA-AIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHR 748
Cdd:cd05091    3 INLSAVRFMEELGEDRFGKVYKGHLfgTAPGEQTQAvAIKTLKDKAEGPLREEFRHEAMLRSRL-QHPNIVCLLGVVTKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFL----RKSRVLETDPAfaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL 824
Cdd:cd05091   82 QPMSMIFSYCSHGDLHEFLvmrsPHSDVGSTDDD----KTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 825 VGENYVAKIADFGLSRgqEVYVK---KTMGR--LPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAE 899
Cdd:cd05091  158 VFDKLNVKISDLGLFR--EVYAAdyyKLMGNslLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQD 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 900 LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05091  236 VIEMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
675-941 2.31e-52

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 185.56  E-value: 2.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQV--LKARIKKDGLRMDA----------AIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLL 742
Cdd:cd05097    5 QQLRLKEKLGEGQFGEVhlCEAEGLAEFLGEGApefdgqpvlvAVKMLRADVTKTARNDFLKEIKIMSRL-KNPNIIRLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 743 GACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETdpaFAIANSTAStLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARN 822
Cdd:cd05097   84 GVCVSDDPLCMITEYMENGDLNQFLSQREIEST---FTHANNIPS-VSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSL-GGTPYCGMTCA 898
Cdd:cd05097  160 CLVGNHYTIKIADFGMSRnlySGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSLLSDE 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 899 ELYEKLPQGYR-------LEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05097  240 QVIENTGEFFRnqgrqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
683-945 2.63e-52

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: 184.85  E-value: 2.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIK---KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05062   14 LGQGSFGMVYEGIAKgvvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCH-HVVRLLGVVSQGQPTLVIMELMT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05062   93 RGDLKSYLRSLRPEMEN------NPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNC 916
Cdd:cd05062  167 RDiyeTDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLDKPDNC 246
                        250       260
                 ....*....|....*....|....*....
gi 759191595 917 DDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd05062  247 PDMLFELMRMCWQYNPKMRPSFLEIISSI 275
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
677-948 7.82e-52

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: 183.68  E-value: 7.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIK--KDGLRMDAAIKRMkEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY--LY 752
Cdd:cd14205    6 LKFLQQLGKGNFGSVEMCRYDplQDNTGEVVAVKKL-QHSTEEHLRDFEREIEILKSL-QHDNIVKYKGVCYSAGRrnLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd14205   84 LIMEYLPYGSLRDYLQKHK---------------ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSR----GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS---------------LGGTPYC 893
Cdd:cd14205  149 IGDFGLTKvlpqDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefmrmIGNDKQG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 894 GMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14205  229 QMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
683-942 1.18e-51

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: 180.54  E-value: 1.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKV--AVKVIPKEKLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd00180   78 LKDLLKENKG---------------PLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdl 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 -GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIvslggtpycgmtcaelyeklpqgyrlekplncdDE 919
Cdd:cd00180  143 dSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EE 189
                        250       260
                 ....*....|....*....|...
gi 759191595 920 VYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd00180  190 LKDLIRRMLQYDPKKRPSAKELL 212
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
677-938 1.45e-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: 182.15  E-value: 1.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKdglRMDAAIKRMKEYASKDDHrdFAGELEVLCKLGHhpNIINLLGACEHRGYLYLAIE 756
Cdd:cd05073   13 LKLEKKLGAGQFGEVWMATYNK---HTKVAVKTMKPGSMSVEA--FLAEANVMKTLQH--DKLVKLHAVVTKEPIYIITE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd05073   86 FMAKGSLLDFLK--------------SDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05073  152 GLARVIEdnEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPE 231
                        250       260
                 ....*....|....*....|....
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd05073  232 NCPEELYNIMMRCWKNRPEERPTF 255
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
672-949 3.29e-50

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: 178.19  E-value: 3.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLR-MDAAIKRMKEYASKDDHRDFAGELevlCKLGH--HPNIINLLGACEHR 748
Cdd:cd05064    2 LDNKSIKIERILGTGRFGELCRGCLKLPSKReLPVAIHTLRAGCSDKQRRGFLAEA---LTLGQfdHSNIVRLEGVITRG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05064   79 NTMMIVTEYMSNGALDSFLRKHE---------------GQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGlsRGQE-----VYVkkTM-GRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYE 902
Cdd:cd05064  144 LVCKISGFR--RLQEdkseaIYT--TMsGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIK 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 903 KLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05064  220 AVEDGFRLPAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV 266
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
671-956 7.67e-50

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: 177.84  E-value: 7.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIKFQDVIGEGNFGQVLKARIKKDG--LRMDAAIKRMKEYASKD------DHRDFAGELEvlcklghHPNIINLL 742
Cdd:cd05111    3 IFKETELRKLKVLGSGVFGTVHKGIWIPEGdsIKIPVAIKVIQDRSGRQsfqavtDHMLAIGSLD-------HAYIVRLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 743 GACEHRGyLYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARN 822
Cdd:cd05111   76 GICPGAS-LQLVTQLLPLGSLLDHVRQHR---------------GSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGENYVAKIADFGLSRGQEVYVKKTM---GRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAE 899
Cdd:cd05111  140 VLLKSPSQVQVADFGVADLLYPDDKKYFyseAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAE 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 900 LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYV 956
Cdd:cd05111  220 VPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYL 276
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
671-956 1.50e-49

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: 177.95  E-value: 1.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIKFQDVIGEGNFGQVLKARIKKDG--LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACeHR 748
Cdd:cd05110    3 ILKETELKRVKVLGSGAFGTVYKGIWVPEGetVKIPVAIKILNETTGPKANVEFMDEALIMASM-DHPHLVRLLGVC-LS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd05110   81 PTIQLVTQLMPHGCLLDYVHEHK---------------DNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLP 905
Cdd:cd05110  146 NHVKITDFGLARlleGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLE 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 906 QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYV 956
Cdd:cd05110  226 KGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYL 276
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
683-938 2.03e-49

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: 175.49  E-value: 2.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGyLYLAIEYAPHGN 762
Cdd:cd14203    3 LGQGCFGEVWMGTWNGT---TKVAIKTLKPGTMSPEA--FLEEAQIMKKL-RHDKLVQLYAVVSEEP-IYIVTEFMSKGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd14203   76 LLDFLK--------------DGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 843 E--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd14203  142 EdnEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESL 221
                        250
                 ....*....|....*...
gi 759191595 921 YDLMRQCWREKPYERPSF 938
Cdd:cd14203  222 HELMCQCWRKDPEERPTF 239
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
676-948 2.61e-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: 2.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARI-----KKDglRMDAAIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY 750
Cdd:cd05094    6 DIVLKRELGEGAFGKVFLAECynlspTKD--KMLVAVKTLKD-PTLAARKDFQREAELLTNL-QHDHIVKFYGVCGDGDP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05094   82 LIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQG 907
Cdd:cd05094  162 VKIGDFGMSRdvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQG 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 759191595 908 YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd05094  242 RVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
677-941 1.48e-48

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: 174.31  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGLRMDA--AIKRMkEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY--LY 752
Cdd:cd05081    6 LKYISQLGKGNFGSVELCRYDPLGDNTGAlvAVKQL-QHSGPDQQRDFQREIQILKAL-HSDFIVKYRGVSYGPGRrsLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05081   84 LVMEYLPSGCLRDFLQRHR---------------ARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSR----GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlggtpYCGMTCA---------- 898
Cdd:cd05081  149 IADFGLAKllplDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT-----YCDKSCSpsaeflrmmg 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 899 ---------ELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05081  224 cerdvpalcRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSAL 275
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
677-950 9.44e-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: 172.01  E-value: 9.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARI--KKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRG--YLY 752
Cdd:cd05080    6 LKKIRDLGEGHFGKVSLYCYdpTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTL-YHENIVKYKGCCSEQGgkSLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRVletdpafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05080   85 LIMEYVPLGSLRDYLPKHSI-----------------GLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSR----GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------------LGGTPYCG 894
Cdd:cd05080  148 IGDFGLAKavpeGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLThcdssqspptkfleMIGIAQGQ 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 895 MTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd05080  228 MTVVRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
683-949 2.24e-46

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: 168.18  E-value: 2.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMD--AAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRG--YLYLAIEYA 758
Cdd:cd05079   12 LGEGHFGKVELCRYDPEGDNTGeqVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGgnGIKLIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05079   91 PSGSLKEYLPRNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRG----QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------------LGGTPYCGMTCAEL 900
Cdd:cd05079  156 TKAietdKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspmtlflkMIGPTHGQMTVTRL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 901 YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd05079  236 VRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
677-938 5.04e-45

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: 163.70  E-value: 5.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGyLYLAIE 756
Cdd:cd05071   11 LRLEVKLGQGCFGEVWMGTWNGT---TRVAIKTLKPGTMSPEA--FLQEAQVMKKL-RHEKLVQLYAVVSEEP-IYIVTE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd05071   84 YMSKGSLLDFLK--------------GEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd05071  150 GLARLIEdnEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPP 229
                        250       260
                 ....*....|....*....|....
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd05071  230 ECPESLHDLMCQCWRKEPEERPTF 253
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
683-941 6.22e-45

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: 163.70  E-value: 6.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGyLYLAIEYAPHGN 762
Cdd:cd05069   20 LGQGCFGEVWMGTWNGT---TKVAIKTLKPGTMMPEA--FLQEAQIMKKL-RHDKLVPLYAVVSEEP-IYIVTEFMGKGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvlETDPAFaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd05069   93 LLDFLK-----EGDGKY---------LKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 843 E--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd05069  159 EdnEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESL 238
                        250       260
                 ....*....|....*....|.
gi 759191595 921 YDLMRQCWREKPYERPSFAQI 941
Cdd:cd05069  239 HELMKLCWKKDPDERPTFEYI 259
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
682-948 3.50e-43

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: 157.94  E-value: 3.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDglrmDAAIKRmkeyASKDDHRDFAGELEVLCK------LGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd14061    1 VIGVGGFGKVYRGIWRGE----EVAVKA----ARQDPDEDISVTLENVRQearlfwMLRHPNIIALRGVCLQPPNLCLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLldflrkSRVLetdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQ---FIHRDLAARNILVGE----- 827
Cdd:cd14061   73 EYARGGAL------NRVL-----------AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaiene 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 ---NYVAKIADFGLSRgqEVYVKKTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAEL-YE 902
Cdd:cd14061  136 dleNKTLKITDFGLAR--EWHKTTRMSAAGTyAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVaYG 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 759191595 903 KLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14061  213 VAVNKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
683-938 1.21e-42

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: 156.77  E-value: 1.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDhrDFAGELEVLCKLgHHPNIINLLGACEHRGyLYLAIEYAPHGN 762
Cdd:cd05070   17 LGNGQFGEVWMGTWNGN---TKVAIKTLKPGTMSPE--SFLEEAQIMKKL-KHDKLVQLYAVVSEEP-IYIVTEYMSKGS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd05070   90 LLDFLK--------------DGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 843 E--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd05070  156 EdnEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISL 235
                        250
                 ....*....|....*...
gi 759191595 921 YDLMRQCWREKPYERPSF 938
Cdd:cd05070  236 HELMIHCWKKDPEERPTF 253
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
682-945 3.02e-39

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: 147.11  E-value: 3.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKE--YASKDDHRDFAGELEVLcklgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14146    1 IIGVGGFGKVYRATWKGQEVAVKAARQDPDEdiKATAESVRQEAKLFSML----RHPNIIKLEGVCLEEPNLCLVMEFAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLldflrkSRVLETDPAfAIANSTASTLSSQQLLHFAADVARGMDYLSQKQF---IHRDLAARNILVGE--------N 828
Cdd:cd14146   77 GGTL------NRALAAANA-APGPRRARRIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLLEkiehddicN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRGQEVYVKKTMGRlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMT-CAELYEKLPQG 907
Cdd:cd14146  150 KTLKITDFGLAREWHRTTKMSAAG-TYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDgLAVAYGVAVNK 227
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 908 YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14146  228 LTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
681-942 1.14e-38

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: 144.97  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRD-FAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELM--AVKEVELSGDSEEELEaLEREIRILSSL-KHPNIVRYLGTERTENTLNIFLEYVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd06606   83 GGSLASLLKK----------------FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R--GQEVYVKKTMGRL--PvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY--CGMTCAELYEKLPQGYRLEKP 913
Cdd:cd06606  147 KrlAEIATGEGTKSLRgtP-YWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWseLGNPVAALFKIGSSGEPPPIP 224
                        250       260
                 ....*....|....*....|....*....
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06606  225 EHLSEEAKDFLRKCLQRDPKKRPTADELL 253
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
683-946 4.15e-38

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: 142.63  E-value: 4.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrmDAAIKRMKEYASKDdhrdfageLEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14059    1 LGSGAQGAVFLGKFRGE----EVAVKKVRDEKETD--------IKHLRKL-NHPNIIKFKGVCTQAPCYCILMEYCPYGQ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVLetdpafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG- 841
Cdd:cd14059   68 LYEVLRAGREI----------------TPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEl 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 QEVYVKKTMGRlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM-TCAELYEKLPQGYRLEKPLNCDDEV 920
Cdd:cd14059  132 SEKSTKMSFAG-TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVdSSAIIWGVGSNSLQLPVPSTCPDGF 209
                        250       260
                 ....*....|....*....|....*.
gi 759191595 921 YDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd14059  210 KLLMKQCWNSKPRNRPSFRQILMHLD 235
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
678-943 4.76e-38

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: 143.11  E-value: 4.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKeYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd05122    3 EILEKIGKGGFGVVYKARHKKTGQIV--AIKKIN-LESKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDflrksrvletdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd05122   79 CSGGSLKD---------------LLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LS-RGQEVYVKKTM-GRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQG--YRLEKP 913
Cdd:cd05122  144 LSaQLSDGKTRNTFvGTPY--WMAPEVIQGKPYGFKADIWSLGITAIEMA-EGKPPYSELPPMKALFLIATNgpPGLRNP 220
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQILV 943
Cdd:cd05122  221 KKWSKEFKDFLKKCLQKDPEKRPTAEQLLK 250
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
676-942 3.17e-37

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


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 140.69  E-value: 3.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM--KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIV--ALKVIskSQLQKSGLEHQLRREIEIQSHL-RHPNILRLYGYFEDKKRIYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd14007   78 ILEYAPNGELYKELKKQKRFDEKEAA----------------KYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTM-GRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRLE 911
Cdd:cd14007  142 ADFGWSVHAPSNRRKTFcGTL--DYLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQETYKRIQNVdIKFP 218
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 912 KPLNcdDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14007  219 SSVS--PEAKDLISKLLQKDPSKRLSLEQVL 247
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
684-948 1.03e-36

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 138.55  E-value: 1.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 684 GEGNFGQVLKAR-IKKDglrMDAAIKRMKEYASkddhrdfagELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14060    2 GGGSFGSVYRAIwVSQD---KEVAVKKLLKIEK---------EAEILSVLSHR-NIIQFYGAILEAPNYGIVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVLETDpafaianstastlsSQQLLHFAADVARGMDYLSQK---QFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14060   69 LFDYLNSNESEEMD--------------MDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGAS 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R-GQEVYVKKTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGgTPYCGMTCAEL-YEKLPQGYRLEKPLNCD 917
Cdd:cd14060  135 RfHSHTTHMSLVGTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTRE-VPFKGLEGLQVaWLVVEKNERPTIPSSCP 211
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 918 DEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14060  212 RSFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
683-951 1.39e-36

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: 139.33  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKkDGLrmDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGT--VVAVKRLNEMNCAASKKEFLTELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRvlETDPafaianstastLSSQQLLHFAADVARGMDYL---SQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14066   77 LEDRLHCHK--GSPP-----------LPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEI------VSLGGTPYCGMTCAELYE-KLPQGYR 909
Cdd:cd14066  144 RlipPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELltgkpaVDENRENASRKDLVEWVEsKGKEELE 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 910 --LEKPLNCDDEV--------YDLMRQCWREKPYERPSFAQILvslnRMLEE 951
Cdd:cd14066  224 diLDKRLVDDDGVeeeevealLRLALLCTRSDPSLRPSMKEVV----QMLEK 271
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
683-950 3.71e-35

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: 134.49  E-value: 3.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdglrMDAAIKrmkEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14058    1 VGRGSFGVVCKARWRN----QIVAVK---IIESESEKKAFEVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGGS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSrvlETDPAFAIANSTASTLSSqqllhfaadvARGMDYL---SQKQFIHRDLAARNILVGENY-VAKIADFGL 838
Cdd:cd14058   73 LYNVLHGK---EPKPIYTAAHAMSWALQC----------AKGVAYLhsmKPKALIHRDLKPPNLLLTNGGtVLKICDFGT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRGQEVYvkKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS-------LGGTPYCGMTCAELYEKLPqgyrLE 911
Cdd:cd14058  140 ACDISTH--MTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITrrkpfdhIGGPAFRIMWAVHNGERPP----LI 213
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 912 KplNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd14058  214 K--NCPKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLMQ 250
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
672-945 7.20e-35

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: 134.40  E-value: 7.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDglrmDAAIKRmkeyASKDDHRDFAGELE------VLCKLGHHPNIINLLGAC 745
Cdd:cd14145    3 IDFSELVLEEIIGIGGFGKVYRAIWIGD----EVAVKA----ARHDPDEDISQTIEnvrqeaKLFAMLKHPNIIALRGVC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRGYLYLAIEYAPHGNLldflrkSRVLetdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQF---IHRDLAARN 822
Cdd:cd14145   75 LKEPNLCLVMEFARGGPL------NRVL-----------SGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSN 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGE--------NYVAKIADFGLSRGQEVYVKKTMGRlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd14145  138 ILILEkvengdlsNKILKITDFGLAREWHRTTKMSAAG-TYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRG 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 895 MT-CAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14145  216 IDgLAVAYGVAMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQL 267
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
682-945 1.82e-34

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: 132.80  E-value: 1.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDglrmDAAIKRMKEYASKD---DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd14148    1 IIGVGGFGKVYKGLWRGE----EVAVKAARQDPDEDiavTAENVRQEARLFWML-QHPNIIALRGVCLNPPHLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVletdPAFAIANstastlssqqllhFAADVARGMDYLSQKQF---IHRDLAARNILVGE-------- 827
Cdd:cd14148   76 RGGALNRALAGKKV----PPHVLVN-------------WAVQIARGMNYLHNEAIvpiIHRDLKSSNILILEpienddls 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVAKIADFGLSRGQEVYVKKTMGRlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM-TCAELYEKLPQ 906
Cdd:cd14148  139 GKTLKITDFGLAREWHKTTKMSAAG-TYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIdALAVAYGVAMN 216
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 907 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14148  217 KLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRL 255
Pkinase pfam00069
Protein kinase domain;
682-942 2.17e-34

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 131.21  E-value: 2.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  682 VIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIV--AIKKIkKEKIKKKKDKNILREIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEYVEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  761 GNLLDFLRKSRVletdpafaianstastLSSQQLLHFAADVARGMDYLSQKqfihrdlaarNILVGenyvakiadfglSR 840
Cdd:pfam00069  83 GSLFDLLSEKGA----------------FSEREAKFIMKQILEGLESGSSL----------TTFVG------------TP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  841 GqevyvkktmgrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEK-LPQGYR-LEKPLNCDD 918
Cdd:pfam00069 125 W---------------YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELiIDQPYAfPELPSNLSE 188
                         250       260
                  ....*....|....*....|....
gi 759191595  919 EVYDLMRQCWREKPYERPSFAQIL 942
Cdd:pfam00069 189 EAKDLLKKLLKKDPSKRLTATQAL 212
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
673-948 3.81e-34

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: 132.08  E-value: 3.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYAS------KDDHRDFAgelevlckLGHHPNIINLLGACE 746
Cdd:cd14147    1 SFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISvtaesvRQEARLFA--------MLAHPNIIALKAVCL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 747 HRGYLYLAIEYAPHGNLLDFLRKSRVletdPAFAIANstastlssqqllhFAADVARGMDYLSQKQF---IHRDLAARNI 823
Cdd:cd14147   73 EEPNLCLVMEYAAGGPLSRALAGRRV----PPHVLVN-------------WAVQIARGMHYLHCEALvpvIHRDLKSNNI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVA--------KIADFGLSRGQEVYVK-KTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd14147  136 LLLQPIENddmehktlKITDFGLAREWHKTTQmSAAGTYA--WMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRG 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 895 MTC-AELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14147  213 IDClAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
683-942 5.36e-34

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: 131.07  E-value: 5.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaaikRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVM-----VMKELKRFDEQRSFLKEVKLMRRL-SHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE---NYVAKIADFGLS 839
Cdd:cd14065   75 LEELLK---------------SMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGRNAVVADFGLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RGQEVYVKKTMGR---LPV----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVS-LGGTPycgmtcaelyEKLP------ 905
Cdd:cd14065  140 REMPDEKTKKPDRkkrLTVvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGrVPADP----------DYLPrtmdfg 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 906 ---QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14065  210 ldvRAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELE 249
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
683-945 2.97e-33

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: 129.19  E-value: 2.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLrmdaAIKRMKE--YASKDDHRDFAGELEVLCKLgHHPNIINLLGAC-EHRGYLYLAIEYAP 759
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKIV----AIKRYRAntYCSKSDVDMFCREVSILCRL-NHPCVIQFVGAClDDPSQFAIVTQYVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLldflrksrvletdpaFAIANSTASTLSSQQLLHFAADVARGMDYL--SQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd14064   76 GGSL---------------FSLLHEQKRVIDLQSKLIIAVDVAKGMEYLhnLTQPIIHRDLNSHNILLYEDGHAVVADFG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRGQEVYVKKTMGRLP--VRWMAIESLNYSV-YTTNSDVWSYGVLLWEIVSlGGTPYCGM----TCAEL-YEKL--PQG 907
Cdd:cd14064  141 ESRFLQSLDEDNMTKQPgnLRWMAPEVFTQCTrYSIKADVFSYALCLWELLT-GEIPFAHLkpaaAAADMaYHHIrpPIG 219
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 908 YRLEKPlncddeVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14064  220 YSIPKP------ISSLLMRGWNAEPESRPSFVEIVALL 251
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
683-945 4.86e-33

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


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 128.72  E-value: 4.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdgLRMDAAIKRMKEYASKDDHR-DFAGELEVLCKLGHhPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd13978    1 LGSGGFGTVSKARHVS--WFGMVAIKCLHSSPNCIEERkALLKEAEKMERARH-SYVLPLLGVCVERRSLGLVMEYMENG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKsrvLETDPAFAIanstastlsSQQLLHfaaDVARGMDYL--SQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd13978   78 SLKSLLER---EIQDVPWSL---------RFRIIH---EIALGMNFLhnMDPPLLHHDLKPENILLDNHFHVKISDFGLS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R-------GQEVYVKKTMGRLPVrWMAIESLN--YSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMT-CAELYEKLPQGYR 909
Cdd:cd13978  143 KlgmksisANRRRGTENLGGTPI-YMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAInPLLIMQIVSKGDR 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 910 LEKPLNCDD-------EVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd13978  221 PSLDDIGRLkqienvqELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
682-942 5.67e-33

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: 128.35  E-value: 5.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd08215    7 VIGKGSFGSAYLVRRKSDGKLY--VLKEIDLSNMSEKEREEAlNEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEYADG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKsrvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd08215   84 GDLAQKIKK------------QKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 --GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAEL--------YEKLPQGYrl 910
Cdd:cd08215  152 vlESTTDLAKTVVGTPY-YLSPELCENKPYNYKSDIWALGCVLYELCTL-KHPFEANNLPALvykivkgqYPPIPSQY-- 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 911 ekplncDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08215  228 ------SSELRDLVNSMLQKDPEKRPSANEIL 253
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
683-941 1.64e-32

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 127.41  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd05087    5 IGHGWFGKVFLGEVNSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHT-NLLQCLAQCAEVTPYLLVMEFCPLGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVLEtdpafaiaNSTASTLSSQQLlhfAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd05087   84 LKGYLRSCRAAE--------SMAPDPLTLQRM---ACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHck 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 -GQEVYVKKTMGRLPVRWMAIE-------SLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAEL--YEKLPQGYRL 910
Cdd:cd05087  153 yKEDYFVTADQLWVPLRWIAPElvdevhgNLLVVDQTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVltYTVREQQLKL 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 911 EKP---LNCDDEVYDLMRQCWREkPYERPSFAQI 941
Cdd:cd05087  233 PKPqlkLSLAERWYEVMQFCWLQ-PEQRPTAEEV 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
679-942 7.58e-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: 125.03  E-value: 7.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd06627    4 LGDLIGRGAFGSVYKGLNLNTGEFV--AIKQISlEKIPKSDLKSVMGEIDLLKKL-NHPNIVKYIGSVKTKDSLYIILEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRK-SRVLETDPAFAIAnstastlssqQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd06627   81 VENGSLASIIKKfGKFPESLVAVYIY----------QVLE-------GLAYLHEQGVIHRDIKGANILTTKDGLVKLADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLS-RGQEVyvkKTMGRLPV---RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYcgmtcaelYEKLPQG--YRL 910
Cdd:cd06627  144 GVAtKLNEV---EKDENSVVgtpYWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPY--------YDLQPMAalFRI 211
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 911 EK------PLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06627  212 VQddhpplPENISPELRDFLLQCFQKDPTLRPSAKELL 249
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
678-942 9.13e-32

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: 124.55  E-value: 9.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRM-KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd14003    3 ELGKTLGEGSFGKVKLARHKLTG--EKVAIKIIdKSKLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENKIYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVLETDPA---FaianstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd14003   80 YASGGELFDYIVNNGRLSEDEArrfF------------QQLIS-------AVDYCHSNGIVHRDLKLENILLDKNGNLKI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSR--GQEVYVKKTMGRLPvrWMAIESLN---YsvYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd14003  141 IDFGLSNefRGGSLLKTFCGTPA--YAAPEVLLgrkY--DGPKADVWSLGVILYAMLT-GYLPFDDDNDSKLFRKILKGK 215
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 909 rLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14003  216 -YPIPSHLSPDARDLIRRMLVVDPSKRITIEEIL 248
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
675-937 9.87e-32

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: 125.41  E-value: 9.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDFAG-ELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEY--AIKVLdKRHIIKEKKVKYVTiEKEVLSRL-AHPGIVKLYYTFQDESKLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05581   78 FVLEYAPNGDLLEYIRK----------------YGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFG----LSRGQEVYVKKTMGRLPVRWMAI--------------ESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd05581  142 ITDFGtakvLGPDSSPESTKGDADSQIAYNQAraasfvgtaeyvspELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRG 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 895 MTCAELYEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPS 937
Cdd:cd05581  221 SNEYLTFQKIVKL-EYEFPENFPPDAKDLIQKLLVLDPSKRLG 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
681-952 1.11e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 130.13  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARikKDGLRMDAAIKRMKEYASKDDH--RDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:COG0515   13 RLLGRGGMGVVYLAR--DLRLGRPVALKVLRPELAADPEarERFRREARALARL-NHPNIVRVYDVGEEDGRPYLVMEYV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:COG0515   90 EGESLADLLRRRG----------------PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRGQEVYVKKTMGRLP--VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRL---EKP 913
Cdd:COG0515  154 ARALGGATLTQTGTVVgtPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPppsELR 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERP-SFAQILVSLNRMLEER 952
Cdd:COG0515  233 PDLPPALDAIVLRALAKDPEERYqSAAELAAALRAVLRSL 272
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
680-945 4.65e-31

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: 123.08  E-value: 4.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGlRmDAAIKRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLG-R-PVAIKVLRPELAEDEefRERFLREARALARL-SHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd14014   82 VEGGSLADLLRERG----------------PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSR----GQEVYVKKTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE-LYEKLPQGYRLEK 912
Cdd:cd14014  146 IARalgdSGLTQTGSVLGTPA--YMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAvLAKHLQEAPPPPS 222
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 913 PLNCD--DEVYDLMRQCWREKPYERP-SFAQILVSL 945
Cdd:cd14014  223 PLNPDvpPALDAIILRALAKDPEERPqSAAELLAAL 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
678-942 8.13e-31

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: 121.93  E-value: 8.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd06614    3 KNLEKIGEGASGEVYKATDRATG--KEVAIKKMR--LRKQNKELIINEILIM-KECKHPNIVDYYDSYLVGDELWVVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd06614   78 MDGGSLTDIITQNPV---------------RMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE-LY----EKLPqgyRL 910
Cdd:cd06614  143 FAAqlTKEKSKRNSVVGTPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEMAE-GEPPYLEEPPLRaLFlittKGIP---PL 217
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06614  218 KNPEKWSPEFKDFLNKCLVKDPEKRPSAEELL 249
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
683-937 1.95e-30

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: 121.54  E-value: 1.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC-EHRGYLyLAIEYAPHG 761
Cdd:cd05042    3 IGNGWFGKVLLGEIYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRIL-QHPNILQCLGQCvEAIPYL-LVMEFCDLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRVLETDPAfaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL--S 839
Cdd:cd05042   81 DLKAYLRSEREHERGDS-----------DTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLahS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RGQEVYVkKTMGRL--PVRWMAIESL-----NYSVY--TTNSDVWSYGVLLWEIVSLGGTPY--------CGMTCAELYE 902
Cdd:cd05042  150 RYKEDYI-ETDDKLwfPLRWTAPELVtefhdRLLVVdqTKYSNIWSLGVTLWELFENGAQPYsnlsdldvLAQVVREQDT 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 903 KLPQGyRLEKPLNcdDEVYDLMRQCWREkPYERPS 937
Cdd:cd05042  229 KLPKP-QLELPYS--DRWYEVLQFCWLS-PEQRPA 259
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
683-946 2.25e-30

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: 121.60  E-value: 2.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14206    5 IGNGWFGKVILGEIFSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSL-QHPNILQCLGLCTETIPFLLIMEFCQLGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVletdpafaiANSTASTLSSQQLL---HFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14206   84 LKRYLRAQRK---------ADGMTPDLPTRDLRtlqRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RG---QEVYVKKTMGRLPVRWMAIESL-----NYSVY--TTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKL--PQG 907
Cdd:cd14206  155 HNnykEDYYLTPDRLWIPLRWVAPELLdelhgNLIVVdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVvrEQQ 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 908 YRLEKP---LNCDDEVYDLMRQCWReKPYERPSFAQILVSLN 946
Cdd:cd14206  235 MKLAKPrlkLPYADYWYEIMQSCWL-PPSQRPSVEELHLQLS 275
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
682-946 5.73e-30

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: 120.41  E-value: 5.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRM----------------DAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC 745
Cdd:cd14000    1 LLGDGGFGSVYRASYKGEPVAVkifnkhtssnfanvpaDTMLRHLRATDAMKNFRLLRQELTVLSHL-HHPSIVYLLGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRgyLYLAIEYAPHGNLLDFLRKSRvletdPAFAianSTASTLSSQQLLHfaadVARGMDYLSQKQFIHRDLAARNILV 825
Cdd:cd14000   80 IHP--LMLVLELAPLGSLDHLLQQDS-----RSFA---SLGRTLQQRIALQ----VADGLRYLHSAMIIYRDLKSHNVLV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYV-----AKIADFGLSRGQEVYVKKTMGRLPvRWMAIESLNYSV-YTTNSDVWSYGVLLWEIVSlGGTPYCG----M 895
Cdd:cd14000  146 WTLYPnsaiiIKIADYGISRQCCRMGAKGSEGTP-GFRAPEIARGNViYNEKVDVFSFGMLLYEILS-GGAPMVGhlkfP 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 896 TCAELYEKLPQ--GYRLEKPLNCddeVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd14000  224 NEFDIHGGLRPplKQYECAPWPE---VEVLMKKCWKENPQQRPTAVTVVSILN 273
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
675-942 3.00e-29

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 118.57  E-value: 3.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKE-YASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATG--EIVAIKKFKEsEDDEDVKKTALREVKVL-RQLRHENIVNLKEAFRRKGRLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHgNLLDFLRKSRVlETDPAfaianstASTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd07833   78 VFEYVER-TLLELLEASPG-GLPPD-------AVRSYIWQLL-------QAIAYCHSHNIIHRDIKPENILVSESGVLKL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSR-----GQEVYVKKtmgrLPVRWM-AIESL-NYSVYTTNSDVWSYGVLLWEIVS-------------------- 886
Cdd:cd07833  142 CDFGFARaltarPASPLTDY----VATRWYrAPELLvGDTNYGKPVDVWAIGCIMAELLDgeplfpgdsdidqlyliqkc 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 887 LGGTP------------YCGMTCAELYEKLPQGYRLEKplNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07833  218 LGPLPpshqelfssnprFAGVAFPEPSQPESLERRYPG--KVSSPALDFLKACLRMDPKERLTCDELL 283
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
678-942 5.81e-29

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: 116.81  E-value: 5.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHKKTGEEY--AVKIIdKKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFL-RKSRVLETDPAFAIanstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV---GENYVAK 832
Cdd:cd05117   80 LCTGGELFDRIvKKGSFSEREAAKIM----------KQIL-------SAVAYLHSQGIVHRDLKPENILLaskDPDSPIK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSRG-QEVYVKKTM-GRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWeiVSLGGT-PYCGMTCAELYEKLPQG-Y 908
Cdd:cd05117  143 IIDFGLAKIfEEGEKLKTVcGTP--YYVAPEVLKGKGYGKKCDIWSLGVILY--ILLCGYpPFYGETEQELFEKILKGkY 218
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 909 RLEKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd05117  219 SFDSPEwkNVSEEAKDLIKRLLVVDPKKRLTAAEAL 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
683-938 4.20e-28

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 114.24  E-value: 4.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLrmDAAIKRM-KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGE--VVAIKEIsRKKLNKKLQENLESEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADFGL 838
Cdd:cd14009   78 DLSQYIRKRGRLPEAVA----------------RHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRG-QEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAEL---YEKLPQGYRLEKPL 914
Cdd:cd14009  142 ARSlQPASMAETLCGSPL-YMAPEILQFQKYDAKADLWSVGAILFEML-VGKPPFRGSNHVQLlrnIERSDAVIPFPIAA 219
                        250       260
                 ....*....|....*....|....
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd14009  220 QLSPDCKDLLRRLLRRDPAERISF 243
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
679-942 9.35e-28

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: 113.25  E-value: 9.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDV--IGEGNFGQVLKARIKKDGLRMdaAIKR-MKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd13997    2 FHELeqIGSGSFSEVFKVRSKVDGCLY--AVKKsKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKsrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd13997   80 ELCENGSLQDALEE-------------LSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLsrgqevyVKKTMGRLPV-----RWMAIESLNYS-VYTTNSDVWSYGVLLWEIVSLGGTPYCGmtcaELYEKLPQGYr 909
Cdd:cd13997  147 FGL-------ATRLETSGDVeegdsRYLAPELLNENyTHLPKADIFSLGVTVYEAATGEPLPRNG----QQWQQLRQGK- 214
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 910 LEKPLNC--DDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd13997  215 LPLPPGLvlSQELTRLLKVMLDPDPTRRPTADQLL 249
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
681-942 1.56e-27

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: 112.69  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKeYASKDDHRD-FAGELEVLCKlGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd06623    7 KVLGQGSSGVVYKVRHKPTGKIY--ALKKIH-VDGDEEFRKqLLRELKTLRS-CESPYVVKCYGAFYKEGEISIVLEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd06623   83 GGSLADLLKKVG----------------KIPEPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRGQEVYVKKTM---GrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIvSLGGTPYC---GMTCAELYEKLPQG--YRL 910
Cdd:cd06623  147 SKVLENTLDQCNtfvG--TVTYMSPERIQGESYSYAADIWSLGLTLLEC-ALGKFPFLppgQPSFFELMQAICDGppPSL 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 911 EkPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06623  224 P-AEEFSPEFRDFISACLQKDPKKRPSAAELL 254
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
683-948 1.56e-27

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: 112.99  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaaikRMKEYASKDD--HRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVM-----VMKELIRFDEeaQRNFLKEVKVM-RSLDHPNVLKFIGVLYKDKKLNLITEYIPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd14154   75 GTLKDVLK---------------DMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLAR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 ----------GQEVYVKKTMGRLPVR-----------WMAIESLNYSVYTTNSDVWSYGVLLWEIVS-LGGTPYC----- 893
Cdd:cd14154  140 liveerlpsgNMSPSETLRHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGrVEADPDYlprtk 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 894 --GMTCAELYEKLPQGyrlekplnCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14154  220 dfGLNVDSFREKFCAG--------CPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
683-948 2.31e-27

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 112.98  E-value: 2.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdglrMDAAIKR---MKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14158   23 LGEGGFGVVFKGYIND----KNVAVKKlaaMVDISTEDLTKQFEQEIQVMAKC-QHENLVELLGYSCDGPQLCLVYTYMP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLrksrvletdpafAIANSTAStLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14158   98 NGSLLDRL------------ACLNDTPP-LSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RGQEVYVKKTMGRLPV---RWMAIESLNYSVyTTNSDVWSYGVLLWEIVSlgGTPycgmtcAELYEKLPQGYRLEKPLNC 916
Cdd:cd14158  165 RASEKFSQTIMTERIVgttAYMAPEALRGEI-TPKSDIFSFGVVLLEIIT--GLP------PVDENRDPQLLLDIKEEIE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 917 DDE---------------------VYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14158  236 DEEktiedyvdkkmgdwdstsieaMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
683-943 3.22e-27

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: 111.88  E-value: 3.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRmdAAIK--------RMKEYAS-----KDDHRDFAGELEVLCKLgHHPNIINLLGACE--H 747
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQL--YAIKifnksrlrKRREGKNdrgkiKNALDDVRREIAIMKKL-DHPNIVRLYEVIDdpE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 RGYLYLAIEYAPHGNLLDFLRKSRVletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 827
Cdd:cd14008   78 SDKLYLVLEYCEGGPVMELDSGDRV--------------PPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVAKIADFGLSR---GQEVYVKKTMGR---LPVRWMAIESLNYSVYttNSDVWSYGVLLWEIVsLGGTPYCGMTCAELY 901
Cdd:cd14008  144 DGTVKISDFGVSEmfeDGNDTLQKTAGTpafLAPELCDGDSKTYSGK--AADIWALGVTLYCLV-FGRLPFNGDNILELY 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 902 EK-LPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILV 943
Cdd:cd14008  221 EAiQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIKE 263
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
673-945 7.48e-27

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: 110.94  E-value: 7.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWNDIKFQDVIGEGNFGQVLKARIKKDGLrmdaAIKRMKEYASKDDHRD-FAGELEVLcKLgHHPNIINLLGA--CEHRG 749
Cdd:cd13979    1 DWEPLRLQEPLGSGGFGSVYKATYKGETV----AVKIVRRRRKNRASRQsFWAELNAA-RL-RHENIVRVLAAetGTDFA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAI-EYAPHGNLldflrKSRVLETDPAfaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd13979   75 SLGLIImEYCGNGTL-----QQLIYEGSEP----------LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLS------RGQEVYVKKTMGRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYE 902
Cdd:cd13979  140 GVCKLCDFGCSvklgegNEVGTPRSHIGGTY--TYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQHVLYA 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 759191595 903 KLPQGYRLEKPLNCDDEVYD----LMRQCWREKPYERPS-FAQILVSL 945
Cdd:cd13979  217 VVAKDLRPDLSGLEDSEFGQrlrsLISRCWSAQPAERPNaDESLLKSL 264
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
664-942 1.08e-26

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: 110.85  E-value: 1.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 664 PDPTiypvldwNDIKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDhrDFAGELEVLCKLGHHPNIINLLG 743
Cdd:cd06608    2 PDPA-------GIFELVEVIGEGTYGKVYKARHKKTG--QLAAIKIMDIIEDEEE--EIKLEINILRKFSNHPNIATFYG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 744 A------CEHRGYLYLAIEYAPHGNLLDFLRKSRVLetdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRD 817
Cdd:cd06608   71 AfikkdpPGGDDQLWLVMEYCGGGSVTDLVKGLRKK------------GKRLKEEWIAYILRETLRGLAYLHENKVIHRD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 818 LAARNILVGENYVAKIADFGLSRgqevYVKKTMGRlpvR--------WMAIE------SLNYSvYTTNSDVWSYGVLLWE 883
Cdd:cd06608  139 IKGQNILLTEEAEVKLVDFGVSA----QLDSTLGR---RntfigtpyWMAPEviacdqQPDAS-YDARCDVWSLGITAIE 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 884 IVSlGGTPYCGMTCAELYEKLPQGY--RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06608  211 LAD-GKPPLCDMHPMRALFKIPRNPppTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELL 270
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
683-950 1.33e-26

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: 109.92  E-value: 1.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIkrmkeYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKI-----YKNDVDQHKIVREISLLQKL-SHPNIVRYLGICVKDEKLHPILEYVSGGC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADFGLS 839
Cdd:cd14156   75 LEELLAREEL---------------PLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGREAVVTDFGLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RgqevyvkkTMGRLPVR-------------WMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------LGGTPYCGMTCA 898
Cdd:cd14156  140 R--------EVGEMPANdperklslvgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEILAripadpevLPRTGDFGLDVQ 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 899 ELYEKLPqgyrlekplNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd14156  212 AFKEMVP---------GCPEPFLDLAASCCRMDAFKRPSFAELLDELEDIAE 254
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
682-946 2.92e-26

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: 108.89  E-value: 2.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDglrmDAAIKRMKEYASkddHRDFAGELEVLCKLgHHPNIINLLGACEHRgyLYLAIEYAPHG 761
Cdd:cd14068    1 LLGDGGFGSVYRAVYRGE----DVAVKIFNKHTS---FRLLRQELVVLSHL-HHPSLVALLAAGTAP--RMLVMELAPKG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLldflrkSRVLETDPAfaianSTASTLSSQQLLHfaadVARGMDYLSQKQFIHRDLAARNILVGENY-----VAKIADF 836
Cdd:cd14068   71 SL------DALLQQDNA-----SLTRTLQHRIALH----VADGLRYLHSAMIIYRDLKPHNVLLFTLYpncaiIAKIADY 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSR-GQEVYVKKTMGRLPVRWMAIESLNYsVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL- 914
Cdd:cd14068  136 GIAQyCCRMGIKTSEGTPGFRAPEVARGNV-IYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPDPVk 214
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 915 --NCDD--EVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd14068  215 eyGCAPwpGVEALIKDCLKENPQCRPTSAQVFDILN 250
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
675-942 3.60e-26

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: 108.97  E-value: 3.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIM--AVKVIRLEIDEALQKQILRELDVLHK-CNSPYIVGFYGAFYSEGDISIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETDPAFAIANStastlssqqllhfaadVARGMDYL-SQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd06605   78 MEYMDGGSLDKILKEVGRIPERILGKIAVA----------------VVKGLIYLhEKHKIIHRDVKPSNILVNSRGQVKL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSrGQEV-YVKKT-MGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEiVSLGGTPY------CGMTCAELYE--- 902
Cdd:cd06605  142 CDFGVS-GQLVdSLAKTfVGTRS--YMAPERISGGKYTVKSDIWSLGLSLVE-LATGRFPYpppnakPSMMIFELLSyiv 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 903 -----KLPQGyrlekplNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06605  218 depppLLPSG-------KFSPDFQDFVSQCLQKDPTERPSYKELM 255
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
676-944 4.00e-26

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: 108.63  E-value: 4.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDN--QVYALKEVNlGSLSQKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd08530   78 MEYAPFGDLSKLISKRKKKRR------------LFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRGQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd08530  146 DLGISKVLKKNLAKTQIGTPL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMATF-RPPFEARTMQELRYKVCRGKFPPIPP 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVS 944
Cdd:cd08530  224 VYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
683-942 6.48e-26

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: 108.78  E-value: 6.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDH---RdfagELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd07830    7 LGDGTFGSVYLARNKETGELV--AIKKMKkKFYSWEECmnlR----EVKSLRKLNEHPNIVKLKEVFRENDELYFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 pHGNLLDFL--RKSRVLETDPAFAIanstastlsSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd07830   81 -EGNLYQLMkdRKGKPFSESVIRSI---------IYQIL-------QGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRgqEV--------YVKktmgrlpVRWM-AIESLNYS-VYTTNSDVWSYGVL-------------------LWEIVSL 887
Cdd:cd07830  144 GLAR--EIrsrppytdYVS-------TRWYrAPEILLRStSYSSPVDIWALGCImaelytlrplfpgsseidqLYKICSV 214
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 888 GGTPycGMT--------CAELYEKLPQ--GYRLEKPL-NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07830  215 LGTP--TKQdwpegyklASKLGFRFPQfaPTSLHQLIpNASPEAIDLIKDMLRWDPKKRPTASQAL 278
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
683-952 7.70e-26

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: 107.56  E-value: 7.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKrMKEYASkdDHRDFAGELEVLCKLGHhPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVM--ALK-MNTLSS--NRANMLREVQLMNRLSH-PNILRFMGVCVHQGQLHALTEYINGGN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVLetdpafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADFGLS 839
Cdd:cd14155   75 LEQLLDSNEPL----------------SWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RGQEVYvKKTMGRLPV----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------LGGTPYCGMTCAELYEKLPqg 907
Cdd:cd14155  139 EKIPDY-SDGKEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIAriqadpdyLPRTEDFGLDYDAFQHMVG-- 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 908 yrlekplNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEER 952
Cdd:cd14155  216 -------DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILEKL 253
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
679-942 9.91e-26

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: 107.35  E-value: 9.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyaSKDDHRDFAGELEVL--CKlghHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd06612    7 ILEKLGEGSYGSVYKAIHKETG--QVVAIKVVP---VEEDLQEIIKEISILkqCD---SPYIVKYYGSYFKNTDLWIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDflrksrvletdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd06612   79 YCGAGSVSD---------------IMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSrGQEVYV---KKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM----TCAELYEKLPQGyr 909
Cdd:cd06612  144 GVS-GQLTDTmakRNTVIGTPF-WMAPEVIQEIGYNNKADIWSLGITAIEMAE-GKPPYSDIhpmrAIFMIPNKPPPT-- 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06612  219 LSDPEKWSPEFNDFVKKCLVKDPEERPSAIQLL 251
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
681-942 1.73e-25

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: 106.88  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMDAAIK---RMKeyASKDD-HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd14080    6 KTIGEGSYSKVKLAEYTKSGLKEKVACKiidKKK--APKDFlEKFLPRELEILRKL-RHPNIIQVYSIFERGSKVFIFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRvletdpafAIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd14080   83 YAEHGDLLEYIQKRG--------ALSESQARIWFRQ--------LALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRgqevYVKKTMGRLPVR-------WMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL---P 905
Cdd:cd14080  147 GFAR----LCPDDDGDVLSKtfcgsaaYAAPEILQGIPYDpKKYDIWSLGVILYIMLC-GSMPFDDSNIKKMLKDQqnrK 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 906 QGYRlEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14080  222 VRFP-SSVKKLSPECKDLIDQLLEPDPTKRATIEEIL 257
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
680-942 1.92e-25

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: 106.95  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd06609    6 LERIGKGSFGEVYKGIDKRTNQVV--AIKVIDLEEAEDEIEDIQQEIQFLSQC-DSPYITKYYGSFLKGSKLWIIMEYCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAFAIanstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd06609   83 GGSVLDLLKPGPLDETYIAFIL----------REVLL-------GLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 rGQevyVKKTMGRL------PVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQgyrlEKP 913
Cdd:cd06609  146 -GQ---LTSTMSKRntfvgtPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVLFLIPK----NNP 215
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 914 LNCDDEVY-----DLMRQCWREKPYERPSFAQIL 942
Cdd:cd06609  216 PSLEGNKFskpfkDFVELCLNKDPKERPSAKELL 249
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
682-893 5.30e-25

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: 105.03  E-value: 5.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRmdAAIKR-MKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYApH 760
Cdd:cd14002    8 LIGEGSFGKVYKGRRKYTGQV--VALKFiPKRGKSEKELRNLRQEIEILRKL-NHPNIIEMLDSFETKKEFVVVTEYA-Q 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPAFAIAnstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd14002   84 GELFQILEDDGTLPEEEVRSIA---------KQLV-------SALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 841 GQEV------YVKKTmgrlPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYC 893
Cdd:cd14002  148 AMSCntlvltSIKGT----PL-YMAPELVQEQPYDHTADLWSLGCILYELF-VGQPPFY 200
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
681-942 7.59e-25

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: 104.62  E-value: 7.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMK--EYASKDDHRDFAGeLEVLCKLGHHPNIINLLGACEHRG--YLYLAIE 756
Cdd:cd05118    5 RKIGEGAFGTVWLARDKVTGEKV--AIKKIKndFRHPKAALREIKL-LKHLNDVEGHPNIVKLLDVFEHRGgnHLCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHgNLLDFLRKSRVLETDPAfaiansTASTLssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV-GENYVAKIAD 835
Cdd:cd05118   82 LMGM-NLYELIKDYPRGLPLDL------IKSYL--YQLL-------QALDFLHSNGIIHRDLKPENILInLELGQLKLAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRgqeVYVKKTMGRLPV-RW-MAIES-LNYSVYTTNSDVWSYGVLLWEIVSlgGTP-YCGmtcaelYEKLPQGYRLE 911
Cdd:cd05118  146 FGLAR---SFTSPPYTPYVAtRWyRAPEVlLGAKPYGSSIDIWSLGCILAELLT--GRPlFPG------DSEVDQLAKIV 214
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 912 KPLNcDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd05118  215 RLLG-TPEALDLLSKMLKYDPAKRITASQAL 244
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
682-942 8.71e-25

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: 104.92  E-value: 8.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYA----SKDDHRD----FAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELM--AVKQVELPSvsaeNKDRKKSmldaLQREIALLREL-QHENIVQYLGSSSDANHLNI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd06628   84 FLEYVPGGSVATLL----------------NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEV--YVKKTMGRLP-----VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQ 906
Cdd:cd06628  148 SDFGISKKLEAnsLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGE 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 907 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06628  227 NASPTIPSNISSEARDFLEKTFEIDHNKRPTADELL 262
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
683-950 1.03e-24

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: 104.71  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARikkdgLRMDAAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAiEYAPHG 761
Cdd:cd14150    8 IGTGSFGTVFRGK-----WHGDVAVKILKvTEPTPEQLQAFKNEMQVLRKT-RHVNILLFMGFMTRPNFAIIT-QWCEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLdflRKSRVLETdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd14150   81 SLY---RHLHVTET------------RFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 QEVYVKKTMGRLP---VRWMAIESL---NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA-ELYEKLPQGYrLEKPL 914
Cdd:cd14150  146 KTRWSGSQQVEQPsgsILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRdQIIFMVGRGY-LSPDL 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 759191595 915 -----NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 950
Cdd:cd14150  224 sklssNCPKAMKRLLIDCLKFKREERPLFPQILVSIELLQR 264
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
683-941 2.93e-24

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: 103.49  E-value: 2.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaaikRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVM-----VMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRksrvlETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd14222   75 GTLKDFLR-----ADDP-----------FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSR 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 -----------GQEVYVKKTMGRLPVR----------WMAIESLNYSVYTTNSDVWSYGVLLWEIV-SLGGTPYC----- 893
Cdd:cd14222  139 liveekkkpppDKPTTKKRTLRKNDRKkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIgQVYADPDClprtl 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 894 --GMTCAELYEKLpqgyrleKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14222  219 dfGLNVRLFWEKF-------VPKDCPPAFFPLAAICCRLEPDSRPAFSKL 261
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
683-942 3.93e-24

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: 102.77  E-value: 3.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKeYASKDDHRDFAGELEVL--CKlghHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd06613    8 IGSGTYGDVYKARNIATG--ELAAVKVIK-LEPGDDFEIIQQEISMLkeCR---HPNIVAYFGSYLRRDKLWIVMEYCGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLrksrvLETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSr 840
Cdd:cd06613   82 GSLQDIY-----QVTGP-----------LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVS- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQevyVKKTMGRlpvR--------WMAIESLN---YSVYTTNSDVWSygvllweivslggtpyCGMTCAELYEKLPQ--- 906
Cdd:cd06613  145 AQ---LTATIAK---RksfigtpyWMAPEVAAverKGGYDGKCDIWA----------------LGITAIELAELQPPmfd 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 907 ----------GYRLEKPLNCDD------EVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06613  203 lhpmralfliPKSNFDPPKLKDkekwspDFHDFIKKCLTKNPKKRPTATKLL 254
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
683-945 4.18e-24

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: 102.47  E-value: 4.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARikkdgLRMDAAIKRMKEYA-SKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGylyLAI--EYAP 759
Cdd:cd14062    1 IGSGSFGTVYKGR-----WHGDVAVKKLNVTDpTPSQLQAFKNEVAVLRKT-RHVNILLFMGYMTKPQ---LAIvtQWCE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRksrVLETDpaFAIanstastlssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL- 838
Cdd:cd14062   72 GSSLYKHLH---VLETK--FEM----------LQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLa 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 ---SRGQ-EVYVKKTMGRlpVRWMAIESLNYSV---YTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE--LYEklpQGYR 909
Cdd:cd14062  137 tvkTRWSgSQQFEQPTGS--ILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDqiLFM---VGRG 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 910 LEKP------LNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14062  211 YLRPdlskvrSDTPKALRRLMEDCIKFQRDERPLFPQILASL 252
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
680-942 6.06e-24

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: 102.38  E-value: 6.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKdgLRMDAAIKRM-KEYASKDDHRDF-AGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14162    5 GKTLGHGSYAVVKKAYSTK--HKCKVAIKIVsKKKAPEDYLQKFlPREIEVIKGL-KHPNLICFYEAIETTSRVYIIMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRvletdpafAIANSTASTLSSQQLLhfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd14162   82 AENGDLLDYIRKNG--------ALPEPQARRWFRQLVA--------GVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRGQevyVKKTMGRLPVR--------WMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGY 908
Cdd:cd14162  146 FARGV---MKTKDGKPKLSetycgsyaYASPEILRGIPYDpFLSDIWSMGVVLYTMVY-GRLPFDDSNLKVLLKQVQRRV 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPyERPSFAQIL 942
Cdd:cd14162  222 VFPKNPTVSEECKDLILRMLSPVK-KRITIEEIK 254
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
681-942 2.78e-23

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: 100.32  E-value: 2.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSL-KHPNIVKFHDCFEDEENVYILLELCSN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS- 839
Cdd:cd14099   86 GSLMELLKRRK----------------ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAa 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 ----RGQEvyvKKTMGRLPvRWMAIESLNYSV-YTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQG-YRLEKP 913
Cdd:cd14099  150 rleyDGER---KKTLCGTP-NYIAPEVLEKKKgHSFEVDIWSLGVILYTLL-VGKPPFETSDVKETYKRIKKNeYSFPSH 224
                        250       260
                 ....*....|....*....|....*....
gi 759191595 914 LNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14099  225 LSISDEAKDLIRSMLQPDPTKRPSLDEIL 253
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
683-903 3.17e-23

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: 101.10  E-value: 3.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRmdAAIKRMKeyasKDDHRD-----FAGELEVLCKLgHHPNIINLL------GACEHRGYL 751
Cdd:cd07840    7 IGEGTYGQVYKARNKKTGEL--VALKKIR----MENEKEgfpitAIREIKLLQKL-DHPNVVRLKeivtskGSAKYKGSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHgnllDFlrkSRVLEtdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd07840   80 YMVFEYMDH----DL---TGLLD---------NPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRgqeVYVKKTMGRLPVRwmaIESLNY---------SVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYE 902
Cdd:cd07840  144 KLADFGLAR---PYTKENNADYTNR---VITLWYrppelllgaTRYGPEVDMWSVGCILAELF-TGKPIFQGKTELEQLE 216

                 .
gi 759191595 903 K 903
Cdd:cd07840  217 K 217
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
683-942 3.29e-23

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: 101.11  E-value: 3.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlRMdAAIKRMK--EYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd07841    8 LGEGTYAVVYKARDKETG-RI-VAIKKIKlgERKEAKDgiNFTALREIKLLQEL-KHPNIIGLLDVFGHKSNINLVFEFM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PhGNLLDFLRKSRVLetdpaFAIANSTASTLssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd07841   85 E-TDLEKVIKDKSIV-----LTPADIKSYML---MTL-------RGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRgQEVYVKKTMGRLPV-RWM-AIESL-NYSVYTTNSDVWSYGVLLWE-------------------IVSLGGTP----Y 892
Cdd:cd07841  149 AR-SFGSPNRKMTHQVVtRWYrAPELLfGARHYGVGVDMWSVGCIFAElllrvpflpgdsdidqlgkIFEALGTPteenW 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 893 CGMTCAELYEKLpqGYRLEKPL-----NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07841  228 PGVTSLPDYVEF--KPFPPTPLkqifpAASDDALDLLQRLLTLNPNKRITARQAL 280
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
720-948 4.90e-23

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: 99.48  E-value: 4.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 720 RDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKsrvletdpafaianSTASTLSSQQLLHFAA 799
Cdd:cd14057   37 RDFNEEYPRL-RIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHE--------------GTGVVVDQSQAVKFAL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 800 DVARGMDYL-SQKQFIHR-DLAARNILVGENYVAKI--ADFGLSRgQEVyvkktmGRL--PVrWMAIESLNYSVYTTN-- 871
Cdd:cd14057  102 DIARGMAFLhTLEPLIPRhHLNSKHVMIDEDMTARInmADVKFSF-QEP------GKMynPA-WMAPEALQKKPEDINrr 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 872 -SDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLP-QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14057  174 sADMWSFAILLWELVTR-EVPFADLSNMEIGMKIAlEGLRVTIPPGISPHMCKLMKICMNEDPGKRPKFDMIVPILEKM 251
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
681-942 4.94e-23

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: 99.92  E-value: 4.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDG----------LRMDAAIKRMkeyaskddhrdFAGELEVLCKLgHHPNIINLLgaceHR-- 748
Cdd:cd08217    6 ETIGKGSFGTVRKVRRKSDGkilvwkeidyGKMSEKEKQQ-----------LVSEVNILREL-KHPNIVRYY----DRiv 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 ----GYLYLAIEYAPHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDY-----LSQKQFIHRDLA 819
Cdd:cd08217   70 dranTTLYIVMEYCEGGDLAQLIKKCK------------KENQYIPEEFIWKIFTQLLLALYEchnrsVGGGKILHRDLK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 820 ARNILVGENYVAKIADFGLSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGMTC 897
Cdd:cd08217  138 PANIFLDSDNNVKLGDFGLARvlSHDSSFAKTYVGTPY-YMSPELLNEQSYDEKSDIWSLGCLIYELCAL-HPPFQAANQ 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 898 AELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08217  216 LELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELL 260
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
681-948 5.18e-23

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: 100.42  E-value: 5.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLrmdaAIKRmkeYASKDDhRDFAGELEVL-CKLGHHPNIINLLGA---CEHR-GYLYLAI 755
Cdd:cd14056    1 KTIGKGRYGEVWLGKYRGEKV----AVKI---FSSRDE-DSWFRETEIYqTVMLRHENILGFIAAdikSTGSwTQLWLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKsRVLETDPAFAIANSTASTLSSqqlLHFAAdvargMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd14056   73 EYHEHGSLYDYLQR-NTLDTEEALRLAYSAASGLAH---LHTEI-----VGTQGKPAIAHRDLKSKNILVKRDGTCCIAD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLS-RGQEVYVKKTMGRLP----VRWMAIESLNYSVYTTN------SDVWSYGVLLWEI---VSLGGT------PYCGM 895
Cdd:cd14056  144 LGLAvRYDSDTNTIDIPPNPrvgtKRYMAPEVLDDSINPKSfesfkmADIYSFGLVLWEIarrCEIGGIaeeyqlPYFGM 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 896 T-------------CAElyEKLPQgyrLEKPLNcDDEVY----DLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14056  224 VpsdpsfeemrkvvCVE--KLRPP---IPNRWK-SDPVLrsmvKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
735-941 7.39e-23

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: 99.50  E-value: 7.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVletdpafaianstasTLSSQQllHFAADVARGMDYLSQKQFI 814
Cdd:cd14027   50 HSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSV---------------PLSVKG--RIILEIIEGMAYLHGKGVI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 815 HRDLAARNILVGENYVAKIADFGL-------------SRGQEVY---VKKTMGRLpvRWMAIESLNySVY---TTNSDVW 875
Cdd:cd14027  113 HKDLKPENILVDNDFHIKIADLGLasfkmwskltkeeHNEQREVdgtAKKNAGTL--YYMAPEHLN-DVNakpTEKSDVY 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 876 SYGVLLWEIVSlGGTPY-CGMTCAELYEKLPQGYR---LEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14027  190 SFAIVLWAIFA-NKEPYeNAINEDQIIMCIKSGNRpdvDDITEYCPREIIDLMKLCWEANPEARPTFPGI 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
672-951 9.57e-23

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: 99.72  E-value: 9.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIkfQDVIGE---GNFGQVLKARIKKDGLrmdAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHR 748
Cdd:cd06644    8 LDPNEV--WEIIGElgdGAFGKVYKAKNKETGA---LAAAKVIETKSEEELEDYMVEIEILATC-NHPYIVKLLGAFYWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYAPHGNLldflrKSRVLETDPAfaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd06644   82 GKLWIMIEFCPGGAV-----DAIMLELDRG----------LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSrgqevyvKKTMGRLPVR--------WMA-----IESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGM 895
Cdd:cd06644  147 GDIKLADFGVS-------AKNVKTLQRRdsfigtpyWMApevvmCETMKDTPYDYKADIWSLGITLIEMAQI-EPPHHEL 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 896 TCAELYEKLPQGY--RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL-------VSLNRMLEE 951
Cdd:cd06644  219 NPMRVLLKIAKSEppTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQLLehpfvssVTSNRPLRE 283
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
675-945 1.07e-22

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: 98.90  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGA-CEHrGYLYL 753
Cdd:cd13996    6 NDFEEIELLGSGGFGSVYKVRNKVDG--VTYAIKKIRLTEKSSASEKVLREVKALAKL-NHPNIVRYYTAwVEE-PPLYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLETdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV-GENYVAK 832
Cdd:cd13996   82 QMELCEGGTLRDWIDRRNSSSK-------------NDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSRGQE-------VYVKKTMGRLP--------VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpycGMtc 897
Cdd:cd13996  149 IGDFGLATSIGnqkrelnNLNNNNNGNTSnnsvgigtPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKT---AM-- 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 898 aELYEKLPQGYRLEKPLNCDD---EVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd13996  224 -ERSTILTDLRNGILPESFKAkhpKEADLIQSLLSKNPEERPSAEQLLRSL 273
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
683-937 2.25e-22

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: 98.01  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC-EHRGYLyLAIEYAPHG 761
Cdd:cd05086    5 IGNGWFGKVLLGEIYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYIL-QHPNILQCVGQCvEAIPYL-LVFEFCDLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKsrvlETDPAFAIANSTastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL--S 839
Cdd:cd05086   83 DLKTYLAN----QQEKLRGDSQIM-------LLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RGQEVYVKKTMGRL-PVRWMAIE-------SLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYE--------K 903
Cdd:cd05086  152 RYKEDYIETDDKKYaPLRWTAPElvtsfqdGLLAAEQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNhvikerqvK 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 904 LPQGYrLEKPLNcdDEVYDLMRQCWReKPYERPS 937
Cdd:cd05086  232 LFKPH-LEQPYS--DRWYEVLQFCWL-SPEKRPT 261
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
682-942 2.51e-22

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: 97.34  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDG-------LRMDAAIKRMKEyASKDdhrdfagELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:cd08225    7 KIGEGSFGKIYLAKAKSDSehcvikeIDLTKMPVKEKE-ASKK-------EVILLAKM-KHPNIVTFFASFQENGRLFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN-YVAKI 833
Cdd:cd08225   78 MEYCDGGDLMKRINRQR--------------GVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRLE 911
Cdd:cd08225  144 GDFGIARqlNDSMELAYTCVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFAP 221
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08225  222 ISPNFSRDLRSLISQLFKVSPRDRPSITSIL 252
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
683-935 2.92e-22

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: 97.20  E-value: 2.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlRMdAAIKRM-KEYASKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTG-KL-YAMKVLrKKEIIKRKEVEHTlNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVL-ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05123   78 GELFSHLSKEGRFpEERARF-----------------YAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R--GQEVYVKKTM-GRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpqgyrLEKPLNC 916
Cdd:cd05123  141 KelSSDGDRTYTFcGTPE--YLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKI-----LKSPLKF 212
                        250       260
                 ....*....|....*....|...
gi 759191595 917 DD----EVYDLMRQCWREKPYER 935
Cdd:cd05123  213 PEyvspEAKSLISGLLQKDPTKR 235
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
676-948 3.23e-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: 97.42  E-value: 3.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARikkdgLRMDAAIKRMKEYASKDDHRDFAgELEVLC-KLGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd14063    1 ELEIKEVIGKGRFGRVHRGR-----WHGDVAIKLLNIDYLNEEQLEAF-KEEVAAyKNTRHDNLVLFMGACMDPPHLAIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVgENYVAKIA 834
Cdd:cd14063   75 TSLCKGRTLYSLIHERK---------------EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVIT 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLS------------------RGQEVYVK-KTMGRLPVRWMAIESLNysvYTTNSDVWSYGVLLWEIVSlGGTPYCGM 895
Cdd:cd14063  139 DFGLFslsgllqpgrredtlvipNGWLCYLApEIIRALSPDLDFEESLP---FTKASDVYAFGTVWYELLA-GRWPFKEQ 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 896 TcAE--LYEKlpqGYRLEKPLN---CDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14063  215 P-AEsiIWQV---GCGKKQSLSqldIGREVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
725-941 4.36e-22

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 97.08  E-value: 4.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 725 ELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVlETDPAFAIAnstastlssqqllhFAADVARG 804
Cdd:cd13992   46 ELNQLKEL-VHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREI-KMDWMFKSS--------------FIKDIVKG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 805 MDYLsQKQFI--HRDLAARNILVGENYVAKIADFGLS---RGQEVYVKKTMGRLPVR-WMAIESLNYSVYTTN----SDV 874
Cdd:cd13992  110 MNYL-HSSSIgyHGRLKSSNCLVDSRWVVKLTDFGLRnllEEQTNHQLDEDAQHKKLlWTAPELLRGSLLEVRgtqkGDV 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 875 WSYGVLLWEIVSLGGTPYCGMTCAELYE--------KLPQGYRLEKPlnCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd13992  189 YSFAIILYEILFRSDPFALEREVAIVEKvisggnkpFRPELAVLLDE--FPPRLVLLVKQCWAENPEKRPSFKQI 261
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
677-942 5.15e-22

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: 97.57  E-value: 5.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRM---KEYASKddhrdfagELEVLCKLgHHPNIINLLGACEHRG---- 749
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETG--EVVAIKKVlqdKRYKNR--------ELQIMRRL-KHPNIVKLKYFFYSSGekkd 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 --YLYLAIEYAPhGNLLDFLRK-SRVLETDPAFAIanstasTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV- 825
Cdd:cd14137   75 evYLNLVMEYMP-ETLYRVIRHySKNKQTIPIIYV------KLYSYQLF-------RGLAYLHSLGICHRDIKPQNLLVd 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYVAKIADFG----LSRGQE--------VYvkktmgRlpvrwmAIES-LNYSVYTTNSDVWSYG-VL----------- 880
Cdd:cd14137  141 PETGVLKLCDFGsakrLVPGEPnvsyicsrYY------R------APELiFGATDYTTAIDIWSAGcVLaelllgqplfp 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 881 -------LWEIVSLGGTPycgmTCAELYE--------KLPQGYR--LEKPLN--CDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14137  209 gessvdqLVEIIKVLGTP----TREQIKAmnpnytefKFPQIKPhpWEKVFPkrTPPDAIDLLSKILVYNPSKRLTALEA 284

                 .
gi 759191595 942 L 942
Cdd:cd14137  285 L 285
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
675-926 6.31e-22

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 97.26  E-value: 6.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEY---ASKD-DHrdFAGELEVLCKLgHHPNIINLLGACEHRGY 750
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYY--ALKILKKAkiiKLKQvEH--VLNEKRILSEV-RHPFIVNLLGSFQDDRN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05580   76 LYMVMEYVPGGELFSLLRRSGRFPNDVA----------------KFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRgqevYVKK---TMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG 907
Cdd:cd05580  140 IKITDFGFAK----RVKDrtyTLCGTP-EYLAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDENPMKIYEKILEG 213
                        250
                 ....*....|....*....
gi 759191595 908 yRLEKPLNCDDEVYDLMRQ 926
Cdd:cd05580  214 -KIRFPSFFDPDAKDLIKR 231
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
683-892 6.89e-22

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: 96.24  E-value: 6.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKddHRDFAGELEVLCKLGHHPNIINLLG-ACEHRGYLYLAIEYAPHG 761
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKM--ALKFVPKPSTK--LKDFLREYNISLELSVHPHIIKTYDvAFETEDYYVFAQEYAPYG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRVLETDpafaianstASTLSSQQllhfaadVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGLS 839
Cdd:cd13987   77 DLFSIIPPQVGLPEE---------RVKRCAAQ-------LASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLT 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 840 RGQEVYVKKTMGRLPvrWMAIESLNYS-----VYTTNSDVWSYGVLL---------WEIVSLGGTPY 892
Cdd:cd13987  141 RRVGSTVKRVSGTIP--YTAPEVCEAKknegfVVDPSIDVWAFGVLLfccltgnfpWEKADSDDQFY 205
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
675-942 8.06e-22

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: 96.74  E-value: 8.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGE---GNFGQVLKARIKKDGLRmdAAIKRMkEYASKDDHRDFAGELEVL--CKlghHPNIINLLGACEHRG 749
Cdd:cd06611    2 NPNDIWEIIGElgdGAFGKVYKAQHKETGLF--AAAKII-QIESEEELEDFMVEIDILseCK---HPNIVGLYEAYFYEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHGNLldflrKSRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd06611   76 KLWILIEFCDGGAL-----DSIMLELE----------RGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSrgqeVYVKKTMGR------LPvRWMAIESLNYSVYTTN-----SDVWSYGVLLWEIVSlGGTPYCGMTCA 898
Cdd:cd06611  141 DVKLADFGVS----AKNKSTLQKrdtfigTP-YWMAPEVVACETFKDNpydykADIWSLGITLIELAQ-MEPPHHELNPM 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 759191595 899 ELYEKLPQGY--RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06611  215 RVLLKILKSEppTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELL 260
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
716-946 8.61e-22

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: 96.01  E-value: 8.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 716 KDDHRDFAG---ELEVLCKLGHHPNIINLLGACEHRGYLyLAIEYAPHGNLLDFLRKSRVLetdpafaianstastLSSQ 792
Cdd:cd05037   39 DSDHRDISEsffETASLMSQISHKHLVKLYGVCVADENI-MVQEYVRYGPLDKYLRRMGNN---------------VPLS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 793 QLLHFAADVARGMDYLSQKQFIHRDLAARNILV------GENYVAKIADFGLSRGqevYVKKTMGRLPVRWMAIESLN-- 864
Cdd:cd05037  103 WKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregldGYPPFIKLSDPGVPIT---VLSREERVDRIPWIAPECLRnl 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 865 YSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPlNCDdEVYDLMRQCWREKPYERPSFAQILVS 944
Cdd:cd05037  180 QANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPAP-DCA-ELAELIMQCWTYEPTKRPSFRAILRD 257

                 ..
gi 759191595 945 LN 946
Cdd:cd05037  258 LN 259
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
683-886 1.30e-21

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: 96.43  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdglrMDAAIKRMKEYASKD---DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14159    1 IGEGGFGCVYQAVMRN----TEYAVKRLKEDSELDwsvVKNSFLTEVEKLSRF-RHPNIVDLAGYSAQQGNYCLIYVYLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKsrvlETD-PAfaianstastLSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARNILVGENYVAKIADF 836
Cdd:cd14159   76 NGSLEDRLHC----QVScPC----------LSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDF 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 837 GLSR--------------GQEVYVKKTMGRLPVRWMAIESLnysvyTTNSDVWSYGVLLWEIVS 886
Cdd:cd14159  142 GLARfsrrpkqpgmsstlARTQTVRGTLAYLPEEYVKTGTL-----SVEIDVYSFGVVLLELLT 200
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
681-942 1.34e-21

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: 96.23  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGA------CEHRGYLYLA 754
Cdd:cd06636   22 EVVGNGTYGQVYKGRHVKTG--QLAAIKVMD--VTEDEEEEIKLEINMLKKYSHHRNIATYYGAfikkspPGHDDQLWLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd06636   98 MEFCGAGSVTDLVK--------------NTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSrgqeVYVKKTMGRLPV-----RWMAIESLNY-----SVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 904
Cdd:cd06636  164 DFGVS----AQLDRTVGRRNTfigtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 905 PQG--YRLeKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06636  239 PRNppPKL-KSKKWSKKFIDFIEGCLVKNYLSRPSTEQLL 277
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
681-942 1.46e-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: 95.16  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGlRMDAaikrMKE--YASKDDHRDFA-----GELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTG-DFFA----VKEvsLVDDDKKSRESvkqleQEIALLSKL-RHPNIVQYYGTEREEDNLYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLEtDPAfaIANSTastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd06632   80 FLEYVPGGSIHKLLQRYGAFE-EPV--IRLYT------RQIL-------SGLAYLHSRNTVHRDIKGANILVDTNGVVKL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQE--VYVKKTMGRlpVRWMAIESLN--YSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYR 909
Cdd:cd06632  144 ADFGMAKHVEafSFAKSFKGS--PYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGVAAIFKIGNSGE 220
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 910 L-EKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06632  221 LpPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLL 254
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
678-942 1.76e-21

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: 94.68  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKE--YASKDDHRDFAgELEVLCKLGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd14050    4 TILSKLGEGSFGEVFKVRSREDGKLY--AVKRSRSrfRGEKDRKRKLE-EVERHEKLGEHPNCVRFIKAWEEKGILYIQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYApHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd14050   81 ELC-DTSLQQYCEET----------------HSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRGQEVYVKKTMGRLPVRWMAIESLNySVYTTNSDVWSYGVLLWEIVSLGGTPYCGmtcaELYEKLPQGYRLEKPLN 915
Cdd:cd14050  144 FGLVVELDKEDIHDAQEGDPRYMAPELLQ-GSFTKAADIFSLGITILELACNLELPSGG----DGWHQLRQGYLPEEFTA 218
                        250       260
                 ....*....|....*....|....*...
gi 759191595 916 -CDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14050  219 gLSPELRSIIKLMMDPDPERRPTAEDLL 246
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
675-942 1.97e-21

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: 95.32  E-value: 1.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKD--DHRdFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSKFIV--ALKVLfKSQIEKEgvEHQ-LRREIEIQSHL-RHPNILRLYNYFHDRKRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd14117   82 YLILEYAPRGELYKELQKH----------------GRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGEL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRGQEVYVKKTM-GRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQgYRL 910
Cdd:cd14117  146 KIADFGWSVHAPSLRRRTMcGTLD--YLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTETYRRIVK-VDL 221
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14117  222 KFPPFLSDGSRDLISKLLRYHPSERLPLKGVM 253
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
683-941 2.08e-21

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: 95.02  E-value: 2.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaaikRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVM-----VMKELIRFDEetQRTFLKEVKVMRCL-EHPNVLKFIGVLYKDKRLNFITEYIKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd14221   75 GTLRGIIK---------------SMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLAR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 -----------GQEVYVKKTMGRLPV----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------LGGTPYCGMTC 897
Cdd:cd14221  140 lmvdektqpegLRSLKKPDRKKRYTVvgnpYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGrvnadpdyLPRTMDFGLNV 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 759191595 898 AELYEKLPqgyrlekPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14221  220 RGFLDRYC-------PPNCPPSFFPIAVLCCDLDPEKRPSFSKL 256
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
682-942 2.98e-21

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: 94.27  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd08219    7 VVGEGSFGRALLVQHVNSDQKY--AMKEIRLPKSSSAVEDSRKEAVLLAKM-KHPNIVAFKESFEADGHLYIVMEYCDGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR- 840
Cdd:cd08219   84 DLMQKIKLQR--------------GKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARl 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 ------------GQEVYVKktmgrlPVRWmaiESLNYSvytTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQGY 908
Cdd:cd08219  150 ltspgayactyvGTPYYVP------PEIW---ENMPYN---NKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGS 216
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08219  217 YKPLPSHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
675-941 4.85e-21

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 93.93  E-value: 4.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLkaRIKKDGLRMDAAIKRM-KEYASKDDHRDFAGELeVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVF--LAVNRNTEEAVAVKFVdMKRAPGDCPENIKKEV-CIQKMLSHKNVVRFYGHRREGEFQYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDflrksrvlETDPAFAIANSTASTLSsQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd14069   78 FLEYASGGELFD--------KIEPDVGMPEDVAQFYF-QQLM-------AGLKYLHSCGITHRDIKPENLLLDENDNLKI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLS-----RGQEVYVKKTMGRLPvrWMAIESLNYSVYTTN-SDVWSYGVLL---------WEIVSLGGTPYCG-MTC 897
Cdd:cd14069  142 SDFGLAtvfryKGKERLLNKMCGTLP--YVAPELLAKKKYRAEpVDVWSCGIVLfamlagelpWDQPSDSCQEYSDwKEN 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 759191595 898 AELYE----KLPQGyrlekplncddeVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14069  220 KKTYLtpwkKIDTA------------ALSLLRKILTENPNKRITIEDI 255
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
675-942 4.98e-21

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: 93.96  E-value: 4.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKdgLRMDAAIKRM---KEYASKDDHRDfagELEVLcKLGHHPNIINLLGACEHRGYL 751
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLP--KKEKVAIKRIdleKCQTSMDELRK---EIQAM-SQCNHPNVVSYYTSFVVGDEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLssqqllhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd06610   75 WLVMPLLSGGSLLDIMKSSYPRGGLDEAIIATVLKEVL-------------KGLEYLHSNGQIHRDVKAGNILLGEDGSV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLS------RGQEVYVKKTMGRLPVrWMAIESLN-YSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 904
Cdd:cd06610  142 KIADFGVSaslatgGDRTRKVRKTFVGTPC-WMAPEVMEqVRGYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLMLT 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 905 PQGYRLEKPLNCDDEVY-----DLMRQCWREKPYERPSFAQIL 942
Cdd:cd06610  220 LQNDPPSLETGADYKKYsksfrKMISLCLQKDPSKRPTAEELL 262
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
683-940 5.32e-21

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: 93.51  E-value: 5.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARiKKDGLRMDAAIKRM-KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14121    3 LGSGTYATVYKAY-RKSGAREVVAVKCVsKSSLNKASTENLLTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGLS 839
Cdd:cd14121   81 DLSRFIRSRR----------------TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEK--------LPQGYRLE 911
Cdd:cd14121  145 QHLKPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKirsskpieIPTRPELS 223
                        250       260
                 ....*....|....*....|....*....
gi 759191595 912 KplNCddevYDLMRQCWREKPYERPSFAQ 940
Cdd:cd14121  224 A--DC----RDLLLRLLQRDPDRRISFEE 246
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
678-942 5.70e-21

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: 93.69  E-value: 5.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQ--DVIGEGNFGQVLKArIKKDGLRMDAA--IKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd14098    1 KYQiiDRLGSGTFAEVKKA-VEVETGKMRAIkqIVKRKVAGNDKNLQLFQREINILKSL-EHPGIVRLIDWYEDDQHIYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLETDPAFAIanstastlsSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGEN--YVA 831
Cdd:cd14098   79 VMEYVEGGDLMDFIMAWGAIPEQHAREL---------TKQIL-------EAMAYTHSMGITHRDLKPENILITQDdpVIV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRGQE-----VYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLP 905
Cdd:cd14098  143 KISDFGLAKVIHtgtflVTFCGTMAYLaPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKRIR 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 906 QGYRLEKPL---NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14098  222 KGRYTQPPLvdfNISEEAIDFILRLLDVDPEKRMTAAQAL 261
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
681-886 7.04e-21

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: 93.93  E-value: 7.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDglrmDAAIKRMKEYaskdDHRDFAGELEV--LCKLgHHPNIINLLGAcEHRGY-----LYL 753
Cdd:cd14053    1 EIKARGRFGAVWKAQYLNR----LVAVKIFPLQ----EKQSWLTEREIysLPGM-KHENILQFIGA-EKHGEsleaeYWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYL----------SQKQFIHRDLAARNI 823
Cdd:cd14053   71 ITEFHERGSLCDYL-----------------KGNVISWNELCKIAESMARGLAYLhedipatnggHKPSIAHRDFKSKNV 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 824 LVGENYVAKIADFGLSR----GQEvyVKKTMGRLPV-RWMAIESLNYSV-YTTNS----DVWSYGVLLWEIVS 886
Cdd:cd14053  134 LLKSDLTACIADFGLALkfepGKS--CGDTHGQVGTrRYMAPEVLEGAInFTRDAflriDMYAMGLVLWELLS 204
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
683-945 7.36e-21

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: 93.32  E-value: 7.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHrdfagELEVLCKLgHHPNIINLLGACE---------------- 746
Cdd:cd14047   14 IGSGGFGQVFKAKHRIDGKTY--AIKRVKLNNEKAER-----EVKALAKL-DHPNIVRYNGCWDgfdydpetsssnssrs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 747 HRGYLYLAIEYAPHGNLLDFLRKSRVLETDPafaianstastLSSQQLLHfaaDVARGMDYLSQKQFIHRDLAARNILVG 826
Cdd:cd14047   86 KTKCLFIQMEFCEKGTLESWIEKRNGEKLDK-----------VLALEIFE---QITKGVEYIHSKKLIHRDLKPSNIFLV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 827 ENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpycGMTCAELYEKLPQ 906
Cdd:cd14047  152 DTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDS---AFEKSKFWTDLRN 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 759191595 907 G---------YRLEKPlncddevydLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14047  229 GilpdifdkrYKIEKT---------IIKKMLSKKPEDRPNASEILRTL 267
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
681-942 8.03e-21

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: 94.02  E-value: 8.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRG------YLYLA 754
Cdd:cd06637   12 ELVGNGTYGQVYKGRHVKTG--QLAAIKVMD--VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNppgmddQLWLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd06637   88 MEFCGAGSVTDLIK--------------NTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSrgqeVYVKKTMGRLPV-----RWMAIESLNY-----SVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 904
Cdd:cd06637  154 DFGVS----AQLDRTVGRRNTfigtpYWMAPEVIACdenpdATYDFKSDLWSLGITAIEMAE-GAPPLCDMHPMRALFLI 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 759191595 905 PQ--GYRLeKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06637  229 PRnpAPRL-KSKKWSKKFQSFIESCLVKNHSQRPSTEQLM 267
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
683-942 9.31e-21

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: 92.70  E-value: 9.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRmdAAIKRM-KEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQK--VAIKIVnKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRVLEtdpafaianstastlsSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGlsrg 841
Cdd:cd14081   87 ELFDYLVKKGRLT----------------EKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFG---- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 qevyvkktMGRLPVRWMAIE----SLNYS----VYTTN-----SDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGy 908
Cdd:cd14081  147 --------MASLQPEGSLLEtscgSPHYAcpevIKGEKydgrkADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRG- 216
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14081  217 VFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIK 250
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
676-942 1.04e-20

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: 92.62  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLrmDAAIKRMKEYASKDDH--RDFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGL--EVAIKMIDKKAMQKAGmvQRVRNEVEIHCQL-KHPSILELYNYFEDSNYVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLrksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd14186   79 VLEMCHNGEMSRYL---------------KNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKK--TMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQGyRLE 911
Cdd:cd14186  144 ADFGLATQLKMPHEKhfTMCGTP-NYISPEIATRSAHGLESDVWSLGCMFYTLL-VGRPPFDTDTVKNTLNKVVLA-DYE 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14186  221 MPAFLSREAQDLIHQLLRKNPADRLSLSSVL 251
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
676-942 1.11e-20

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: 92.47  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDG----------LRMDAaikRMKEYAskddhrdfAGELEVLCKLgHHPNIINLLGAC 745
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGrvyalkqidiSRMSR---KMREEA--------IDEARVLSKL-NSPYVIKYYDSF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRGYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 825
Cdd:cd08529   69 VDKGKLNIVMEYAENGDLHSLIKSQR--------------GRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYVAKIADFGLSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEK 903
Cdd:cd08529  135 DKGDNVKIGDLGVAKilSDTTNFAQTIVGTPY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILK 212
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 904 LPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08529  213 IVRGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTELL 251
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
673-951 1.15e-20

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: 93.20  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWN----DIKFQDVIGEGNFGQVLKARikkdgLRMDAAIKRMKEYASKDDH-RDFAGELEVLCKLGHhpniINLLgaceh 747
Cdd:cd14151    2 DWEipdgQITVGQRIGSGSFGTVYKGK-----WHGDVAVKMLNVTAPTPQQlQAFKNEVGVLRKTRH----VNIL----- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 rgyLYLAIEYAPHGNLLdflrkSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 827
Cdd:cd14151   68 ---LFMGYSTKPQLAIV-----TQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVAKIADFGLSRGQEVY-----VKKTMGRlpVRWMAIESL---NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA- 898
Cdd:cd14151  140 DLTVKIGDFGLATVKSRWsgshqFEQLSGS--ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRd 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 899 ELYEKLPQGYrLEKPL-----NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEE 951
Cdd:cd14151  217 QIIFMVGRGY-LSPDLskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
678-941 1.36e-20

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: 92.32  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLrmdAAIKRMKEYASKD--DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd14161    6 EFLETLGKGTYGRVKKARDSSGRL---VAIKSIRKDRIKDeqDLLHIRREIEIMSSL-NHPHIISVYEVFENSSKIVIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd14161   82 EYASRGDLYDYI----------------SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR--GQEVYVKKTMGRlPVrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRle 911
Cdd:cd14161  146 FGLSNlyNQDKFLQTYCGS-PL-YASPEIVNGRPYIgPEVDSWSLGVLLYILVH-GTMPFDGHDYKILVKQISSGaYR-- 220
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 912 KPLNCDDEVyDLMRQCWREKPYERPSFAQI 941
Cdd:cd14161  221 EPTKPSDAC-GLIRWLLMVNPERRATLEDV 249
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
677-935 1.54e-20

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: 92.41  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM--KEYASKDDH----RDFAGELEVLCKLGHHPNIINLLGACEHRGY 750
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKY--AIKCLykSGPNSKDGNdfqkLPQLREIDLHRRVSRHPNIITLHDVFETEVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRVLETDPafaianstastlssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY- 829
Cdd:cd13993   80 IYIVLEYCPNGDLFEAITENRIYVGKT--------------ELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEg 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSRGQEVYVKKTMGRLpvRWMAIESL------NYSVYTTNSDVWSYGVLLWEIVSlGGTPYcgmTCAELYEK 903
Cdd:cd13993  146 TVKLCDFGLATTEKISMDFGVGSE--FYMAPECFdevgrsLKGYPCAAGDIWSLGIILLNLTF-GRNPW---KIASESDP 219
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 904 LPQGYRLEKP------LNCDDEVYDLMRQCWREKPYER 935
Cdd:cd13993  220 IFYDYYLNSPnlfdviLPMSDDFYNLLRQIFTVNPNNR 257
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
706-948 1.99e-20

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: 92.66  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 706 AIKRMkEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDflrksrVLETDpafAIanst 785
Cdd:cd14042   34 AIKKV-NKKRIDLTREVLKELKHMRDL-QHDNLTRFIGACVDPPNICILTEYCPKGSLQD------ILENE---DI---- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 786 asTLSSQQLLHFAADVARGMDYLSQKQFI-HRDLAARNILVGENYVAKIADFGLSR----------GQEVYVKKTmgrlp 854
Cdd:cd14042   99 --KLDWMFRYSLIHDIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSfrsgqeppddSHAYYAKLL----- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 855 vrWMAIESLNYSVY----TTNSDVWSYGVLLWEIVSLGGTPYCGMTCAE----LYEKLPQGYR-----LEKPLNCDDEVY 921
Cdd:cd14042  172 --WTAPELLRDPNPpppgTQKGDVYSFGIILQEIATRQGPFYEEGPDLSpkeiIKKKVRNGEKppfrpSLDELECPDEVL 249
                        250       260
                 ....*....|....*....|....*..
gi 759191595 922 DLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14042  250 SLMQRCWAEDPEERPDFSTLRNKLKKL 276
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
683-942 2.01e-20

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: 91.80  E-value: 2.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRM---DAAIKRMkeyaSKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd08218    8 IGEGSFGKALLVKSKEDGKQYvikEINISKM----SPKEREESRKEVAVLSKM-KHPNIVQYQESFEENGNLYIVMDYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd08218   83 GGDLYKRINAQR--------------GVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRLEKPLNCD 917
Cdd:cd08218  149 RvlNSTVELARTCIGTPY-YLSPEICENKPYNNKSDIWALGCVLYEMCTL-KHAFEAGNMKNLVLKIIRGSYPPVPSRYS 226
                        250       260
                 ....*....|....*....|....*
gi 759191595 918 DEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08218  227 YDLRSLVSQLFKRNPRDRPSINSIL 251
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
682-942 3.70e-20

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 91.63  E-value: 3.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKeYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGY----LYLAIEY 757
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRY--ALKRMY-FNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDSAILSSEgrkeVLLLMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APhGNLLDFLRKSrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARNILVGENYVAKIAD 835
Cdd:cd13985   84 CP-GSLVDILEKS--------------PPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FG--------LSRGQEVYV------KKT--MGRLPvrwmaiESLN-YSVY--TTNSDVWSYGVLLWEIVSLgGTPYcgmt 896
Cdd:cd13985  149 FGsattehypLERAEEVNIieeeiqKNTtpMYRAP------EMIDlYSKKpiGEKADIWALGCLLYKLCFF-KLPF---- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 897 caELYEKL---PQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd13985  218 --DESSKLaivAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
683-943 3.91e-20

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: 91.17  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDG--LRMDAAIKRMKEYASKDdhRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14116   13 LGKGKFGNVYLAREKQSKfiLALKVLFKAQLEKAGVE--HQLRREVEIQSHL-RHPNILRLYGYFHDATRVYLILEYAPL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd14116   90 GTVYRELQK----------------LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQEVYVKKTM-GRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQgYRLEKPLNCDDE 919
Cdd:cd14116  154 HAPSSRRTTLcGTLD--YLPPEMIEGRMHDEKVDLWSLGVLCYEFL-VGKPPFEANTYQETYKRISR-VEFTFPDFVTEG 229
                        250       260
                 ....*....|....*....|....
gi 759191595 920 VYDLMRQCWREKPYERPSFAQILV 943
Cdd:cd14116  230 ARDLISRLLKHNPSQRPMLREVLE 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
679-941 4.58e-20

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: 90.91  E-value: 4.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKD--DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd14073    5 LLETLGKGTYGKVKLAIERATG--REVAIKSIKKDKIEDeqDMVRIRREIEIMSSL-NHPHIIRIYEVFENKDKIVIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVLetdpafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd14073   82 YASGGELYDYISERRRL----------------PEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSrgqEVYVK----KTMGRLPVrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQG--YR 909
Cdd:cd14073  146 GLS---NLYSKdkllQTFCGSPL-YASPEIVNGTPYQgPEVDCWSLGVLLYTLV-YGTMPFDGSDFKRLVKQISSGdyRE 220
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 910 LEKPlncdDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14073  221 PTQP----SDASGLIRWMLTVNPKRRATIEDI 248
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
675-963 5.15e-20

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: 91.45  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaaikRMKEYASKDDHRDFAG---ELEVLCKlGHHPNIINLLGACEHRGYL 751
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTM-----AMKEIRLELDESKFNQiimELDILHK-AVSPYIVDFYGAFFIEGAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLldflrksrvletDPAFAiANSTASTLSSQQLLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENYV 830
Cdd:cd06622   75 YMCMEYMDAGSL------------DKLYA-GGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRGQEVYVKKT-MGrlPVRWMA---IESLNYS---VYTTNSDVWSYGVLLWEIvSLGGTPYCGMTCAELYEK 903
Cdd:cd06622  142 VKLCDFGVSGNLVASLAKTnIG--CQSYMAperIKSGGPNqnpTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIFAQ 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 904 LP---QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI-----LVSLNRMLEERKTYVNTTLYEK 963
Cdd:cd06622  219 LSaivDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLlehpwLVKYKNADVDMAEWVTGALKRK 286
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
676-943 7.89e-20

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: 90.41  E-value: 7.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLrmDAAIKRMK--EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGR--LVALKKVQifEMMDAKARQDCLKEIDLLQQL-NHPNIIKYLASFIENNELNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd08224   78 VLELADAGDLSRLIKHFK------------KQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCG--MTCAELYEKLPQG-Y 908
Cdd:cd08224  146 GDLGLGRffSSKTTAAHSLVGTPY-YMSPERIREQGYDFKSDIWSLGCLLYEMAAL-QSPFYGekMNLYSLCKKIEKCeY 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 909 rleKPLNCD---DEVYDLMRQCWREKPYERPSFAQILV 943
Cdd:cd08224  224 ---PPLPADlysQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
683-964 8.99e-20

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: 90.52  E-value: 8.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKA---RIKKDglrmdAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd06641   12 IGKGSFGEVFKGidnRTQKV-----VAIKIIDLEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKDTKLWIIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETdpafaianstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd06641   86 GGSALDLLEPGPLDET-----------------QIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 rGQ--EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyrlEKPL--- 914
Cdd:cd06641  149 -GQltDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAR-GEPPHSELHPMKVLFLIPKN---NPPTleg 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKF 964
Cdd:cd06641  224 NYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRY 273
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
735-948 9.16e-20

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: 90.30  E-value: 9.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFI 814
Cdd:cd14045   61 HPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDI---------------PLNWGFRFSFATDIARGMAYLHQHKIY 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 815 HRDLAARNILVGENYVAKIADFGL--------SRGQEVYVKKTMGrlpvRWMAIE--SLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd14045  126 HGRLKSSNCVIDDRWVCKIADYGLttyrkedgSENASGYQQRLMQ----VYLPPEnhSNTDTEPTQATDVYSYAIILLEI 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 885 VSLG------GTPYCGMTCAELYEkLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14045  202 ATRNdpvpedDYSLDEAWCPPLPE-LISG-KTENSCPCPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
683-942 9.55e-20

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 90.56  E-value: 9.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGAC--EHRGYLYLAIEYAPH 760
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIF--ALKTITTDPNPDVQKQILRELEIN-KSCASPYIVKYYGAFldEQDSSIGIAMEYCEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSr 840
Cdd:cd06621   86 GSLDSIYKKVK------------KKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQEV-YVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSL------GGTPYCG----------MTCAELYEK 903
Cdd:cd06621  153 GELVnSLAGTFTGTSY-YMAPERIQGGPYSITSDVWSLGLTLLEVAQNrfpfppEGEPPLGpiellsyivnMPNPELKDE 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 904 LPQGYRLEKPLNcddevyDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06621  232 PENGIKWSESFK------DFIEKCLEKDGTRRPGPWQML 264
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
678-942 1.24e-19

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: 89.50  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd14072    3 RLLKTIGKGNFAKVKLARHVLTG--REVAIKIIdKTQLNPSSLQKLFREVRIM-KILNHPNIVKLFEVIETEKTLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSsqqllhfaadvargmdYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd14072   80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQ----------------YCHQKRIVHRDLKAENLLLDADMNIKIADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSR----GQEvyVKKTMGRLPvrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRL 910
Cdd:cd14072  144 GFSNeftpGNK--LDTFCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRI 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 911 EKPLNCDDEvyDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14072  219 PFYMSTDCE--NLLKKFLVLNPSKRGTLEQIM 248
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
682-942 1.33e-19

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: 90.17  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd07846    8 LVGEGSYGMVMKCRHKETG--QIVAIKKFLESEDDKMVKKIAmREIKMLKQL-RHENLVNLIEVFRRKKRWYLVFEFVDH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDflrksrvLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd07846   85 TVLDD-------LEKYP---------NGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 ----GQEVYVKKtmgrLPVRWM-AIESLNYSV-YTTNSDVWSYGVLLWEIVSlgGTP-----------YCGMTC------ 897
Cdd:cd07846  149 tlaaPGEVYTDY----VATRWYrAPELLVGDTkYGKAVDVWAVGCLVTEMLT--GEPlfpgdsdidqlYHIIKClgnlip 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 898 --AELYEKLP--QGYRLE-----KPLN-----CDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07846  223 rhQELFQKNPlfAGVRLPevkevEPLErrypkLSGVVIDLAKKCLHIDPDKRPSCSELL 281
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
683-887 1.84e-19

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


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 89.64  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDdhrdfaG-------ELEVLCKLGH--HPNIINLLGAC-----EHR 748
Cdd:cd07838    7 IGEGAYGTVYKARDLQDG--RFVALKKVRVPLSEE------GiplstirEIALLKQLESfeHPNVVRLLDVChgprtDRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 GYLYLAIEYApHGNLLDFLRKSrvletdPAFAIANSTASTLSsQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd07838   79 LKLTLVFEHV-DQDLATYLDKC------PKPGLPPETIKDLM-RQLL-------RGLDFLHSHRIVHRDLKPQNILVTSD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 829 YVAKIADFGLSRgqeVYvKKTMGRLPV---RWM-AIESLNYSVYTTNSDVWSYGVLLWEIVSL 887
Cdd:cd07838  144 GQVKLADFGLAR---IY-SFEMALTSVvvtLWYrAPEVLLQSSYATPVDMWSVGCIFAELFNR 202
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
676-949 1.91e-19

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: 89.59  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFqdvIGEGNFGQVLKARikKDGLRMDAAIKRMKEYA--SKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYL 753
Cdd:cd14026    1 DLRY---LSRGAFGTVSRAR--HADWRVTVAIKCLKLDSpvGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKsRVLETDPAFAIanstastlsSQQLLHfaaDVARGMDYLSQKQ--FIHRDLAARNILVGENYVA 831
Cdd:cd14026   75 VTEYMTNGSLNELLHE-KDIYPDVAWPL---------RLRILY---EIALGVNYLHNMSppLLHHDLKTQNILLDGEFHV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRGQEVYVKKTMGRLP------VRWMAIESLNYSVYTTNS---DVWSYGVLLWEIVSLgGTPYCGMTCA-ELY 901
Cdd:cd14026  142 KIADFGLSKWRQLSISQSRSSKSapeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSR-KIPFEEVTNPlQIM 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 902 EKLPQGYRL---EKPLNCD----DEVYDLMRQCWREKPYERPSFAQILVSLNRML 949
Cdd:cd14026  221 YSVSQGHRPdtgEDSLPVDiphrATLINLIESGWAQNPDERPSFLKCLIELEPVL 275
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
676-926 2.15e-19

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: 89.80  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEV-SHPFIIRLFWTEHDQRFLYMLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05612   81 EYVPGGELFSYLRNSG----------------RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRgqEVYVKK-TMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPL 914
Cdd:cd05612  145 FGFAK--KLRDRTwTLCGTP-EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFDDNPFGIYEKILAG-KLEFPR 219
                        250
                 ....*....|..
gi 759191595 915 NCDDEVYDLMRQ 926
Cdd:cd05612  220 HLDLYAKDLIKK 231
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
728-941 2.17e-19

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: 89.00  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 728 VLCKLG--HHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVlETDPAFaianstastlSSQQLLhfaaDVARGM 805
Cdd:cd14043   46 VFSKLRelRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDM-KLDWMF----------KSSLLL----DLIKGM 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 806 DYLSQKQFIHRDLAARNILVGENYVAKIADFGLSrgqEVYVKKTMGRLPVR-----WMAIESLNYSVY----TTNSDVWS 876
Cdd:cd14043  111 RYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYN---EILEAQNLPLPEPApeellWTAPELLRDPRLerrgTFPGDVFS 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 877 YGVLLWEIVSLGGtPYC--GMTCAELYEKLPQGYRLEKPLNCDD----EVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14043  188 FAIIMQEVIVRGA-PYCmlGLSPEEIIEKVRSPPPLCRPSVSMDqaplECIQLMKQCWSEAPERRPTFDQI 257
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
683-938 2.22e-19

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: 88.96  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlRMDAAIKRM-KEYASKDdhRDFAG-ELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKP-DLPVAIKCItKKNLSKS--QNLLGkEIKILKEL-SHENVVALLDCQETSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY---------VA 831
Cdd:cd14120   77 GDLADYLQAKG----------------TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRG-QEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAEL---YEKlPQG 907
Cdd:cd14120  141 KIADFGFARFlQDGMMAATLCGSPM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELkafYEK-NAN 217
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 908 YRLEKPLNCDDEVYDLMRQCWREKPYERPSF 938
Cdd:cd14120  218 LRPNIPSGTSPALKDLLLGLLKRNPKDRIDF 248
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
675-941 2.66e-19

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: 89.16  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDglRMDAAIKRMKeYASKDDHRD-FAGELEVLCKLgHHPNIINLLGACEHR----- 748
Cdd:cd14048    6 TDFEPIQCLGRGGFGVVFEAKNKVD--DCNYAVKRIR-LPNNELAREkVLREVRALAKL-DHPGIVRYFNAWLERppegw 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 ------GYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAianstastlssqqLLHFAADVARGMDYLSQKQFIHRDLAARN 822
Cdd:cd14048   82 qekmdeVYLYIQMQLCRKENLKDWMNRRCTMESRELFV-------------CLNIFKQIASAVEYLHSKGLIHRDLKPSN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGENYVAKIADFGL--SRGQ-----------EVYVKKTmGRLPVR-WMAIESLNYSVYTTNSDVWSYGVLLWEIVslg 888
Cdd:cd14048  149 VFFSLDDVVKVGDFGLvtAMDQgepeqtvltpmPAYAKHT-GQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELI--- 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 889 gtpYCGMTCAELYEKLPQGYRLEKPLNCDDEV---YDLMRQCWREKPYERPSFAQI 941
Cdd:cd14048  225 ---YSFSTQMERIRTLTDVRKLKFPALFTNKYpeeRDMVQQMLSPSPSERPEAHEV 277
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
681-886 3.29e-19

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: 89.03  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDglrmDAAIKRMkeyaSKDDHRDFAGELEVLCKLG-HHPNIINLLGAcEHRGY-----LYLA 754
Cdd:cd13998    1 EVIGKGRFGEVWKASLKNE----PVAVKIF----SSRDKQSWFREKEIYRTPMlKHENILQFIAA-DERDTalrteLWLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSrvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFI---------HRDLAARNILV 825
Cdd:cd13998   72 TAFHPNGSL*DYLSLH-----------------TIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILV 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 826 GENYVAKIADFGLS----RGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNS------DVWSYGVLLWEIVS 886
Cdd:cd13998  135 KNDGTCCIADFGLAvrlsPSTGEEDNANNGQVgTKRYMAPEVLEGAINLRDFesfkrvDIYAMGLVLWEMAS 206
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
683-942 3.69e-19

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: 88.09  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAI---KRMKEYASKDdhrdfagELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFipkRDKKKEAVLR-------EISILNQL-QHPRIIQLHEAYESPTELVLILELCS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVL-ETDPAFAIanstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV---GENYVaKIAD 835
Cdd:cd14006   73 GGELLDRLAERGSLsEEEVRTYM----------RQLL-------EGLQYLHNHHILHLDLKPENILLadrPSPQI-KIID 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR--GQEVYVKKTMGRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWeiVSLGGT-PYCGMTCAELYEKLPQG-YRLE 911
Cdd:cd14006  135 FGLARklNPGEELKEIFGTP--EFVAPEIVNGEPVSLATDMWSIGVLTY--VLLSGLsPFLGEDDQETLANISACrVDFS 210
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 912 KPLNCD--DEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14006  211 EEYFSSvsQEAKDFIRKLLVKEPRKRPTAQEAL 243
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
682-942 4.24e-19

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: 88.18  E-value: 4.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlrMDAAIKRM----KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTG--RELAVKQVeidpINTEASKEVKALECEIQLLKNL-QHERIVQYYGCLQDEKSLSIFMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLetdpafaiaNSTASTLSSQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd06625   84 MPGGSVKDEIKAYGAL---------TENVTRKYTRQILE-------GLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LS-RGQEVYVKKTMGrlPVR----WMAIESLNYSVYTTNSDVWSYGVLLWEIvsLGGTP----YCGMtcAELYEKLPQGY 908
Cdd:cd06625  148 ASkRLQTICSSTGMK--SVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEM--LTTKPpwaeFEPM--AAIFKIATQPT 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 909 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06625  222 NPQLPPHVSEDARDFLSLIFVRNKKQRPSAEELL 255
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
676-942 4.50e-19

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: 88.27  E-value: 4.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRmdAAIKrMKEYASKDDHRDFAGELE--------------VLCKLGHHPNIINL 741
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEK--CAIK-IIPRASNAGLKKEREKRLekeisrdirtireaALSSLLNHPHICRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 742 LGACEHRGYLYLAIEYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAAR 821
Cdd:cd14077   79 RDFLRTPNHYYMLFEYVDGGQLLDYIISH----------------GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 822 NILVGENYVAKIADFGLSrgqEVYVKKTM-----GRLpvRWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGM 895
Cdd:cd14077  143 NILISKSGNIKIIDFGLS---NLYDPRRLlrtfcGSL--YFAAPELLQAQPYTgPEVDVWSFGVVLYVLVC-GKVPFDDE 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 896 TCAELYEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14077  217 NMPALHAKIKKG-KVEYPSYLSSECKSLISRMLVVDPKKRATLEQVL 262
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
678-944 4.88e-19

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: 87.78  E-value: 4.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVL---------KARIK-KDGLRMDAAIKRM--KEYASkddhrdfageLEVLcklgHHPNIINLLGAC 745
Cdd:cd14075    5 RIRGELGSGNFSQVKlgihqltkeKVAIKiLDKTKLDQKTQRLlsREISS----------MEKL----HHPNIIRLYEVV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRGYLYLAIEYAPHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 825
Cdd:cd14075   71 ETLSKLHLVMEYASGGELYTKI----------------STEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFY 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYVAKIADFGLSrgqeVYVKKTmgrlpvrwmaiESLN-------Y---------SVYTTNSDVWSYGVLLWEIVSlGG 889
Cdd:cd14075  135 ASNNCVKVGDFGFS----THAKRG-----------ETLNtfcgsppYaapelfkdeHYIGIYVDIWALGVLLYFMVT-GV 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 890 TPYCGMTCAELYEKLPQG-YRLekPLNCDDEVYDLMRQCWREKPYERPSFAQILVS 944
Cdd:cd14075  199 MPFRAETVAKLKKCILEGtYTI--PSYVSEPCQELIRGILQPVPSDRYSIDEIKNS 252
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
665-945 5.25e-19

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: 88.55  E-value: 5.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 665 DPTIYPVLDWNDIKFQDVIGEGNFGQVLKARikkdgLRMDAAIKRMKEY-ASKDDHRDFAGELEVLCKLgHHPNIINLLG 743
Cdd:cd14149    2 DSSYYWEIEASEVMLSTRIGSGSFGTVYKGK-----WHGDVAVKILKVVdPTPEQFQAFRNEVAVLRKT-RHVNILLFMG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 744 ACEhRGYLYLAIEYAPHGNLLDFLRksrVLETDpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNI 823
Cdd:cd14149   76 YMT-KDNLAIVTQWCEGSSLYKHLH---VQETK------------FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVAKIADFGLSRGQEVYVKKTMGRLP---VRWMAIESL---NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC 897
Cdd:cd14149  140 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPtgsILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMT-GELPYSHINN 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 898 A-ELYEKLPQGY------RLEKplNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14149  219 RdQIIFMVGRGYaspdlsKLYK--NCPKAMKRLVADCIKKVKEERPLFPQILSSI 271
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
681-899 6.99e-19

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: 87.71  E-value: 6.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDfagELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKN---EINIMNQL-NHVNLIQLYDAFESKTNLTLIMEYVDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLrksrvleTDPAFaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGL 838
Cdd:cd14192   86 GELFDRI-------TDESY--------QLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 839 SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 899
Cdd:cd14192  151 ARRYKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAE 210
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
680-942 8.19e-19

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: 87.92  E-value: 8.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyasKDDHRDfaG-------ELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd07829    4 LEKLGEGTYGVVYKAKDKKTG--EIVALKKIR----LDNEEE--GipstalrEISLLKEL-KHPNIVKLLDVIHTENKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHgNLLDFLRKSRVletdpafaiaNSTASTLSS--QQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd07829   75 LVFEYCDQ-DLKKYLDKRPG----------PLPPNLIKSimYQLL-------RGLAYCHSHRILHRDLKPQNLLINRDGV 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRGQEVyvkktmgrlPVRWMAIES-----------LNYSVYTTNSDVWSYG----------VL--------- 880
Cdd:cd07829  137 LKLADFGLARAFGI---------PLRTYTHEVvtlwyrapeilLGSKHYSTAVDIWSVGcifaelitgkPLfpgdseidq 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 881 LWEIVSLGGTP----YCGMT-CAELYEKLPQgyRLEKPL-----NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07829  208 LFKIFQILGTPteesWPGVTkLPDYKPTFPK--WPKNDLekvlpRLDPEGIDLLSKMLQYNPAKRISAKEAL 277
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
683-951 1.39e-18

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: 86.78  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14664    1 IGRGGAGTVYKGVMPNG---TLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHR-NIVRLRGYCSNPTTNLLVYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQK---QFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14664   77 LGELLHSR------------PESQPPLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R-----GQEVY--VKKTMGrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYC------GMTCAELYEKLPQ 906
Cdd:cd14664  145 KlmddkDSHVMssVAGSYG-----YIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDeaflddGVDIVDWVRGLLE 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 907 GYRLEKPLNCD-------DEVYDLMR---QCWREKPYERPSFAQILvslnRMLEE 951
Cdd:cd14664  219 EKKVEALVDPDlqgvyklEEVEQVFQvalLCTQSSPMERPTMREVV----RMLEG 269
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
682-942 1.61e-18

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: 86.68  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDglRMDAAIKRMKEYASK-------DDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:cd14084   13 TLGSGACGEVKLAYDKST--CKKVAIKIINKRKFTigsrreiNKPRNIETEIEILKKL-SHPCIIKIEDFFDAEDDYYIV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETDPAFAIAnstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVG---ENYVA 831
Cdd:cd14084   90 LELMEGGELFDRVVSNKRLKEAICKLYF---------YQMLL-------AVKYLHSNGIIHRDLKPENVLLSsqeEECLI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSR-GQEVYVKKTMGRLPVrWMAIESLNY---SVYTTNSDVWSYGVLLWeiVSLGGTP-----YCGMTCAEL-- 900
Cdd:cd14084  154 KITDFGLSKiLGETSLMKTLCGTPT-YLAPEVLRSfgtEGYTRAVDCWSLGVILF--ICLSGYPpfseeYTQMSLKEQil 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 901 ---YEKLPQGYRlekplNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14084  231 sgkYTFIPKAWK-----NVSEEAKDLVKKMLVVDPSRRPSIEEAL 270
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
680-929 1.63e-18

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: 86.51  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDfagELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14193    9 EEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKN---EIEVMNQL-NHANLIQLYDAFESRNDIVLVMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFG 837
Cdd:cd14193   85 GGELFD-----RIIDEN----------YNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE-LYEKLPQGYRLEKP--L 914
Cdd:cd14193  150 LARRYKPREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNEtLNNILACQWDFEDEefA 228
                        250       260
                 ....*....|....*....|.
gi 759191595 915 NCDDEVYDLM------RQCWR 929
Cdd:cd14193  229 DISEEAKDFIskllikEKSWR 249
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
680-903 1.66e-18

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: 86.60  E-value: 1.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARiKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14202    7 KDLIGHGAFAVVFKGR-HKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHE-NIVALYDFQEIANSVYLVMEYCN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVG---------ENYV 830
Cdd:cd14202   85 GGDLADYLHTMR----------------TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 831 AKIADFGLSRG-QEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAEL---YEK 903
Cdd:cd14202  149 IKIADFGFARYlQNNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLrlfYEK 223
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
683-936 1.67e-18

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: 86.39  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARikKDGLRMDAAIKRMkeYASKDDH-RDFAGELEVLCKLGHHPNIINLLGAcehrgylylAIEYAPHG 761
Cdd:cd13975    8 LGRGQYGVVYACD--SWGGHFPCALKSV--VPPDDKHwNDLALEFHYTRSLPKHERIVSLHGS---------VIDYSYGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 N-----LLDFLRKSRVLETdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd13975   75 GssiavLLIMERLHRDLYT--------GIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRgQEVYVKKTMGRLPVRwMAIESLNySVYTTNSDVWSYGVLLWEIVSlgGT---PYCGMTCA---ELYEKLPQGYRL 910
Cdd:cd13975  147 GFCK-PEAMMSGSIVGTPIH-MAPELFS-GKYDNSVDVYAFGILFWYLCA--GHvklPEAFEQCAskdHLWNNVRKGVRP 221
                        250       260
                 ....*....|....*....|....*.
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYERP 936
Cdd:cd13975  222 ERLPVFDEECWNLMEACWSGDPSQRP 247
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
678-913 1.94e-18

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: 86.27  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14083    6 EFKEVLGTGAFSEVVLAEDKATGKLV--AIKCIDKKALKGKEDSLENEIAVLRKI-KHPNIVQLLDIYESKSHLYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLD-FLRKSRVLETDpafaianstASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV---GENYVAKI 833
Cdd:cd14083   83 VTGGELFDrIVEKGSYTEKD---------ASHLIRQ--------VLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG-YRLEK 912
Cdd:cd14083  146 SDFGLSKMEDSGVMSTACGTP-GYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPFYDENDSKLFAQILKAeYEFDS 223

                 .
gi 759191595 913 P 913
Cdd:cd14083  224 P 224
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
679-942 2.10e-18

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: 86.58  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDhRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd14166    7 FMEVLGSGAFSEVYLVKQRSTGKLY--ALKCIKKSPLSRD-SSLENEIAVLKRI-KHENIVTLEDIYESTTHYYLVMQLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDflrksRVLETdpafAIANSTASTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV---GENYVAKIAD 835
Cdd:cd14166   83 SGGELFD-----RILER----GVYTEKDASRVINQVL-------SAVKYLHENGIVHRDLKPENLLYltpDENSKIMITD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRGQEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG-YRLEKPL 914
Cdd:cd14166  147 FGLSKMEQNGIMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETESRLFEKIKEGyYEFESPF 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 915 --NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14166  225 wdDISESAKDFIRHLLEKNPSKRYTCEKAL 254
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
682-887 3.38e-18

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: 85.55  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDglRMDAAIKRMK-EYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd08220    7 VVGRGAYGTVYLCRRKDD--NKLVIIKQIPvEQMTKEERQAALNEVKVL-SMLHHPNIIEYYESFLEDKALMIVMEYAPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY-VAKIADFGLS 839
Cdd:cd08220   84 GTLFEYIQQRK--------------GSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRtVVKIGDFGIS 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 840 RgqeVYVKKTMGRLPVR---WMAIESLNYSVYTTNSDVWSYGVLLWEIVSL 887
Cdd:cd08220  150 K---ILSSKSKAYTVVGtpcYISPELCEGKPYNQKSDIWALGCVLYELASL 197
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
682-935 5.77e-18

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: 86.11  E-value: 5.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKK-DGLrmdAAIKRM-KEYASKDDHRD-FAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05570    2 VLGKGSFGKVMLAERKKtDEL---YAIKVLkKEVIIEDDDVEcTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPA-FaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILV-GENYVaKIADF 836
Cdd:cd05570   79 NGGDLMFHIQRARRFTEERArF-----------------YAAEICLALQFLHERGIIYRDLKLDNVLLdAEGHI-KIADF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQEVYVKK--TMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLpQGYRLEKPL 914
Cdd:cd05570  141 GMCKEGIWGGNTtsTFCGTP-DYIAPEILREQDYGFSVDWWALGVLLYEML-AGQSPFEGDDEDELFEAI-LNDEVLYPR 217
                        250       260
                 ....*....|....*....|.
gi 759191595 915 NCDDEVYDLMRQCWREKPYER 935
Cdd:cd05570  218 WLSREAVSILKGLLTKDPARR 238
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
682-941 5.87e-18

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: 84.75  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKA--RIKKdglrMDAAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd14071    7 TIGKGNFAVVKLArhRITK----TEVAIKIIdKSQLDEENLKKIYREVQIM-KMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPA---FaianstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd14071   82 SNGEIFDYLAQHGRMSEKEArkkF------------WQIL-------SAVEYCHKRHIVHRDLKAENLLLDANMNIKIAD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLS----RGQevYVKKTMGRLPvrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRL 910
Cdd:cd14071  143 FGFSnffkPGE--LLKTWCGSPP--YAAPEVFEGKEYEgPQLDIWSLGVVLYVLVC-GALPFDGSTLQTLRDRVLSG-RF 216
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14071  217 RIPFFMSTDCEHLIRRMLVLDPSKRLTIEQI 247
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
681-942 7.64e-18

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: 84.74  E-value: 7.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRD---------FAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEML--AVKQVELPKTSSDRADsrqktvvdaLKSEIDTLKDL-DHPNIVQYLGFEETEDYF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSRVLETDpafaianstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd06629   84 SIFLEYVPGGSIGSCLRKYGKFEED----------------LVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGIC 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSR-GQEVY--VKKTMGRLPVRWMAIE--SLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC-AELYE--K 903
Cdd:cd06629  148 KISDFGISKkSDDIYgnNGATSMQGSVFWMAPEviHSQGQGYSAKVDIWSLGCVVLEMLA-GRRPWSDDEAiAAMFKlgN 226
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 904 LPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06629  227 KRSAPPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELL 265
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
683-942 7.81e-18

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: 84.66  E-value: 7.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaaikRMKEYASKDD----HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELM-----AMKEIRFQDNdpktIKEIADEMKVLEGL-DHPNLVRYYGVEVHREEVYIFMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLetdPAFAIANSTAstlssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd06626   82 QEGTLEELLRHGRIL---DEAVIRVYTL------QLL-------EGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SrgqeVYVKK---TMGRLPVR-------WMAIESLNYSVYTTN---SDVWSYGVLLWEIVSlGGTPYcgmtcAELYEKLP 905
Cdd:cd06626  146 A----VKLKNnttTMAPGEVNslvgtpaYMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPW-----SELDNEWA 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 906 QGYRL---EKP-----LNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06626  216 IMYHVgmgHKPpipdsLQLSPEGKDFLSRCLESDPKKRPTASELL 260
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
665-943 7.88e-18

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: 85.12  E-value: 7.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 665 DPTIYPVlDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGA 744
Cdd:cd06618    6 DGKKYKA-DLNDLENLGEIGSGTCGQVYKMRHKKTGHVM--AVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 745 CEHRGYLYLAIEYAphGNLLDFLRKsRVLETDPAFAIANSTASTLSSqqllhfaadvargMDYLSQKQ-FIHRDLAARNI 823
Cdd:cd06618   83 FITDSDVFICMELM--STCLDKLLK-RIQGPIPEDILGKMTVSIVKA-------------LHYLKEKHgVIHRDVKPSNI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVAKIADFGLSrGQEVYVK-KTMGRLPVRWMAIESL---NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGmtCAE 899
Cdd:cd06618  147 LLDESGNVKLCDFGIS-GRLVDSKaKTRSAGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELAT-GQFPYRN--CKT 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 900 LYEKLPQGYRLEKPLNCDDEVY-----DLMRQCWREKPYERPSFAQILV 943
Cdd:cd06618  223 EFEVLTKILNEEPPSLPPNEGFspdfcSFVDLCLTKDHRYRPKYRELLQ 271
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
678-884 8.62e-18

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: 84.78  E-value: 8.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDV--IGEGNFGQVLKAR-IKKDGLRMdaAIKRMKEYAS--KDDHRDFAgELEVLCKLGH--HPNIINLLGACEHRGY 750
Cdd:cd14052    1 RFANVelIGSGEFSQVYKVSeRVPTGKVY--AVKKLKPNYAgaKDRLRRLE-EVSILRELTLdgHDNIVQLIDSWEYHGH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKsrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd14052   78 LYIQTELCENGSLDVFLSE-------------LGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFG------LSRGQEVYVKKTmgrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd14052  145 LKIGDFGmatvwpLIRGIEREGDRE-------YIAPEILSEHMYDKPADIFSLGLILLEA 197
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
681-942 9.02e-18

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: 84.21  E-value: 9.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLrmDAAIKRM-----KEYASKDDHRDFAGE--LEVLCKLGHHPNIINLLGACEHR-GYLy 752
Cdd:cd14005    6 DLLGKGGFGTVYSGVRIRDGL--PVAVKFVpksrvTEWAMINGPVPVPLEiaLLLKASKPGVPGVIRLLDWYERPdGFL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEY-APHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILV----GE 827
Cdd:cd14005   83 LIMERpEPCQDLFDFITERGALSENLA----------------RIIFRQVVEAVRHCHQRGVLHRDIKDENLLInlrtGE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 nyvAKIADFGLS-----------RGQEVYvkktmgrLPVRWmaiesLNYSVYTTNS-DVWSYGVLLWEIVslggtpyCGm 895
Cdd:cd14005  147 ---VKLIDFGCGallkdsvytdfDGTRVY-------SPPEW-----IRHGRYHGRPaTVWSLGILLYDML-------CG- 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 896 tcaelyeKLPQGYRLEkplNCDDEVY----------DLMRQCWREKPYERPSFAQIL 942
Cdd:cd14005  204 -------DIPFENDEQ---ILRGNVLfrprlskeccDLISRCLQFDPSKRPSLEQIL 250
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
675-956 9.94e-18

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: 84.72  E-value: 9.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd06616    6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIM--AVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWIC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEyaphgnLLDflrksrvLETDPAFAIA-NSTASTLSSQQLLHFAADVARGMDYLSQK-QFIHRDLAARNILVGENYVAK 832
Cdd:cd06616   84 ME------LMD-------ISLDKFYKYVyEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSrGQEV-YVKKTM--GRLPvrWMAIESLNYSV----YTTNSDVWSYGVLLWEiVSLGGTPYCGMTcaELYEKLP 905
Cdd:cd06616  151 LCDFGIS-GQLVdSIAKTRdaGCRP--YMAPERIDPSAsrdgYDVRSDVWSLGITLYE-VATGKFPYPKWN--SVFDQLT 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 906 QGYRLEKP--LNCDDEVY-----DLMRQCWREKPYERPSFAQIL-VSLNRMLEERKTYV 956
Cdd:cd06616  225 QVVKGDPPilSNSEEREFspsfvNFVNLCLIKDESKRPKYKELLkHPFIKMYEERNVDV 283
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
683-941 1.89e-17

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 85.47  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARiKKDGLRMdAAIKRMKEYASK--DDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05600   19 VGQGGYGSVFLAR-KKDTGEI-CALKIMKKKVLFklNEVNHVLTERDILTT-TNSPWLVKLLYAFQDPENVYLAMEYVPG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPA-FAIANStastlssqqllhFAAdvargMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05600   96 GDFRTLLNNSGILSEEHArFYIAEM------------FAA-----ISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 RG--------------QEVYV---------------KKTMGRLPVR---------WMAIESLNYSVYTTNSDVWSYGVLL 881
Cdd:cd05600  159 SGtlspkkiesmkirlEEVKNtafleltakerrniyRAMRKEDQNYansvvgspdYMAPEVLRGEGYDLTVDYWSLGCIL 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 882 WEIVSlGGTPYCGMTCAELYEKLpqgYR----LEKPL--------NCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05600  239 FECLV-GFPPFSGSTPNETWANL---YHwkktLQRPVytdpdlefNLSDEAWDLITKLITDPQDRLQSPEQI 306
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
682-951 2.29e-17

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: 83.95  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIkkDGLRMdaAIKRMkeyaSKDDHRDFAGELEVL-CKLGHHPNIINLLGACEH------RGYLyLA 754
Cdd:cd14054    2 LIGQGRYGTVWKGSL--DERPV--AVKVF----PARHRQNFQNEKDIYeLPLMEHSNILRFIGADERptadgrMEYL-LV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQ---------FIHRDLAARNILV 825
Cdd:cd14054   73 LEYAPKGSLCSYLR-----------------ENTLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYVAKIADFGLS---RGQEVYVKKT--------MGRLPVRWMAIESLNYSVYTTNS-------DVWSYGVLLWEIvsl 887
Cdd:cd14054  136 KADGSCVICDFGLAmvlRGSSLVRGRPgaaenasiSEVGTLRYMAPEVLEGAVNLRDCesalkqvDVYALGLVLWEI--- 212
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 888 ggtpycGMTCAELYE-------KLPqgYRLEKPLNCDDEVYDLMRQcwREKpyERPSFAQILVSLN---RMLEE 951
Cdd:cd14054  213 ------AMRCSDLYPgesvppyQMP--YEAELGNHPTFEDMQLLVS--REK--ARPKFPDAWKENSlavRSLKE 274
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
683-942 2.34e-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: 82.86  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglRMDAAIKRMKEYA----SKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd08222    8 LGSGNFGTVYLVSDLKA--TADEELKVLKEISvgelQPDETVDANREAKLLSKL-DHPAIVKFHDSFVEKESFCIVTEYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENyVAKIADFGL 838
Cdd:cd08222   85 EGGDLDDKISEYK------------KSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN-VIKVGDFGI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPLNC 916
Cdd:cd08222  152 SRilMGTSDLATTFTGTPY-YMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHA-FDGQNLLSVMYKIVEGETPSLPDKY 229
                        250       260
                 ....*....|....*....|....*.
gi 759191595 917 DDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08222  230 SKELNAIYSRMLNKDPALRPSAAEIL 255
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
679-942 2.99e-17

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: 82.77  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDglRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd14167    7 FREVLGTGAFSEVVLAEEKRT--QKLVAIKCIAKKALEGKETSIENEIAVLHKI-KHPNIVALDDIYESGGHLYLIMQLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLD-FLRKSRVLETDpafaianstASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNIL---VGENYVAKIA 834
Cdd:cd14167   84 SGGELFDrIVEKGFYTERD---------ASKLIFQ--------ILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMIS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRGQEV-YVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG-YRLEK 912
Cdd:cd14167  147 DFGLSKIEGSgSVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQILKAeYEFDS 224
                        250       260       270
                 ....*....|....*....|....*....|..
gi 759191595 913 PL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14167  225 PYwdDISDSAKDFIQHLMEKDPEKRFTCEQAL 256
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
683-942 3.02e-17

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: 83.15  E-value: 3.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMkeyASKDDHRDFAG----ELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd07832    8 IGEGAHGIVFKAKDRETG--ETVALKKV---ALRKLEGGIPNqalrEIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGnLLDFLRKSRvletDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd07832   83 LSS-LSEVLRDEE----RP-----------LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRgqeVYVKKTmGRLP-----VRW-MAIESLNYS-VYTTNSDVWSYGVLLWE-------------------IVSLGGTP- 891
Cdd:cd07832  147 AR---LFSEED-PRLYshqvaTRWyRAPELLYGSrKYDEGVDLWAVGCIFAEllngsplfpgendieqlaiVLRTLGTPn 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 892 ---YCGMTCAELYEKLPQGYRLEKPL-----NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07832  223 ektWPELTSLPDYNKITFPESKGIRLeeifpDCSPEAIDLLKGLLVYNPKKRLSAEEAL 281
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
679-942 3.05e-17

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: 82.48  E-value: 3.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACE-HRGYLYLAIE 756
Cdd:cd08223    4 FLRVIGKGSYGEVWLVRHKRDRKQY--VIKKLNlKNASKRERKAAEQEAKLLSKL-KHPNIVSYKESFEgEDGFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd08223   81 FCEGGDLYTRLK--------------EQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQEVY--VKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd08223  147 GIARVLESSsdMATTLIGTPY-YMSPELFSNKPYNHKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYKILEGKLPPMPK 224
                        250       260
                 ....*....|....*....|....*...
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08223  225 QYSPELGELIKAMLHQDPEKRPSVKRIL 252
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
678-942 3.13e-17

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 82.91  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKdgLRMDAAIKRM-KEYASKDDHRDF-AGELEVLCKLgHHPNIINLLGACE-HRGYLYLA 754
Cdd:cd14165    4 ILGINLGEGSYAKVKSAYSER--LKCNVAIKIIdKKKAPDDFVEKFlPRELEILARL-NHKSIIKTYEIFEtSDGKVYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETDPAfaianstastlssQQLLHfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd14165   81 MELGVQGDLLEFIKLRGALPEDVA-------------RKMFH---QLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSR-------GQEVYVKKTMGRLPvrWMAIESLNYSVYTTN-SDVWSYGVLLWeIVSLGGTPYCGMTCAE-LYEKLP 905
Cdd:cd14165  145 DFGFSKrclrdenGRIVLSKTFCGSAA--YAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMPYDDSNVKKmLKIQKE 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 906 QGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14165  222 HRVRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVL 258
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
683-899 3.22e-17

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: 82.27  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDfagELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRN---EIEIMNQL-RHPRLLQLYDAFETPREMVLVMEYVAGGE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGLSR 840
Cdd:cd14103   77 LFE-----RVVDDD----------FELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCvsRTGNQIKIIDFGLAR 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 841 GqevYVKKTmgRLPVRW-----MAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 899
Cdd:cd14103  142 K---YDPDK--KLKVLFgtpefVAPEVVNYEPISYATDMWSVGVICYVLLS-GLSPFMGDNDAE 199
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
677-942 5.61e-17

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: 81.89  E-value: 5.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEY-ASKDDHRDFAGELEVLCKLgHHPNIINLLGACE--HRGYLYL 753
Cdd:cd13983    3 LKFNEVLGRGSFKTVYRAFDTEEG--IEVAWNEIKLRkLPKAERQRFKQEIEILKSL-KHPNIIKFYDSWEskSKKEVIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLETdpafaianstastlssQQLLHFAADVARGMDYL-SQKQ-FIHRDLAARNILV-GENYV 830
Cdd:cd13983   80 ITELMTSGTLKQYLKRFKRLKL----------------KVIKSWCRQILEGLNYLhTRDPpIIHRDLKCDNIFInGNTGE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRGQEVYVKKTMGRLPvRWMAIESLNYSvYTTNSDVWSYGVLLWEIVSlGGTPYCgmTC---AELYEKLPQG 907
Cdd:cd13983  144 VKIGDLGLATLLRQSFAKSVIGTP-EFMAPEMYEEH-YDEKVDIYAFGMCLLEMAT-GEYPYS--ECtnaAQIYKKVTSG 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 908 YR---LEKPLncDDEVYDLMRQCWReKPYERPSFAQIL 942
Cdd:cd13983  219 IKpesLSKVK--DPELKDFIEKCLK-PPDERPSARELL 253
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
681-964 5.91e-17

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: 82.41  E-value: 5.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDglRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd06640   10 ERIGKGSFGEVFKGIDNRT--QQVVAIKIIDLEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKGTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSr 840
Cdd:cd06640   87 GSALDLLR-----------------AGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVA- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQ--EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRLEKPLNCDD 918
Cdd:cd06640  149 GQltDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAK-GEPPNSDMHPMRVLFLIPKNNPPTLVGDFSK 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 759191595 919 EVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKF 964
Cdd:cd06640  228 PFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTSYLTELIDRF 273
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
706-945 6.21e-17

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: 82.45  E-value: 6.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 706 AIKRMKEYASKDDHRDFAG----ELEVLCKLgHHPNIINLLGACEHR-GYLYLAIEYApHGNLLDFLRKSRVLETDPafa 780
Cdd:cd14001   32 AVKKINSKCDKGQRSLYQErlkeEAKILKSL-NHPNIVGFRAFTKSEdGSLCLAMEYG-GKSLNDLIEERYEAGLGP--- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 781 ianstastLSSQQLLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENY-VAKIADFG----LSRGQEVYVKKT---MG 851
Cdd:cd14001  107 --------FPAATILKVALSIARALEYLhNEKKILHGDIKSGNVLIKGDFeSVKLCDFGvslpLTENLEVDSDPKaqyVG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 852 RLPvrWMAIESLNYSVYTTN-SDVWSYGVLLWEIVSL---------GGTPYCGMTCAE-------LYEKLPQgyRLEKPL 914
Cdd:cd14001  179 TEP--WKAKEALEEGGVITDkADIFAYGLVLWEMMTLsvphlnlldIEDDDEDESFDEdeedeeaYYGTLGT--RPALNL 254
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 915 NCDDEVY----DLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14001  255 GELDDSYqkviELFYACTQEDPKDRPSAAHIVEAL 289
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
667-942 7.79e-17

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: 83.15  E-value: 7.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 667 TIYPVLDWNDIKFQDV------IGEGNFgQVLKARIKKdGLRMDAAIKRMKEyaskdDHRDFAGELEVLCKLGHHPNIIN 740
Cdd:cd14176    5 SIVQQLHRNSIQFTDGyevkedIGVGSY-SVCKRCIHK-ATNMEFAVKIIDK-----SKRDPTEEIEILLRYGQHPNIIT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 741 LLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTlssqqllhfaadvargMDYLSQKQFIHRDLAA 820
Cdd:cd14176   78 LKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKT----------------VEYLHAQGVVHRDLKP 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 821 RNILV----GENYVAKIADFGLSRgqEVYVKKTMGRLP---VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYC 893
Cdd:cd14176  142 SNILYvdesGNPESIRICDFGFAK--QLRAENGLLMTPcytANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFA 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 894 GM---TCAELYEKLPQG-YRLEKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14176  219 NGpddTPEEILARIGSGkFSLSGGYwnSVSDTAKDLVSKMLHVDPHQRLTAALVL 273
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
682-935 8.52e-17

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 82.45  E-value: 8.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARiKKDGlrMDA----AIKRMKEYASK-DDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd05582    2 VLGQGSFGKVFLVR-KITG--PDAgtlyAMKVLKKATLKvRDRVRTKMERDILADV-NHPFIVKLHYAFQTEGKLYLILD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLldFLRKSR-VL--ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05582   78 FLRGGDL--FTRLSKeVMftEEDVKF-----------------YLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEK 912
Cdd:cd05582  139 TDFGLSKESIDHEKKAYSFCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMILKA-KLGM 216
                        250       260
                 ....*....|....*....|...
gi 759191595 913 PLNCDDEVYDLMRQCWREKPYER 935
Cdd:cd05582  217 PQFLSPEAQSLLRALFKRNPANR 239
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
681-964 9.15e-17

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: 81.64  E-value: 9.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKAriKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd06642   10 ERIGKGSFGEVYKG--IDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQC-DSPYITRYYGSYLKGTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETdpafaianSTASTLSsqqllhfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSr 840
Cdd:cd06642   87 GSALDLLKPGPLEET--------YIATILR---------EILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVA- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GQ--EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGY------RLEK 912
Cdd:cd06642  149 GQltDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAK-GEPPNSDLHPMRVLFLIPKNSpptlegQHSK 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 913 PLNcddevyDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKF 964
Cdd:cd06642  228 PFK------EFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRY 273
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
675-942 1.03e-16

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: 81.61  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGE---GNFGQVLKARIKKDGLRMDAAIKRMKeyaSKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd06643    2 NPEDFWEIVGElgdGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILASC-DHPNIVKLLDAFYYENNL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLldflrKSRVLETDPAfaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd06643   78 WILIEFCAGGAV-----DAVMLELERP----------LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRGQevyvKKTMGR------LPVrWMAIESLNYSV-----YTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAEL 900
Cdd:cd06643  143 KLADFGVSAKN----TRTLQRrdsfigTPY-WMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQI-EPPHHELNPMRV 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 759191595 901 YEKLPQGY--RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06643  217 LLKIAKSEppTLAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLL 260
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
665-926 1.67e-16

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: 81.99  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 665 DPTIYPvldwNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGA 744
Cdd:cd05602    1 NPHAKP----SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 745 CEHRGYLYLAIEYAPHGNLLDFLRKSRV-LETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNI 823
Cdd:cd05602   77 FQTTDKLYFVLDYINGGELFYHLQRERCfLEPRARF-----------------YAAEIASALGYLHSLNIVYRDLKPENI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVAKIADFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELY 901
Cdd:cd05602  140 LLDSQGHIVLTDFGLCKEniEPNGTTSTFCGTP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMY 217
                        250       260
                 ....*....|....*....|....*
gi 759191595 902 EKLpqgyrLEKPLNCDDEVYDLMRQ 926
Cdd:cd05602  218 DNI-----LNKPLQLKPNITNSARH 237
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
683-942 1.80e-16

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 80.61  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAA-IKRMKEYASKD--DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14105   13 LGSGQFAVVKKCREKSTGLEYAAKfIKKRRSKASRRgvSREDIEREVSILRQV-LHPNIITLHDVFENKTDVVLILELVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA----KIAD 835
Cdd:cd14105   92 GGELFDFL----------------AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPipriKLID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR----GQEVyvkKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRL 910
Cdd:cd14105  156 FGLAHkiedGNEF---KNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITAVnYDF 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 911 EKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14105  231 DDEYfsNTSELAKDFIRQLLVKDPRKRMTIQESL 264
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
680-894 1.87e-16

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: 80.35  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDdhRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd14190    9 KEVLGGGKFGKVHTCTEKRTGLKL--AAKVINKQNSKD--KEMVlLEIQVMNQL-NHRNLIQLYEAIETPNEIVLFMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADF 836
Cdd:cd14190   84 EGGELFE-----RIVDED----------YHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDF 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 837 GLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd14190  149 GLARRYNPREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPFLG 205
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
682-839 2.20e-16

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: 80.49  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14046   13 VLGKGAFGQVVKVRNKLDGRYY--AIKKIKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQMEYCEKS 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 762 NLLDFLRKSRVLETDpafaianstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14046   90 TLRDLIDSGLFQDTD----------------RLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLA 151
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
678-887 2.66e-16

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: 80.39  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAgELEVLCKLGHHPNIINLlgaCEH-----RGYL 751
Cdd:cd07831    2 KILGKIGEGTFSEVLKAQSRKTGKYY--AIKCMKKhFKSLEQVNNLR-EIQALRRLSPHPNILRL---IEVlfdrkTGRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYApHGNLLDFLRKSRVLetdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVgENYVA 831
Cdd:cd07831   76 ALVFELM-DMNLYELIKGRKRP---------------LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDIL 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 832 KIADFGLSRGqeVYVKktmgrLP------VRWM-AIESLNYS-VYTTNSDVWSYGVLLWEIVSL 887
Cdd:cd07831  139 KLADFGSCRG--IYSK-----PPyteyisTRWYrAPECLLTDgYYGPKMDIWAVGCVFFEILSL 195
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
683-935 2.84e-16

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: 79.96  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYA--SKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTF--ALKCVKKRHivQTRQQEHIFSEKEIL-EECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRkSRVLetdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG--- 837
Cdd:cd05572   78 GELWTILR-DRGL---------------FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGfak 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 -LSRGQEVYvkkTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG-----MtcaELYEKLPQG-YRL 910
Cdd:cd05572  142 kLGSGRKTW---TFCGTP-EYVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFGGddedpM---KIYNIILKGiDKI 213
                        250       260
                 ....*....|....*....|....*
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYER 935
Cdd:cd05572  214 EFPKYIDKNAKNLIKQLLRRNPEER 238
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
683-942 3.05e-16

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: 79.97  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrmdaaikrmKEYASK---------DDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd14198   16 LGRGKFAVVRQCISKSTG----------QEYAAKflkkrrrgqDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFlrksrvletdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV--- 830
Cdd:cd14198   86 ILEYAAGGEIFNL--------------CVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlgd 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSR--GQEVYVKKTMGrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQ-- 906
Cdd:cd14198  152 IKIVDFGMSRkiGHACELREIMG--TPEYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQETFLNISQvn 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 907 -GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14198  229 vDYSEETFSSVSQLATDFIQKLLVKNPEKRPTAEICL 265
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
683-899 3.36e-16

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 79.68  E-value: 3.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHR-----DFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14194   13 LGSGQFAVVKKCREKSTGLQY--AAKFIKKRRTKSSRRgvsreDIEREVSILKEI-QHPNVITLHEVYENKTDVILILEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA----KI 833
Cdd:cd14194   90 VAGGELFDFL----------------AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPkpriKI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSR----GQEVyvkKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 899
Cdd:cd14194  154 IDFGLAHkidfGNEF---KNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 218
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
681-945 3.97e-16

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: 79.65  E-value: 3.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKdglrmdaAIkrmkEY---ASKDDHR--DFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd14010    6 DEIGRGKHSVVYKGRRKG-------TI----EFvaiKCVDKSKrpEVLNEVRLTHEL-KHPNVLKFYEWYETSNHLWLVV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd14010   74 EYCTGGDLETLLRQDG----------------NLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRGQEVYVKKTMG-------------RLPVR----WMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA 898
Cdd:cd14010  138 FGLARREGEILKELFGqfsdegnvnkvskKQAKRgtpyYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFVAESFT 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 899 ELYEKLpqgyrLEKPLNcddevydLMRQCWREKPyeRPSFAQILVSL 945
Cdd:cd14010  217 ELVEKI-----LNEDPP-------PPPPKVSSKP--SPDFKSLLKGL 249
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
683-942 4.16e-16

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: 79.27  E-value: 4.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKrmkEYASKDDHRD-------FAGELEVLCKLgHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd13994    1 IGKGATSVVRIVTKKNPRSGVLYAVK---EYRRRDDESKrkdyvkrLTSEYIISSKL-HHPNIVKVLDLCQDLHGKWCLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 -EYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd13994   77 mEYCPGGDLFTLIEKAD----------------SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSR------GQEVYVKKTM-GRLPvrWMAIESLNYSVYT-TNSDVWSYGVLL---------WEIVS---LGGTPYCG 894
Cdd:cd13994  141 DFGTAEvfgmpaEKESPMSAGLcGSEP--YMAPEVFTSGSYDgRAVDVWSCGIVLfalftgrfpWRSAKksdSAYKAYEK 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 759191595 895 MtcAELYEKLPQGYRLEKPLNCDDEVYDLMRQcwreKPYERPSFAQIL 942
Cdd:cd13994  219 S--GDFTNGPYEPIENLLPSECRRLIYRMLHP----DPEKRITIDEAL 260
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
676-942 5.79e-16

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: 79.60  E-value: 5.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKkdGLRMDAAIKRMKEyaSKDDHRDfagELEVLCKLGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHK--ATGKEYAVKIIDK--SKRDPSE---EIEILLRYGQHPNIITLRDVYDDGNSVYLVT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLD-FLRKSRVLETDPAFAIANstastlssqqllhfaadVARGMDYLSQKQFIHRDLAARNILvgenYVA--- 831
Cdd:cd14091   74 ELLRGGELLDrILRQKFFSEREASAVMKT-----------------LTKTVEYLHSQGVVHRDLKPSNIL----YADesg 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 -----KIADFGLSrgqevyvkKTM----GRL--P---VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYC---G 894
Cdd:cd14091  133 dpeslRICDFGFA--------KQLraenGLLmtPcytANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFAsgpN 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 895 MTCAELYEKLPQG-YRLEKP--LNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14091  204 DTPEVILARIGSGkIDLSGGnwDHVSDSAKDLVRKMLHVDPSQRPTAAQVL 254
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
683-941 6.27e-16

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: 79.08  E-value: 6.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdgLRMDAAIKRMKEYASKDDHRDF----AGELEVLcKLGHhpnIINLLGACehRGYLYLAIEYA 758
Cdd:cd14025    4 VGSGGFGQVYKVRHKH--WKTWLAIKCPPSLHVDDSERMElleeAKKMEMA-KFRH---ILPVYGIC--SEPVGLVMEYM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLrKSRVLETDPAFAIANSTAStlssqqllhfaadvarGMDYLS--QKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd14025   76 ETGSLEKLL-ASEPLPWELRFRIIHETAV----------------GMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDF 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQEVYVKKTMGRLPVR----WMAIESLNYS--VYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC-AELYEKLPQGYR 909
Cdd:cd14025  139 GLAKWNGLSHSHDLSRDGLRgtiaYLPPERFKEKnrCPDTKHDVYSFAIVIWGILT-QKKPFAGENNiLHIMVKVVKGHR 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 910 LEKPLNCD------DEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14025  218 PSLSPIPRqrpsecQQMICLMKRCWDQDPRKRPTFQDI 255
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
678-942 6.27e-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: 78.65  E-value: 6.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDV--IGEGNFGQVLKARIKKDglRMDAAIKRMkEYASKDDH---RDFAGELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd06607    2 IFEDLreIGHGSFGAVYYARNKRT--SEVVAIKKM-SYSGKQSTekwQDIIKEVKFLRQL-RHPNTIEYKGCYLREHTAW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEY--APHGNLLDFLRKSrvLETDPAFAIAnstastlssqqllhfaADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd06607   78 LVMEYclGSASDIVEVHKKP--LQEVEIAAIC----------------HGALQGLAYLHSHNRIHRDVKAGNILLTEPGT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGlsRGQEVYVKKTMGRLPVrWMAIE---SLNYSVYTTNSDVWSYGVllweivslggtpycgmTCAELYEKLPQG 907
Cdd:cd06607  140 VKLADFG--SASLVCPANSFVGTPY-WMAPEvilAMDEGQYDGKVDVWSLGI----------------TCIELAERKPPL 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 908 YRL------------EKPLNCDDEVYDLMRQ----CWREKPYERPSFAQIL 942
Cdd:cd06607  201 FNMnamsalyhiaqnDSPTLSSGEWSDDFRNfvdsCLQKIPQDRPSAEDLL 251
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
683-941 6.49e-16

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: 78.45  E-value: 6.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVlkarikKDGLRMD----AAIKRMKeyasKDDHRDFAG-------ELEVLCKLgHHPNIINLLGAC--EHRG 749
Cdd:cd14119    1 LGEGSYGKV------KEVLDTEtlcrRAVKILK----KRKLRRIPNgeanvkrEIQILRRL-NHRNVIKLVDVLynEEKQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYApHGNLLDFLRKSrvleTDPAFAIAnstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd14119   70 KLYMVMEYC-VGGLQEMLDSA----PDKRLPIW----------QAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDG 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFG----LSRGQEVYV-KKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 904
Cdd:cd14119  135 TLKISDFGvaeaLDLFAEDDTcTTSQGSPAFQPPEIANGQDSFSGFKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENI 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 905 PQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14119  214 GKG-EYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
724-941 6.62e-16

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: 78.94  E-value: 6.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 724 GELEVLCKLgHHPNIINLLGACE--HRGYLYLAIEyaphgnlldFLRKSRVLEtDPafaiansTASTLSSQQLLHFAADV 801
Cdd:cd14118   63 REIAILKKL-DHPNVVKLVEVLDdpNEDNLYMVFE---------LVDKGAVME-VP-------TDNPLSEETARSYFRDI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 802 ARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS---RGQEVYVKKTMGRlPVrWMAIESL-----NYSVYTTnsD 873
Cdd:cd14118  125 VLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSnefEGDDALLSSTAGT-PA-FMAPEALsesrkKFSGKAL--D 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 874 VWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQGyRLEKPLNC--DDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14118  201 IWAMGVTLYCFV-FGRCPFEDDHILGLHEKIKTD-PVVFPDDPvvSEQLKDLILRMLDKNPSERITLPEI 268
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
681-942 6.72e-16

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: 79.02  E-value: 6.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQV---------LKArIKKDGLRMDAAIKRMKEYASKDDhrdfagELEVLCKLGHHpNIINLLGACEHRGYL 751
Cdd:cd06631    7 NVLGKGAYGTVycgltstgqLIA-VKQVELDTSDKEKAEKEYEKLQE------EVDLLKTLKHV-NIVGYLGTCLEDNVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRKSRVLEtDPAFAianstastLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd06631   79 SIFMEFVPGGSIASILARFGALE-EPVFC--------RYTKQIL-------EGVAYLHNNNVIHRDIKGNNIMLMPNGVI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFG--------LSRGQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMT--CAELY 901
Cdd:cd06631  143 KLIDFGcakrlcinLSSGSQSQLLKSMRGTPY-WMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNpmAAIFA 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 759191595 902 EKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06631  221 IGSGRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLL 261
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
683-884 8.71e-16

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: 78.92  E-value: 8.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdAAIKRMKEYASKDDHR-DFAGELEVLCKLG--HHPNIINLLGAC-----EHRGYLYLA 754
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGGRF-VALKRVRVQTGEEGMPlSTIREVAVLRHLEtfEHPNVVRLFDVCtvsrtDRETKLTLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHgNLLDFLRKSrvletdPAFAIANSTASTLSSQQLlhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd07862   88 FEHVDQ-DLTTYLDKV------PEPGVPTETIKDMMFQLL--------RGLDFLHSHRVVHRDLKPQNILVTSSGQIKLA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd07862  153 DFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEM 202
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
683-837 9.38e-16

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: 74.79  E-value: 9.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYAsKDDHRDFAGELEVLCKL-GHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGV--AVKIGDDVN-NEEGEDLESEMDILRRLkGLELNIPKVLVTEDVDGPNILLMELVKGG 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 762 NLLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd13968   78 TLIAYT-----------------QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
676-942 9.85e-16

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: 78.62  E-value: 9.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd06617    2 DLEVIEELGRGAYGVVDKMRHVPTGTIM--AVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYApHGNLLDFLRKsrVLETDpafaianstaSTLSSQQLLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd06617   80 EVM-DTSLDKFYKK--VYDKG----------LTIPEDILGKIAVSIVKALEYLhSKLSVIHRDVKPSNVLINRNGQVKLC 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSrGQEV-YVKKTM--GRLPvrWMAIE----SLNYSVYTTNSDVWSYGVLLWEIvSLGGTPYcgMTCAELYEKLPQG 907
Cdd:cd06617  147 DFGIS-GYLVdSVAKTIdaGCKP--YMAPErinpELNQKGYDVKSDVWSLGITMIEL-ATGRFPY--DSWKTPFQQLKQV 220
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 908 YRLEKPLNCDD----EVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06617  221 VEEPSPQLPAEkfspEFQDFVNKCLKKNYKERPNYPELL 259
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
725-944 1.02e-15

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: 78.85  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 725 ELEVLCKLgHHPNIINLLGACE--HRGYLYLAIEYAPHGNLLDFlrksrvletdpafaianSTASTLSSQQLLHFAADVA 802
Cdd:cd14199   75 EIAILKKL-DHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVMEV-----------------PTLKPLSEDQARFYFQDLI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 803 RGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS---RGQEVYVKKTMGRlPVrWMAIESLNYS--VYTTNS-DVWS 876
Cdd:cd14199  137 KGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSnefEGSDALLTNTVGT-PA-FMAPETLSETrkIFSGKAlDVWA 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 877 YGVLLWEIVsLGGTPYCGMTCAELYEKLpQGYRLEKPLNCD--DEVYDLMRQCWREKPYERPSFAQILVS 944
Cdd:cd14199  215 MGVTLYCFV-FGQCPFMDERILSLHSKI-KTQPLEFPDQPDisDDLKDLLFRMLDKNPESRISVPEIKLH 282
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
678-840 1.06e-15

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: 79.25  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKeyASKDDH--------RDFAgelevLCKLGHHPNIINLLGAC-EH- 747
Cdd:cd07842    3 EIEGCIGRGTYGRVYKAKRKNGKDGKEYAIKKFK--GDKEQYtgisqsacREIA-----LLRELKHENVVSLVEVFlEHa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 RGYLYLAIEYAPH--GNLLDFLRKSRVLETDPafaianstaSTLSS--QQLLHfaadvarGMDYLSQKQFIHRDLAARNI 823
Cdd:cd07842   76 DKSVYLLFDYAEHdlWQIIKFHRQAKRVSIPP---------SMVKSllWQILN-------GIHYLHSNWVLHRDLKPANI 139
                        170       180
                 ....*....|....*....|.
gi 759191595 824 LV----GENYVAKIADFGLSR 840
Cdd:cd07842  140 LVmgegPERGVVKIGDLGLAR 160
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
682-915 1.08e-15

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: 79.24  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd05603    2 VIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSR-VLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd05603   82 ELFFHLQRERcFLEPRARF-----------------YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCK 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 841 -GQEVY-VKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLpqgyrLEKPLN 915
Cdd:cd05603  145 eGMEPEeTTSTFCGTP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFYSRDVSQMYDNI-----LHKPLH 214
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
671-899 1.10e-15

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 78.46  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 671 VLDWNDIkfQDVIGEGNFGQVLKARIKKDGLRMDAA-IKRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEH 747
Cdd:cd14196    3 VEDFYDI--GEELGSGQFAIVKKCREKSTGLEYAAKfIKKRQSRASRRGvsREEIEREVSILRQV-LHPNIITLHDVYEN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 RGYLYLAIEYAPHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 827
Cdd:cd14196   80 RTDVVLILELVSGGELFDFL----------------AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLD 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 828 NYVA----KIADFGLSRGQEVYVK-KTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 899
Cdd:cd14196  144 KNIPiphiKLIDFGLAHEIEDGVEfKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 218
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
678-891 1.16e-15

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: 79.11  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYaskDDHRDFAG----ELEVLCKLgHHPNIINLLGACEHRGY--- 750
Cdd:cd07834    3 ELLKPIGSGAYGVVCSAYDKRTGRKV--AIKKISNV---FDDLIDAKrilrEIKILRHL-KHENIIGLLDILRPPSPeef 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 --LYLAIEYaphgnlldflrksrvLETDPAFAIANStaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd07834   77 ndVYIVTEL---------------METDLHKVIKSP--QPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSN 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 829 YVAKIADFGLSRGQEVYVKKTM--GRLPVRW------MaiesLNYSVYTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd07834  140 CDLKICDFGLARGVDPDEDKGFltEYVVTRWyrapelL----LSSKKYTKAIDIWSVGCIFAEL--LTRKP 204
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
681-941 1.21e-15

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: 77.69  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQV-------------LK--ARIKKDGLRMDAAIKRmkeyaskddhrdfagELEVLcKLGHHPNIINLLGAC 745
Cdd:cd14079    8 KTLGVGSFGKVklaeheltghkvaVKilNRQKIKSLDMEEKIRR---------------EIQIL-KLFRHPHIIRLYEVI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIAnstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV 825
Cdd:cd14079   72 ETPTDIFMVMEYVSGGELFDYIVQKGRLSEDEARRFF---------QQII-------SGVEYCHRHMVVHRDLKPENLLL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYVAKIADFGLSR----GQevYVKKTMGRlPvRWMAIESLNYSVYT-TNSDVWSYGVLLWeiVSLGGT-PYCGMTCAE 899
Cdd:cd14079  136 DSNMNVKIADFGLSNimrdGE--FLKTSCGS-P-NYAAPEVISGKLYAgPEVDVWSCGVILY--ALLCGSlPFDDEHIPN 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 900 LYEKLPQG-YRLEKPLNcdDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14079  210 LFKKIKSGiYTIPSHLS--PGARDLIKRMLVVDPLKRITIPEI 250
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
683-892 1.32e-15

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: 77.87  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQV--AVKKMD--LRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVLETdpafAIAnstasTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL--SR 840
Cdd:cd06648   91 LTDIVTHTRMNEE----QIA-----TVCRA--------VLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFcaQV 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 841 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06648  154 SKEVPRRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPY 203
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
712-942 1.61e-15

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: 78.13  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 712 EYASK---DDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANStast 788
Cdd:cd14178   30 EYAVKiidKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQKCFSEREASAVLCT---- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 789 lssqqllhfaadVARGMDYLSQKQFIHRDLAARNIL----VGENYVAKIADFGLSRgqEVYVKKTMGRLP---VRWMAIE 861
Cdd:cd14178  106 ------------ITKTVEYLHSQGVVHRDLKPSNILymdeSGNPESIRICDFGFAK--QLRAENGLLMTPcytANFVAPE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 862 SLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM---TCAELYEKLPQGYRLEKPLNCD---DEVYDLMRQCWREKPYER 935
Cdd:cd14178  172 VLKRQGYDAACDIWSLGILLYTMLA-GFTPFANGpddTPEEILARIGSGKYALSGGNWDsisDAAKDIVSKMLHVDPHQR 250

                 ....*..
gi 759191595 936 PSFAQIL 942
Cdd:cd14178  251 LTAPQVL 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
680-942 1.80e-15

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: 78.15  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFgQVLKARIKKdGLRMDAAIKRMKEyaskdDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14175    6 KETIGVGSY-SVCKRCVHK-ATNMEYAVKVIDK-----SKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAFAIanstastlssqqlLHfaaDVARGMDYLSQKQFIHRDLAARNILV----GENYVAKIAD 835
Cdd:cd14175   79 GGELLDKILRQKFFSEREASSV-------------LH---TICKTVEYLHSQGVVHRDLKPSNILYvdesGNPESLRICD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRgqEVYVKKTMGRLP---VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYC---GMTCAELYEKLPQGYR 909
Cdd:cd14175  143 FGFAK--QLRAENGLLMTPcytANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFAngpSDTPEEILTRIGSGKF 219
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 910 LEKPLNCD---DEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14175  220 TLSGGNWNtvsDAAKDLVSKMLHVDPHQRLTAKQVL 255
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
493-585 2.00e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 493 PPQPENIKISNITDSTAMISWTILDGysISSIIIRYKIQ--GKNEDQHIDVKIKNATITQYQLKGLEPQTVYQVDIFAEN 570
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPED--DGGPITGYVVEyrEKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                         90
                 ....*....|....*
gi 759191595 571 NIGSSNPTFSHELTT 585
Cdd:cd00063   79 GGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
397-480 2.24e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.06  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRAR-VNTKA 475
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQaVNGGG 80

                  ....*
gi 759191595  476 QGEWS 480
Cdd:pfam00041  81 EGPPS 85
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
683-942 2.40e-15

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 78.26  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDD---HRDFAG----------ELEVLCKLgHHPNIINLLGACEHRG 749
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTG--KIVAIKKVKIIEISNDvtkDRQLVGmcgihfttlrELKIMNEI-KHENIMGLVDVYVEGD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYApHGNLldflrkSRVLETDPAFAIANSTASTLssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:PTZ00024  94 FINLVMDIM-ASDL------KKVVDRKIRLTESQVKCILL---QIL-------NGLNVLHKWYFMHRDLSPANIFINSKG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSR--GQEVYVKKTMG-------------------RLPVRWMAIESLNYSVyttnsDVWSYGVLLWE----- 883
Cdd:PTZ00024 157 ICKIADFGLARryGYPPYSDTLSKdetmqrreemtskvvtlwyRAPELLMGAEKYHFAV-----DMWSVGCIFAElltgk 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 884 --------------IVSLGGTP-------------YCGMTCAElyeklPQGYRLEKPLNCDDEVyDLMRQCWREKPYERP 936
Cdd:PTZ00024 232 plfpgeneidqlgrIFELLGTPnednwpqakklplYTEFTPRK-----PKDLKTIFPNASDDAI-DLLQSLLKLNPLERI 305

                 ....*.
gi 759191595 937 SFAQIL 942
Cdd:PTZ00024 306 SAKEAL 311
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
725-942 2.55e-15

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: 77.01  E-value: 2.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 725 ELEVLCKLgHHPNIINLLG-ACEHRGY-----LYLAIEYAPHGNLLDFLrkSRVLETDPAfaianstastlssqQLLHFA 798
Cdd:cd14012   48 ELESLKKL-RHPNLVSYLAfSIERRGRsdgwkVYLLTEYAPGGSLSELL--DSVGSVPLD--------------TARRWT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 799 ADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADFGL--------SRGQEVYVKKTmgrlpvRWMAIESLNYSV 867
Cdd:cd14012  111 LQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLgktlldmcSRGSLDEFKQT------YWLPPELAQGSK 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 868 -YTTNSDVWSYGVLLWEIVslggtpyCGMTCAELYEkLPQGYRLekPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14012  185 sPTRKTDVWDLGLLFLQML-------FGLDVLEKYT-SPNPVLV--SLDLSASLQDFLSKCLSLDPKKRPTALELL 250
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
682-942 2.98e-15

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: 76.91  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDfaGELEVLCKLGHhPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14185    7 TIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIE--SEILIIKSLSH-PNIVKLFEVYETEKEIYLILEYVRGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKS-RVLETDPAFAIanstastlssqqllhfaADVARGMDYLSQKQFIHRDLAARNILVGEN----YVAKIADF 836
Cdd:cd14185   84 DLFDAIIESvKFTEHDAALMI-----------------IDLCEALVYIHSKHIVHRDLKPENLLVQHNpdksTTLKLADF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRgqevYVKK---TMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCG--MTCAELYEKLPQG-YRL 910
Cdd:cd14185  147 GLAK----YVTGpifTVCGTPT-YVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFRSpeRDQEELFQIIQLGhYEF 220
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 911 EKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14185  221 LPPYwdNISEAAKDLISRLLVVDPEKRYTAKQVL 254
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
676-942 3.06e-15

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 77.48  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDV-----IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVL--CklgHHPNIINLLGAC-EH 747
Cdd:cd06620    1 DLKNQDLetlkdLGAGNGGSVSKVLHIPTGTIM--AKKVIHIDAKSSVRKQILRELQILheC---HSPYIVSFYGAFlNE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 RGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANStastlssqqllhfaadVARGMDYL-SQKQFIHRDLAARNILVG 826
Cdd:cd06620   76 NNNIIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVA----------------VLEGLTYLyNVHRIIHRDIKPSNILVN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 827 ENYVAKIADFGLSRG-----QEVYVKKTMGRLPVRwmaIESLNYSVyttNSDVWSYGVLLWEIVsLGGTPYCGMTCAELY 901
Cdd:cd06620  140 SKGQIKLCDFGVSGElinsiADTFVGTSTYMSPER---IQGGKYSV---KSDVWSLGLSIIELA-LGEFPFAGSNDDDDG 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759191595 902 EKLPQGY-------------RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06620  213 YNGPMGIldllqrivnepppRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLL 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
683-942 3.59e-15

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 76.62  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrmdaaikrmKEYASK---------DDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd14106   16 LGRGKFAVVRKCIHKETG----------KEYAAKflrkrrrgqDCRNEILHEIAVLELCKDCPRVVNLHEVYETRSELIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLldflrkSRVLETDPAFaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA-- 831
Cdd:cd14106   86 ILELAAGGEL------QTLLDEEECL----------TEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLgd 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 -KIADFGLSR--GQEVYVKKTMGrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGy 908
Cdd:cd14106  150 iKLCDFGISRviGEGEEIREILG--TPDYVAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDKQETFLNISQC- 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 909 RLEKPLNCDDEV----YDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14106  226 NLDFPEELFKDVsplaIDFIKRLLVKDPEKRLTAKECL 263
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
683-936 4.24e-15

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: 76.49  E-value: 4.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyasKDD-------HRDFAgELEVLCKLgHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLY--AIKVIK----KRDmirknqvDSVLA-ERNILSQA-QNPFVVKLYYSFQGKKNLYLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05579   73 EYLPGGDLYSLLENVGALDEDVA----------------RIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR----GQEVYVKKTMGRLPVR------------WMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 899
Cdd:cd05579  137 FGLSKvglvRRQIKLSIQKKSNGAPekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLV-GIPPFHAETPEE 215
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 900 LYEKLPQGyRLEKP--LNCDDEVYDLMRQCWREKPYERP 936
Cdd:cd05579  216 IFQNILNG-KIEWPedPEVSDEAKDLISKLLTPDPEKRL 253
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
683-935 5.67e-15

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: 75.98  E-value: 5.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMK--EYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYF--AIKVLKksDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd05611   82 GDCASLIK----------------TLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 GqeVYVKKTMGRL---PvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQ---GYRLEKPL 914
Cdd:cd05611  146 N--GLEKRHNKKFvgtP-DYLAPETILGVGDDKMSDWWSLGCVIFEFL-FGYPPFHAETPDAVFDNILSrriNWPEEVKE 221
                        250       260
                 ....*....|....*....|.
gi 759191595 915 NCDDEVYDLMRQCWREKPYER 935
Cdd:cd05611  222 FCSPEAVDLINRLLCMDPAKR 242
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
676-904 6.05e-15

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: 76.96  E-value: 6.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKAriKKDGLRMDAAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLA--ERKGTDELYAVKILKKdvVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRK-SRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05616   79 VMEYVNGGDLMYHIQQvGRFKEPHAVF-----------------YAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIK 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 833 IADFGLSRGQ--EVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 904
Cdd:cd05616  142 IADFGMCKENiwDGVTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSI 213
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
676-948 6.33e-15

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: 76.22  E-value: 6.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDglRMDAAIKRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATCLLD--RKPVALKKVQIFEMMDAkaRQDCVKEIDLLKQL-NHPNVIKYLDSFIEDNELNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNL---LDFLRKSRVLetdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd08228   80 VLELADAGDLsqmIKYFKKQKRL---------------IPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCG--MTCAELYEKLPQ 906
Cdd:cd08228  145 VKLGDLGLGRffSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGdkMNLFSLCQKIEQ 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 907 -GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd08228  223 cDYPPLPTEHYSEKLRELVSMCIYPDPDQRPDIGYVHQIAKQM 265
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
682-915 6.85e-15

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: 76.92  E-value: 6.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd05604    3 VIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd05604   83 ELFFHLQRER----------------SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 842 --QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpqgyrLEKPLN 915
Cdd:cd05604  147 giSNSDTTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEMLY-GLPPFYCRDTAEMYENI-----LHKPLV 215
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
678-892 6.97e-15

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: 75.76  E-value: 6.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARiKKDGLRMDAaikrMKeYASKDDH------RDFAGELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd05578    3 QILRVIGKGSFGKVCIVQ-KKDTKKMFA----MK-YMNKQKCiekdsvRNVLNELEILQEL-EHPFLVNLWYSFQDEEDM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLaieyaphgnLLDFLrksrvLETDPAFAIanSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd05578   76 YM---------VVDLL-----LGGDLRYHL--QQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHV 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 832 KIADFGLSR--GQEVYVKKTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPY 892
Cdd:cd05578  140 HITDFNIATklTDGTLATSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYEML-RGKRPY 199
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
681-935 7.74e-15

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: 76.33  E-value: 7.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDglrmDAAIKRMkeyaSKDDHRDFAGELEVL-CKLGHHPNIINLLGACEHRG----YLYLAI 755
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGE----DVAVKIF----SSREERSWFREAEIYqTVMLRHENILGFIAADNKDNgtwtQLWLVS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRVletdPAFAIANSTASTLSSQQLLHFAADVARGmdylsqKQFI-HRDLAARNILVGENYVAKIA 834
Cdd:cd14143   73 DYHEHGSLFDYLNRYTV----TVEGMIKLALSIASGLAHLHMEIVGTQG------KPAIaHRDLKSKNILVKKNGTCCIA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLS-------------RGQEVYVKktmgrlpvRWMAIESLNYSVYTTN------SDVWSYGVLLWEIV---SLGGT-- 890
Cdd:cd14143  143 DLGLAvrhdsatdtidiaPNHRVGTK--------RYMAPEVLDDTINMKHfesfkrADIYALGLVFWEIArrcSIGGIhe 214
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 891 ----PYCGMTCA----ELYEKL--PQGYRLEKP---LNCD--DEVYDLMRQCWREKPYER 935
Cdd:cd14143  215 dyqlPYYDLVPSdpsiEEMRKVvcEQKLRPNIPnrwQSCEalRVMAKIMRECWYANGAAR 274
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
675-904 7.81e-15

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: 76.94  E-value: 7.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMK--EYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLY 752
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVY--AMKILRksDMLKREQIAHVRAERDILAD-ADSPWIVRLHYAFQDEDHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05573   78 LVMEYMPGGDLMNLLIKYDVFPEETA----------------RFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSRG------------QEVYVKKTMGRLPVRW------------------MAIESLNYSVYTTNSDVWSYGVLLW 882
Cdd:cd05573  142 LADFGLCTKmnksgdresylnDSVNTLFQDNVLARRRphkqrrvraysavgtpdyIAPEVLRGTGYGPECDWWSLGVILY 221
                        250       260
                 ....*....|....*....|..
gi 759191595 883 EIVSlGGTPYCGMTCAELYEKL 904
Cdd:cd05573  222 EMLY-GFPPFYSDSLVETYSKI 242
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
735-946 1.05e-14

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: 75.36  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEHRGYLYLAIEYAPHGNLLDFL-RKSRVLETDPAFAIANSTASTLSsqqllhfaadvargmdYLSQKQF 813
Cdd:cd05077   67 HKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMhRKSDVLTTPWKFKVAKQLASALS----------------YLEDKDL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 814 IHRDLAARNILVGENYV-------AKIADFG-----LSRGQEVyvkktmGRLPvrWMAIESLNYS-VYTTNSDVWSYGVL 880
Cdd:cd05077  131 VHGNVCTKNILLAREGIdgecgpfIKLSDPGipitvLSRQECV------ERIP--WIAPECVEDSkNLSIAADKWSFGTT 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 881 LWEIVSLGGTPYCGMTCAElYEKLPQG-YRLEKPlNCdDEVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd05077  203 LWEICYNGEIPLKDKTLAE-KERFYEGqCMLVTP-SC-KELADLMTHCMNYDPNQRPFFRAIMRDIN 266
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
680-894 1.17e-14

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: 75.04  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHrDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14191    7 EERLGSGKFGQVFRLVEKKTKKVW--AGKFFKAYSAKEKE-NIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLEMVS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA--DFG 837
Cdd:cd14191   83 GGELFE-----RIIDED----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKliDFG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 838 LSRGQEvyvkkTMGRLPV-----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd14191  148 LARRLE-----NAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 203
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
682-944 1.19e-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: 75.13  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDG---------------LRMDAAIKRmkeyaskddhrdfagELEVLcKLGHHPNIINLLGACE 746
Cdd:cd14663    7 TLGEGTFAKVKFARNTKTGesvaikiidkeqvarEGMVEQIKR---------------EIAIM-KLLRHPNIVELHEVMA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 747 HRGYLYLAIEYAPHGNLLDFLRKSRVLETDPA---FaianstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNI 823
Cdd:cd14663   71 TKTKIFFVMELVTGGELFSKIAKNGRLKEDKArkyF------------QQLI-------DAVDYCHSRGVFHRDLKPENL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 824 LVGENYVAKIADFGLSRGQEVYvkKTMGRLPVR-----WMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTC 897
Cdd:cd14663  132 LLDEDGNLKISDFGLSALSEQF--RQDGLLHTTcgtpnYVAPEVLARRGYDgAKADIWSCGVILFVLLA-GYLPFDDENL 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 898 AELYEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVS 944
Cdd:cd14663  209 MALYRKIMKG-EFEYPRWFSPGAKSLIKRILDPNPSTRITVEQIMAS 254
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
681-942 1.33e-14

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: 74.73  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14078    9 ETIGSGGFAKVKLATHILTGEKV--AIKIMDKKALGDDLPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVLEYCPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFL-RKSRVLETDPAfaianstastlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL- 838
Cdd:cd14078   86 GELFDYIvAKDRLSEDEAR-----------------VFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLc 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 --SRGQEVYVKKTMGRLPVrWMAIESLNYSVYTTN-SDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPLN 915
Cdd:cd14078  149 akPKGGMDHHLETCCGSPA-YAAPELIQGKPYIGSeADVWSMGVLLYALLC-GFLPFDDDNVMALYRKIQSG-KYEEPEW 225
                        250       260
                 ....*....|....*....|....*..
gi 759191595 916 CDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14078  226 LSPSSKLLLDQMLQVDPKKRITVKELL 252
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
683-891 1.42e-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: 75.87  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDdhrdfaG-------ELEVLCKLgHHPNIINLLG--ACEHRGYLYL 753
Cdd:cd07845   15 IGEGTYGIVYRARDTTSGEIV--ALKKVRMDNERD------GipisslrEITLLLNL-RHPNIVELKEvvVGKHLDSIFL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPH--GNLLDflrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd07845   86 VMEYCEQdlASLLD------------------NMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 832 KIADFGLSRGQEVYVKKTMGRLPVRWM-AIESL-NYSVYTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd07845  148 KIADFGLARTYGLPAKPMTPKVVTLWYrAPELLlGCTTYTTAIDMWAVGCILAEL--LAHKP 207
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
676-955 1.56e-14

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 76.01  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHhPNIINLLGACEHRGYLYLAI 755
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSH-PFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKsrvletdpAFAIANSTASTLSSQQLLHFaadvargmDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:PTZ00263  98 EFVVGGELFTHLRK--------AGRFPNDVAKFYHAELVLAF--------EYLHSKDIIYRDLKPENLLLDNKGHVKVTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRgqevyvkktmgRLPVR---------WMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQ 906
Cdd:PTZ00263 162 FGFAK-----------KVPDRtftlcgtpeYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPFFDDTPFRIYEKILA 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 907 GyRLEKPLNCDDEVYDLMRQCWREKPYERpsfaqiLVSLNRMLEERKTY 955
Cdd:PTZ00263 230 G-RLKFPNWFDGRARDLVKGLLQTDHTKR------LGTLKGGVADVKNH 271
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
672-935 1.56e-14

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: 76.12  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRG 749
Cdd:cd05619    2 LTIEDFVLHKMLGKGSFGKVFLAELKGTNQFF--AIKALKKdvVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHGNLLDFLRKSRvletdpAFAIANSTastlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd05619   80 NLFFVMEYLNGGDLMFHIQSCH------KFDLPRAT----------FYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSRGQEVYVKKTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYeklpQGY 908
Cdd:cd05619  144 HIKIADFGMCKENMLGDAKTSTFCGTpDYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELF----QSI 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 909 RLEKPLN---CDDEVYDLMRQCWREKPYER 935
Cdd:cd05619  219 RMDNPFYprwLEKEAKDILVKLFVREPERR 248
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
493-575 1.59e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.57  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595   493 PPQPENIKISNITDSTAMISWTILDGYSISSIIIRYKIQGKNEDQHIDVKIKNATITQYQLKGLEPQTVYQVDIFAENNI 572
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                   ...
gi 759191595   573 GSS 575
Cdd:smart00060  81 GEG 83
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
673-942 1.69e-14

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: 74.75  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWNDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDD---HRDFAgelevLCKLGHHPNIINLLGACEHRG 749
Cdd:cd06624    6 EYDESGERVVLGKGTFGVVYAARDLSTQVRI--AIKEIPERDSREVqplHEEIA-----LHSRLSHKNIVQYLGSVSEDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHGNLldflrkSRVLETDPAFAIANSTASTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGE-N 828
Cdd:cd06624   79 FFKIFMEQVPGGSL------SALLRSKWGPLKDNENTIGYYTKQIL-------EGLKYLHDNKIVHRDIKGDNVLVNTyS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSR---GQEVYVKKTMGRLpvRWMAIESLNYSV--YTTNSDVWSYGVLLWEIVSLG------GTPYCGMTC 897
Cdd:cd06624  146 GVVKISDFGTSKrlaGINPCTETFTGTL--QYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKppfielGEPQAAMFK 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 759191595 898 AELYEKLPqgyrlEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06624  224 VGMFKIHP-----EIPESLSEEAKSFILRCFEPDPDKRATASDLL 263
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
679-886 1.73e-14

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 74.85  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDV--IGEGNFGQVLKARIKKDG-------LRMDAAIKRMKEYASKddhrdfagELEVLCKLgHHPNIINLLGACEHRG 749
Cdd:cd07860    2 FQKVekIGEGTYGVVYKARNKLTGevvalkkIRLDTETEGVPSTAIR--------EISLLKEL-NHPNIVKLLDVIHTEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYApHGNLLDFLrksrvlETDPAFAIANSTASTLSsQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd07860   73 KLYLVFEFL-HQDLKKFM------DASALTGIPLPLIKSYL-FQLLQ-------GLAFCHSHRVLHRDLKPQNLLINTEG 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 830 VAKIADFGLSRGQEVYVKKTMGRLPVRWM-AIES-LNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd07860  138 AIKLADFGLARAFGVPVRTYTHEVVTLWYrAPEIlLGCKYYSTAVDIWSLGCIFAEMVT 196
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
675-935 1.73e-14

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: 75.80  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKkdGLRMDAAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLY 752
Cdd:cd05615   10 TDFNFLMVLGKGSFGKVMLAERK--GSDELYAIKILKKdvVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05615   88 FVMEYVNGGDLMYHIQQ----------------VGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSRGQ--EVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQgYRL 910
Cdd:cd05615  152 IADFGMCKEHmvEGVTTRTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME-HNV 228
                        250       260
                 ....*....|....*....|....*
gi 759191595 911 EKPLNCDDEVYDLMRQCWREKPYER 935
Cdd:cd05615  229 SYPKSLSKEAVSICKGLMTKHPAKR 253
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
675-883 2.03e-14

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 75.43  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINLLG-ACEH----- 747
Cdd:cd07866    8 RDYEILGKLGEGTFGEVYKARQIKTGRVV--ALKKILMHNEKDGFPITAlREIKILKKL-KHPNVVPLIDmAVERpdksk 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 --RGYLYLAIEYAPHgNLLDFLRKSRVLETDPAFaianstasTLSSQQLLHfaadvarGMDYLSQKQFIHRDLAARNILV 825
Cdd:cd07866   85 rkRGSVYMVTPYMDH-DLSGLLENPSVKLTESQI--------KCYMLQLLE-------GINYLHENHILHRDIKAANILI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 826 GENYVAKIADFGLSRGQEVYVKKTMGRLPV-----------RWM-AIE-SLNYSVYTTNSDVWSYGVLLWE 883
Cdd:cd07866  149 DNQGILKIADFGLARPYDGPPPNPKGGGGGgtrkytnlvvtRWYrPPElLLGERRYTTAVDIWGIGCVFAE 219
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
682-943 2.42e-14

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: 74.39  E-value: 2.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAG----ELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd06630    7 LLGTGAFSSCYQARDVKTGTLM--AVKQVSFcRNSSSEQEEVVEaireEIRMMARL-NHPNIVRMLGATQHKSHFNIFVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLldflrkSRVLETDPAFAIANSTASTLssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILV-GENYVAKIAD 835
Cdd:cd06630   84 WMAGGSV------ASLLSKYGAFSENVIINYTL---QIL-------RGLAYLHDNQIIHRDLKGANLLVdSTGQRLRIAD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLS---RGQEVYVKKTMGRL--PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY----------------CG 894
Cdd:cd06630  148 FGAAarlASKGTGAGEFQGQLlgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPWnaekisnhlalifkiaSA 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 895 MTCAELYEKLPQGYRlekplncddevyDLMRQCWREKPYERPSFAQILV 943
Cdd:cd06630  227 TTPPPIPEHLSPGLR------------DVTLRCLELQPEDRPPARELLK 263
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
680-903 2.55e-14

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: 74.27  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDgLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14201   11 KDLVGHGAFAVVFKGRHRKK-TDWEVAIKSINKKNLSKSQILLGKEIKILKEL-QHENIVALYDVQEMPNSVFLVMEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVgeNYVA-------- 831
Cdd:cd14201   89 GGDLADYLQ----------------AKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILL--SYASrkkssvsg 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 832 ---KIADFGLSRG-QEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAEL---YEK 903
Cdd:cd14201  151 iriKIADFGFARYlQSNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDLrmfYEK 227
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
683-946 2.65e-14

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: 74.23  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVL-KAR------------IKKDGLRMD-AAIKRMKEYASKDDHR---DFAGELEVLCKLgHHPNIINLLGAC 745
Cdd:cd14067    1 LGQGGSGTVIyRARyqgqpvavkrfhIKKCKKRTDgSADTMLKHLRAADAMKnfsEFRQEASMLHSL-QHPCIVYLIGIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRgyLYLAIEYAPHGNLldflrkSRVLETDPAfaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 825
Cdd:cd14067   80 IHP--LCFALELAPLGSL------NTVLEENHK----GSSFMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 -----GENYVAKIADFGLSRGQ----EVYVKKTMGrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMT 896
Cdd:cd14067  148 wsldvQEHINIKLSDYGISRQSfhegALGVEGTPG-----YQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHH 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 897 CAELYEKLPQGYR--LEKPlncdDEV-----YDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd14067  222 QLQIAKKLSKGIRpvLGQP----EEVqffrlQALMMECWDTKPEKRPLACSVVEQMK 274
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
675-904 3.15e-14

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: 75.04  E-value: 3.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGlrmDA-AIKRMK--EYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYL 751
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATG---DIyAMKVLKksETLAQEEVSFFEEERDIMAK-ANSPWITKLQYAFQDSENL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFL-RKSRVLETDPA-FaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd05601   77 YLVMEYHPGGDLLSLLsRYDDIFEESMArF-----------------YLAELVLAIHSLHSMGYVHRDIKPENILIDRTG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFG----LSRGQEVYVKktmgrLPV---RWMAIE---SLNY---SVYTTNSDVWSYGVLLWEIVsLGGTPYCGMT 896
Cdd:cd05601  140 HIKLADFGsaakLSSDKTVTSK-----MPVgtpDYIAPEvltSMNGgskGTYGVECDWWSLGIVAYEML-YGKTPFTEDT 213

                 ....*...
gi 759191595 897 CAELYEKL 904
Cdd:cd05601  214 VIKTYSNI 221
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
682-963 3.25e-14

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: 74.60  E-value: 3.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05620    2 VLGKGSFGKVLLAELKGKGEYF--AVKALKKdvVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLR-KSRvletdpaFAIANSTastlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05620   80 GGDLMFHIQdKGR-------FDLYRAT----------FYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGM 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRgQEVYVKK---TMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLpqgyRLEKPLN 915
Cdd:cd05620  143 CK-ENVFGDNrasTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESI----RVDTPHY 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 916 ---CDDEVYDLMrqcwrEKPYERPSFAQILVSLNRMLEERKTYVNTTLYEK 963
Cdd:cd05620  216 prwITKESKDIL-----EKLFERDPTRRLGVVGNIRGHPFFKTINWTALEK 261
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
683-942 3.30e-14

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 73.82  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGqVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14197   17 LGRGKFA-VVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGGE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDflrkSRVLETDPAFaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV---AKIADFGLS 839
Cdd:cd14197   96 IFN----QCVADREEAF----------KEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlgdIKIVDFGLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 R--GQEVYVKKTMGRlPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQ---GYRLEKPL 914
Cdd:cd14197  162 RilKNSEELREIMGT-P-EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDDKQETFLNISQmnvSYSEEEFE 238
                        250       260
                 ....*....|....*....|....*...
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14197  239 HLSESAIDFIKTLLIKKPENRATAEDCL 266
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
719-945 3.36e-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: 73.79  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 719 HRDFA---GELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRV-LETDPAFAIANSTASTLSsqql 794
Cdd:cd05076   55 HHDIAlafFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKGhVPMAWKFVVARQLASALS---- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 795 lhfaadvargmdYLSQKQFIHRDLAARNILV-------GENYVAKIADFG-----LSRGQEVYvkktmgRLPvrWMAIES 862
Cdd:cd05076  131 ------------YLENKNLVHGNVCAKNILLarlgleeGTSPFIKLSDPGvglgvLSREERVE------RIP--WIAPEC 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 863 L-NYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPlNCdDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd05076  191 VpGGNSLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLPEP-SC-PELATLISQCLTYEPTQRPSFRTI 268

                 ....
gi 759191595 942 LVSL 945
Cdd:cd05076  269 LRDL 272
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
725-948 3.44e-14

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: 73.77  E-value: 3.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 725 ELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPHGNLLDFLrKSRVLETDPAFAIANSTASTLSsqqllhfaaDVARG 804
Cdd:cd14044   53 ELNKLLQIDYY-NLTKFYGTVKLDTMIFGVIEYCERGSLRDVL-NDKISYPDGTFMDWEFKISVMY---------DIAKG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 805 MDYL-SQKQFIHRDLAARNILVGENYVAKIADFGlsrGQEVyvkktmgrLPVR---WMAIESLNYSVYTTNSDVWSYGVL 880
Cdd:cd14044  122 MSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFG---CNSI--------LPPSkdlWTAPEHLRQAGTSQKGDVYSYGII 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 881 LWEIVSLGGTPYCgMTCAELYEKLpqgYRLEKP---------LNCDD------EVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:cd14044  191 AQEIILRKETFYT-AACSDRKEKI---YRVQNPkgmkpfrpdLNLESagererEVYGLVKNCWEEDPEKRPDFKKIENTL 266

                 ...
gi 759191595 946 NRM 948
Cdd:cd14044  267 AKI 269
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
682-942 3.55e-14

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


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 73.57  E-value: 3.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKD---DHRDFAG---ELEVLCKLGH--HPNIINLLGACEHRGYLY 752
Cdd:cd14004    7 EMGEGAYGQVNLAIYKSKGKEV--VIKFIfKERILVDtwvRDRKLGTvplEIHILDTLNKrsHPNIVKLLDFFEDDEFYY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEyaPHGN---LLDFL-RKSRVLETDpafaianstASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd14004   85 LVME--KHGSgmdLFDFIeRKPNMDEKE---------AKYIFRQ--------VADAVKHLHDQGIVHRDIKDENVILDGN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFG----LSRGQEVYVKKTMGrlpvrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVsLGGTPYCgmtcaELYEK 903
Cdd:cd14004  146 GTIKLIDFGsaayIKSGPFDTFVGTID-----YAAPEVLRGNPYGgKEQDIWALGVLLYTLV-FKENPFY-----NIEEI 214
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 904 LPQGYRLEKPLNcdDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14004  215 LEADLRIPYAVS--EDLIDLISRMLNRDVGDRPTIEELL 251
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
662-942 3.77e-14

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: 73.89  E-value: 3.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 662 NNPDPTIypvlDWNDIkfqDVIGEGNFGQVLKARIKKDGLRmdAAIKRMKEYASKDDhrDFAGELEVLCKLGHHPNIINL 741
Cdd:cd06638   12 SFPDPSD----TWEII---ETIGKGTYGKVFKVLNKKNGSK--AAVKILDPIHDIDE--EIEAEYNILKALSDHPNVVKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 742 LGACEHRGY-----LYLAIEYAPHGNLLD----FLRKSRVLEtDPAFAIanstastlssqqLLHfaaDVARGMDYLSQKQ 812
Cdd:cd06638   81 YGMYYKKDVkngdqLWLVLELCNGGSVTDlvkgFLKRGERME-EPIIAY------------ILH---EALMGLQHLHVNK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 813 FIHRDLAARNILVGENYVAKIADFGLS-RGQEVYVKKTMGRLPVRWMAIESLNY-----SVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd06638  145 TIHRDVKGNNILLTTEGGVKLVDFGVSaQLTSTRLRRNTSVGTPFWMAPEVIACeqqldSTYDARCDVWSLGITAIELGD 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 887 lGGTPYCGMTCAELYEKLPQG--YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd06638  225 -GDPPLADLHPMRALFKIPRNppPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLL 281
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
682-902 3.89e-14

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 74.56  E-value: 3.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05590    2 VLGKGSFGKVMLARLKESGRLY--AVKVLKKdvILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05590   80 GGDLMFHIQKSRRFDEARA----------------RFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 840 RgQEVYVKKTMGRL--PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYE 902
Cdd:cd05590  144 K-EGIFNGKTTSTFcgTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFE 206
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
683-942 4.49e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 74.86  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMkeYASKDD--HRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLY--ALKVI--YGNHEDtvRRQICREIEIL-RDVNHPNVVKCHDMFDHNGEIQVLLEFMDG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLldflrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:PLN00034 157 GSL--------------------EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSR 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 gqevYVKKTMGrlP-------VRWMAIESLN-------YSVYTtnSDVWSYGVLLWEIVsLGGTPY--------CGMTCA 898
Cdd:PLN00034 217 ----ILAQTMD--PcnssvgtIAYMSPERINtdlnhgaYDGYA--GDIWSLGVSILEFY-LGRFPFgvgrqgdwASLMCA 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 759191595 899 ELYEKLPqgyrlEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:PLN00034 288 ICMSQPP-----EAPATASREFRHFISCCLQREPAKRWSAMQLL 326
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
681-884 4.50e-14

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 74.07  E-value: 4.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINL----------LGACEHRG 749
Cdd:cd07864   13 GIIGEGTYGQVYKAKDKDTGELV--ALKKVRLDNEKEGFPITAiREIKILRQL-NHRSVVNLkeivtdkqdaLDFKKDKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHgNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd07864   90 AFYLVFEYMDH-DLMGLLESGLV---------------HFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 830 VAKIADFGLSR-----GQEVYVKK--TMGRLPVRWMaiesLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd07864  154 QIKLADFGLARlynseESRPYTNKviTLWYRPPELL----LGEERYGPAIDVWSCGCILGEL 211
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
683-886 4.62e-14

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 73.80  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKeyasKDDHRD-FA----GELEVLCKLgHHPNIINL----LGACEHRgyLYL 753
Cdd:cd07843   13 IEEGTYGVVYRARDKKTG--EIVALKKLK----MEKEKEgFPitslREINILLKL-QHPNIVTVkevvVGSNLDK--IYM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHgnllDFlrKSrVLET-DPAFAIanSTASTLSsQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd07843   84 VMEYVEH----DL--KS-LMETmKQPFLQ--SEVKCLM-LQLL-------SGVAHLHDNWILHRDLKTSNLLLNNRGILK 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 833 IADFGLSRGQEVyVKKTMGRLPVR-WM-AIESL-NYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd07843  147 ICDFGLAREYGS-PLKPYTQLVVTlWYrAPELLlGAKEYSTAIDMWSVGCIFAELLT 202
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
678-894 4.95e-14

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 74.26  E-value: 4.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKeyasKDD--HRDfagELEVL-CK--------LGHHPNIINLLGACE 746
Cdd:cd05589    2 RCIAVLGRGHFGKVLLAEYKPTGELF--AIKALK----KGDiiARD---EVESLmCEkrifetvnSARHPFLVNLFACFQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 747 HRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILV- 825
Cdd:cd05589   73 TPEHVCFVMEYAAGGDLMMHIHEDVFSEPRAVF-----------------YAACVVLGLQFLHEHKIVYRDLKLDNLLLd 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 826 GENYVaKIADFGLsrgqevyVKKTMGR---------LPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCG 894
Cdd:cd05589  136 TEGYV-KIADFGL-------CKEGMGFgdrtstfcgTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPG 203
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
682-882 5.89e-14

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: 72.74  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14095    7 VIGDGNFAVVKECRDKATDKEY--ALKIIDKAKCKGKEHMIENEVAILRRV-KHPNIVQLIEEYDTDTELYLVMELVKGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKS-RVLETDPAFAIanstastlssqqllhfaADVARGMDYLSQKQFIHRDLAARNILVGENYVA----KIADF 836
Cdd:cd14095   84 DLFDAITSStKFTERDASRMV-----------------TDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGskslKLADF 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 837 GLSrgqeVYVKK---TMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLW 882
Cdd:cd14095  147 GLA----TEVKEplfTVCGTPT-YVAPEILAETGYGLKVDIWAAGVITY 190
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
682-935 5.91e-14

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: 73.98  E-value: 5.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARiKKDGLRMDA--AIKRMKEYASKDDHRDFA---GELEVLCKLgHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd05584    3 VLGKGGYGKVFQVR-KTTGSDKGKifAMKVLKKASIVRNQKDTAhtkAERNILEAV-KHPFIVDLHYAFQTGGKLYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVLETDpafaiansTAStlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd05584   81 YLSGGELFMHLEREGIFMED--------TAC--------FYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLS--RGQEVYVKKTM-GrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKP 913
Cdd:cd05584  145 GLCkeSIHDGTVTHTFcG--TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKTIDKILKG-KLNLP 220
                        250       260
                 ....*....|....*....|..
gi 759191595 914 LNCDDEVYDLMRQCWREKPYER 935
Cdd:cd05584  221 PYLTNEARDLLKKLLKRNVSSR 242
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
703-891 5.98e-14

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 73.16  E-value: 5.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 703 MDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLrKSRVletdpafaia 782
Cdd:cd14093   36 IDITGEKSSENEAEELREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFELCRKGELFDYL-TEVV---------- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 783 nstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG----LSRGQEVY-VKKTMGrlpvrW 857
Cdd:cd14093  105 -----TLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGfatrLDEGEKLReLCGTPG-----Y 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 759191595 858 MAIESLNYSV------YTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd14093  175 LAPEVLKCSMydnapgYGKEVDMWACGVIMYTL--LAGCP 212
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
682-886 6.06e-14

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: 73.57  E-value: 6.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKD--GLRMDAAIK--RMKEYASKDDHRDFAGELEVlcklgHHPNIINLLGACEHRGYL----YL 753
Cdd:cd14055    2 LVGKGRFAEVWKAKLKQNasGQYETVAVKifPYEEYASWKNEKDIFTDASL-----KHENILQFLTAEERGVGLdrqyWL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSrvletdpafaianstasTLSSQQLLHFAADVARGMDYL--------SQKQFI-HRDLAARNIL 824
Cdd:cd14055   77 ITAYHENGSLQDYLTRH-----------------ILSWEDLCKMAGSLARGLAHLhsdrtpcgRPKIPIaHRDLKSSNIL 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 825 VGENYVAKIADFGLSRGQEVYVK----KTMGRL-PVRWMAIESLNYSVYTTN------SDVWSYGVLLWEIVS 886
Cdd:cd14055  140 VKNDGTCVLADFGLALRLDPSLSvdelANSGQVgTARYMAPEALESRVNLEDlesfkqIDVYSMALVLWEMAS 212
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
681-892 6.48e-14

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: 73.04  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd06647   13 EKIGQGASGTVYTAIDVATG--QEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd06647   89 GSLTDVV-----------------TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759191595 841 --GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06647  152 qiTPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 203
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
677-948 6.88e-14

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: 73.09  E-value: 6.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGLRmdAAIKRMkeyASKDDH--RDFAGELEVLCKLGHHPNIINLL---------GAC 745
Cdd:cd14037    5 VTIEKYLAEGGFAHVYLVKTSNGGNR--AALKRV---YVNDEHdlNVCKREIEIMKRLSGHKNIVGYIdssanrsgnGVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EhrgyLYLAIEYAPHGNLLDFLrksrvletdpafaiaNSTAST-LSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARN 822
Cdd:cd14037   80 E----VLLLMEYCKGGGVIDLM---------------NQRLQTgLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVEN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 823 ILVGENYVAKIADFGLSRG---------------QEVYVKKTMG-RLPvrwmaiESLN-YS--VYTTNSDVWSYGVLLWE 883
Cdd:cd14037  141 VLISDSGNYKLCDFGSATTkilppqtkqgvtyveEDIKKYTTLQyRAP------EMIDlYRgkPITEKSDIWALGCLLYK 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 884 IVSLgGTPYcGMT-----CAELYEkLPQGYRLEKPLNCddevydLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14037  215 LCFY-TTPF-EESgqlaiLNGNFT-FPDNSRYSKRLHK------LIRYMLEEDPEKRPNIYQVSYEAFEL 275
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
682-935 7.15e-14

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: 73.89  E-value: 7.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd05595    2 LLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVL-QNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd05595   81 ELFFHLSRERVFTEDRA----------------RFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 842 --QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEK-LPQGYRLekPLNCDD 918
Cdd:cd05595  145 giTDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELiLMEEIRF--PRTLSP 220
                        250
                 ....*....|....*..
gi 759191595 919 EVYDLMRQCWREKPYER 935
Cdd:cd05595  221 EAKSLLAGLLKKDPKQR 237
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
682-902 7.99e-14

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: 73.57  E-value: 7.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05592    2 VLGKGSFGKVMLAELKGTNQYF--AIKALKKdvVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLdflrksrvletdpaFAIANSTASTLSSQQLlhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05592   80 GGDLM--------------FHIQQSGRFDEDRARF--YGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 840 RgQEVYVKKTMGRL---PvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYE 902
Cdd:cd05592  144 K-ENIYGENKASTFcgtP-DYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPFHGEDEDELFW 206
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
681-941 1.01e-13

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: 72.53  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDG--------LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLY 752
Cdd:cd08528    6 ELLGSGAFGCVYKVRKKSNGqtllalkeINMTNPAFGRTEQERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLENDRLY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LA---IEYAPHGNLLDFLRksrvlETDPAFaianstastlSSQQLLHFAADVARGMDYL-SQKQFIHRDLAARNILVGEN 828
Cdd:cd08528   86 IVmelIEGAPLGEHFSSLK-----EKNEHF----------TEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGED 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGLSRGQ---EVYVKKTMGRLpVRWMAiESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPY--CGMTCAE---- 899
Cdd:cd08528  151 DKVTITDFGLAKQKgpeSSKMTSVVGTI-LYSCP-EIVQNEPYGEKADIWALGCILYQMCTLQPPFYstNMLTLATkive 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 900 -LYEKLPQGYRlekplncDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd08528  229 aEYEPLPEGMY-------SDDITFVIRSCLTPDPEARPDIVEV 264
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
675-902 1.11e-13

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: 73.58  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd05593   15 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETDpafaianstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd05593   94 MEYVNGGELFFHLSRERVFSED----------------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYE 902
Cdd:cd05593  158 DFGLCKEgiTDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 225
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
677-949 1.26e-13

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: 72.86  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGLRMdaaikrmKEYASKDDhRDFAGELEVLCK-LGHHPNIINLLGA-------CEHr 748
Cdd:cd14142    7 ITLVECIGKGRYGEVWRGQWQGESVAV-------KIFSSRDE-KSWFRETEIYNTvLLRHENILGFIASdmtsrnsCTQ- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 gyLYLAIEYAPHGNLLDFLRKSrvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQF--------IHRDLAA 820
Cdd:cd14142   78 --LWLITHYHENGSLYDYLQRT-----------------TLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 821 RNILVGENYVAKIADFGLSrgqeVYVKKTMGRLPV---------RWMAIESLNYSVYTT------NSDVWSYGVLLWEIV 885
Cdd:cd14142  139 KNILVKSNGQCCIADLGLA----VTHSQETNQLDVgnnprvgtkRYMAPEVLDETINTDcfesykRVDIYAFGLVLWEVA 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 886 SLggTPYCGMtcAE-----LYEKLPQGYRLE--KPLNCDDE-----------------VYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14142  215 RR--CVSGGI--VEeykppFYDVVPSDPSFEdmRKVVCVDQqrpnipnrwssdptltaMAKLMKECWYQNPSARLTALRI 290

                 ....*...
gi 759191595 942 LVSLNRML 949
Cdd:cd14142  291 KKTLLKIL 298
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
683-948 1.46e-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: 72.12  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglrmDAAIKRM--KEYASkddhrdFAGELEVL-CKLGHHPNIINLLgACEHRG-----YLYLA 754
Cdd:cd14144    3 VGKGRYGEVWKGKWRGE----KVAVKIFftTEEAS------WFRETEIYqTVLMRHENILGFI-AADIKGtgswtQLYLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQF--------IHRDLAARNILVG 826
Cdd:cd14144   72 TDYHENGSLYDFLR-----------------GNTLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 827 ENYVAKIADFGL-----SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTN------SDVWSYGVLLWEIVS---LGGT-- 890
Cdd:cd14144  135 KNGTCCIADLGLavkfiSETNEVDLPPNTRVGTKRYMAPEVLDESLNRNHfdaykmADMYSFGLVLWEIARrciSGGIve 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 891 ----PYCGMTCAE-LYEKLPQGYRLEK--P-----LNCDD---EVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14144  215 eyqlPYYDAVPSDpSYEDMRRVVCVERrrPsipnrWSSDEvlrTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
725-942 1.56e-13

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: 71.58  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 725 ELEvLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLeTDPafaianstastlssqQLLHFAADVARG 804
Cdd:cd14188   51 EIE-LHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVL-TEP---------------EVRYYLRQIVSG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 805 MDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEV--YVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLW 882
Cdd:cd14188  114 LKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPleHRRRTICGTP-NYLSPEVLNKQGHGCESDIWALGCVMY 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 883 EIVsLGGTPYCGMTCAELYEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14188  193 TML-LGRPPFETTNLKETYRCIREA-RYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEII 250
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
683-942 1.57e-13

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 71.96  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAA-IKRMKEYASKD--DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKfIKKRRLSSSRRgvSREEIEREVNILREI-QHPNIITLHDIFENKTDVVLILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA----KIAD 835
Cdd:cd14195   92 GGELFDFL----------------AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPnpriKLID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR----GQEVyvkKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQ-GYRL 910
Cdd:cd14195  156 FGIAHkieaGNEF---KNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGETKQETLTNISAvNYDF 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 911 EKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14195  231 DEEYfsNTSELAKDFIRRLLVKDPKKRMTIAQSL 264
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
681-944 1.87e-13

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: 71.74  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHH--PNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd06917    7 ELVGRGSYGAVYRGYHVKTGRVV--ALKVLNLDTDDDDVSDIQKEVALLSQLKLGqpKNIIKYYGSYLKGPSLWIIMDYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRksrvletdpAFAIANSTASTLSSQQLLhfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd06917   85 EGGSIRTLMR---------AGPIAERYIAVIMREVLV--------ALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 --SRGQEVYVKKTMGRLPVrWMAIESLNYSV-YTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQgyrlEKPLN 915
Cdd:cd06917  148 aaSLNQNSSKRSTFVGTPY-WMAPEVITEGKyYDTKADIWSLGITTYEMAT-GNPPYSDVDALRAVMLIPK----SKPPR 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 759191595 916 CDDEVYD-LMRQ----CWREKPYERPSFAQILVS 944
Cdd:cd06917  222 LEGNGYSpLLKEfvaaCLDEEPKDRLSADELLKS 255
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
648-942 1.97e-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: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 648 QFNSGTLALnrkaKNNPDPTIypvlDWNDIkfqDVIGEGNFGQVLKARIKKDGLRmdAAIKRMKEYASKDDhrDFAGELE 727
Cdd:cd06639    6 PYNSSMLGL----ESLADPSD----TWDII---ETIGKGTYGKVYKVTNKKDGSL--AAVKILDPISDVDE--EIEAEYN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 728 VLCKLGHHPNIINLLG---ACEHR--GYLYLAIEYAPHGNLLDFLRK-----SRVLETDPAFAIANStastlssqqLLhf 797
Cdd:cd06639   71 ILRSLPNHPNVVKFYGmfyKADQYvgGQLWLVLELCNGGSVTELVKGllkcgQRLDEAMISYILYGA---------LL-- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 798 aadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSrgqevyVKKTMGRL--------PVrWMAIESL------ 863
Cdd:cd06639  140 ------GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS------AQLTSARLrrntsvgtPF-WMAPEVIaceqqy 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 864 NYSvYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG--YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd06639  207 DYS-YDARCDVWSLGITAIELAD-GDPPLFDMHPVKALFKIPRNppPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHL 284

                 .
gi 759191595 942 L 942
Cdd:cd06639  285 L 285
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
683-891 2.27e-13

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: 72.71  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAGELEVLcKLGHHPNIINLLGAcehrgylylaieYAPHG 761
Cdd:cd07851   23 VGSGAYGQVCSAFDTKTGRKV--AIKKLSRpFQSAIHAKRTYRELRLL-KHMKHENVIGLLDV------------FTPAS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFlrkSRV-LETDPAFAIANSTAST--LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd07851   88 SLEDF---QDVyLVTHLMGADLNNIVKCqkLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGL 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 839 SRGQEvyvKKTMGRLPVRW-MAIE-SLNYSVYTTNSDVWSYGVLLWE-------------------IVSLGGTP 891
Cdd:cd07851  165 ARHTD---DEMTGYVATRWyRAPEiMLNWMHYNQTVDIWSVGCIMAElltgktlfpgsdhidqlkrIMNLVGTP 235
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
712-942 2.38e-13

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: 71.97  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 712 EYASK---DDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTAST 788
Cdd:cd14177   31 EFAVKiidKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 789 LssqqllhfaadvargmDYLSQKQFIHRDLAARNILVGENYVA----KIADFGLSRgqevYVKKTMGRL-----PVRWMA 859
Cdd:cd14177  111 V----------------DYLHCQGVVHRDLKPSNILYMDDSANadsiRICDFGFAK----QLRGENGLLltpcyTANFVA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 860 IESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM---TCAELYEKLPQGYRLEKPLNCD---DEVYDLMRQCWREKPY 933
Cdd:cd14177  171 PEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFANGpndTPEEILLRIGSGKFSLSGGNWDtvsDAAKDLLSHMLHVDPH 249

                 ....*....
gi 759191595 934 ERPSFAQIL 942
Cdd:cd14177  250 QRYTAEQVL 258
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
654-907 2.95e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 72.32  E-value: 2.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 654 LALNRK--AKNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRmDAAIKRM-KEYASKDDHRDFAGELEVLC 730
Cdd:PTZ00426   7 LQLHKKkdSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDFP-PVAIKRFeKSKIIKQKQVDHVFSERKIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 731 KLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQ 810
Cdd:PTZ00426  86 NYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVG----------------CFYAAQIVLIFEYLQS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 811 KQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGT 890
Cdd:PTZ00426 150 LNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYTLCG--TPEYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCP 226
                        250
                 ....*....|....*..
gi 759191595 891 PYCGMTCAELYEKLPQG 907
Cdd:PTZ00426 227 PFYANEPLLIYQKILEG 243
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
678-941 3.02e-13

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: 70.66  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDF-AGELEVLCKLgHHPNIINLLGACE-HRGYLYLA 754
Cdd:cd14164    3 TLGTTIGEGSFSKVKLATSQKYCCKV--AIKIVdRRRASPDFVQKFlPRELSILRRV-NHPNIVQMFECIEvANGRLYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHgNLLDFLRKSRVLETDpafaiansTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV-GENYVAKI 833
Cdd:cd14164   80 MEAAAT-DLLQKIQEVHHIPKD--------LARDMFAQ--------MVGAVNYLHDMNIVHRDLKCENILLsADDRKIKI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTMGRLPVR-WMAIESLNYSVYTTNS-DVWSYGVLLWEIVSlGGTPYCGMTCAELYEK-----LPQ 906
Cdd:cd14164  143 ADFGFARFVEDYPELSTTFCGSRaYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFDETNVRRLRLQqrgvlYPS 221
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 907 GYRLEKPLNCddevydLMRQCWREKPYERPSFAQI 941
Cdd:cd14164  222 GVALEEPCRA------LIRTLLQFNPSTRPSIQQV 250
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
683-892 3.96e-13

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 71.10  E-value: 3.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRdFAGELEVLCKLgHHPNIINLLGACEHRGYL-----YLAIE 756
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKI--AIKSCRlELSVKNKDR-WCHEIQIMKKL-NHPNVVKACDVPEEMNFLvndvpLLAME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL---VGENYVAKI 833
Cdd:cd14039   77 YCSGGDLRKLLNKPE-------------NCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVlqeINGKIVHKI 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 834 ADFGLSR--GQEVYVKKTMGRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd14039  144 IDLGYAKdlDQGSLCTSFVGTL--QYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPF 201
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
683-892 4.51e-13

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: 70.84  E-value: 4.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQV--AVKKMD--LRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRvletdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd06658  106 LTDIVTHTR-----------------MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAqv 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 841 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06658  169 SKEVPKRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPY 218
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
683-948 4.81e-13

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: 70.84  E-value: 4.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKkdGLRMDAAIKRMKEYASkddhrdFAGELEVL-CKLGHHPNIINLLGAcEHRG-----YLYLAIE 756
Cdd:cd14220    3 IGKGRYGEVWMGKWR--GEKVAVKVFFTTEEAS------WFRETEIYqTVLMRHENILGFIAA-DIKGtgswtQLYLITD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQF--------IHRDLAARNILVGEN 828
Cdd:cd14220   74 YHENGSLYDFLK-----------------CTTLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 829 YVAKIADFGL-----SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTN------SDVWSYGVLLWEIVS---LGGT---- 890
Cdd:cd14220  137 GTCCIADLGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHfqayimADIYSFGLIIWEMARrcvTGGIveey 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 891 --PYCGMTCAE-LYEKLPQGYRLE--KPL--------NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14220  217 qlPYYDMVPSDpSYEDMREVVCVKrlRPTvsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
679-907 4.87e-13

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: 70.27  E-value: 4.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14097    5 FGRKLGQGSFGVVIEATHKETQTKW--AIKKInREKAGSSAVKLLEREVDILKHV-NHAHIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLETDPAFAIANSTASTLssqqllhfaadvargmDYLSQKQFIHRDLAARNILVGENYV------- 830
Cdd:cd14097   82 CEDGELKELLLRKGFFSENETRHIIQSLASAV----------------AYLHKNDIVHRDLKLENILVKSSIIdnndkln 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLS----RGQEVYVKKTMGRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQ 906
Cdd:cd14097  146 IKVTDFGLSvqkyGLGEDMLQETCGTP--IYMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRK 222

                 .
gi 759191595 907 G 907
Cdd:cd14097  223 G 223
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
734-925 6.39e-13

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


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 70.51  E-value: 6.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 734 HHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQF 813
Cdd:cd14209   59 NFPFLVKLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIG----------------RFSEPHARFYAAQIVLAFEYLHSLDL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 814 IHRDLAARNILVGENYVAKIADFGlsrgqevYVKKTMGR------LPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSl 887
Cdd:cd14209  123 IYRDLKPENLLIDQQGYIKVTDFG-------FAKRVKGRtwtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA- 193
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 759191595 888 GGTPYCGMTCAELYEKLPQGyRLEKPLNCDDEVYDLMR 925
Cdd:cd14209  194 GYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLR 230
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
683-942 7.34e-13

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: 70.48  E-value: 7.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRM-----KEYASKDDHRdfagELEVLCKLgHHPNIINLLGAC--------EHRG 749
Cdd:cd07865   20 IGQGTFGEVFKARHRKTGQIV--ALKKVlmeneKEGFPITALR----EIKILQLL-KHENVVNLIEICrtkatpynRYKG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHgNLLDFLRKSRVletdpAFaianstasTLSS-----QQLLHfaadvarGMDYLSQKQFIHRDLAARNIL 824
Cdd:cd07865   93 SIYLVFEFCEH-DLAGLLSNKNV-----KF--------TLSEikkvmKMLLN-------GLYYIHRNKILHRDMKAANIL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 825 VGENYVAKIADFGLSRgqeVYVKKTMGRLPVRWMAIESLNYSV---------YTTNSDVWSYGVLLWE------------ 883
Cdd:cd07865  152 ITKDGVLKLADFGLAR---AFSLAKNSQPNRYTNRVVTLWYRPpelllgerdYGPPIDMWGAGCIMAEmwtrspimqgnt 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 884 -------IVSLGG--TP--YCGMTCAELYEK--LPQGY------RLeKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07865  229 eqhqltlISQLCGsiTPevWPGVDKLELFKKmeLPQGQkrkvkeRL-KPYVKDPYALDLIDKLLVLDPAKRIDADTAL 305
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
674-891 8.26e-13

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: 70.51  E-value: 8.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 674 WNDIKFqdvIGEGNFGQVLKARIKKDGLRMDAAIKRM-----KEYASKDDHRdfagELEVLCKLGHHPNIINL--LGACE 746
Cdd:cd07857    2 YELIKE---LGQGAYGIVCSARNAETSEEETVAIKKItnvfsKKILAKRALR----ELKLLRHFRGHKNITCLydMDIVF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 747 HRGY--LYLAIEyaphgnlldflrksrVLETDPAFAIAnstastlSSQQL--LHFAA---DVARGMDYLSQKQFIHRDLA 819
Cdd:cd07857   75 PGNFneLYLYEE---------------LMEADLHQIIR-------SGQPLtdAHFQSfiyQILCGLKYIHSANVLHRDLK 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 820 ARNILVGENYVAKIADFGLSRGQEVYVKKTMGRL----PVRWM-AIE-SLNYSVYTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd07857  133 PGNLLVNADCELKICDFGLARGFSENPGENAGFMteyvATRWYrAPEiMLSFQSYTKAIDVWSVGCILAEL--LGRKP 208
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
678-942 9.52e-13

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: 69.63  E-value: 9.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGlRMdAAIKRMKeYASKDDHRDFAGELEVlCKLGHHPNIINLLGAC-------EHRGY 750
Cdd:cd13986    3 RIQRLLGEGGFSFVYLVEDLSTG-RL-YALKKIL-CHSKEDVKEAMREIEN-YRLFNHPNILRLLDSQivkeaggKKEVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLaiEYAPHGNLLDFLRKSRVletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQ---KQFIHRDLAARNILVGE 827
Cdd:cd13986   79 LLL--PYYKRGSLQDEIERRLV------------KGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVAKIADFGLSRGQEVYVKKTmgRLPVRWMAIESLN---------------YSVYTTNSDVWsygvllweivSLGGTPY 892
Cdd:cd13986  145 DDEPILMDLGSMNPARIEIEGR--REALALQDWAAEHctmpyrapelfdvksHCTIDEKTDIW----------SLGCTLY 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 893 CGMtcaelYEKLPQGYRLEK---------------PLNC--DDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd13986  213 ALM-----YGESPFERIFQKgdslalavlsgnysfPDNSrySEELHQLVKSMLVVNPAERPSIDDLL 274
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
681-944 1.02e-12

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: 69.84  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGA-CEH-RGYLYLAIEY 757
Cdd:cd14049   12 ARLGKGGYGKVYKVRNKLDGQYY--AIKKILiKKVTKRDCMKVLREVKVLAGL-QHPNIVGYHTAwMEHvQLMLYIQMQL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 ApHGNLLDFL----RKSRVLETDPA---FAIANSTASTLssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILV-GENY 829
Cdd:cd14049   89 C-ELSLWDWIvernKRPCEEEFKSApytPVDVDVTTKIL--QQLLE-------GVTYIHSMGIVHRDLKPRNIFLhGSDI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFGLSRG---QEVYVKKTMGRLP----------VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPycgMT 896
Cdd:cd14049  159 HVRIGDFGLACPdilQDGNDSTTMSRLNglthtsgvgtCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQPFGTE---ME 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 897 CAELYEKLPQGyRLEKPLNCDDEVY-DLMRQCWREKPYERPSFAQILVS 944
Cdd:cd14049  236 RAEVLTQLRNG-QIPKSLCKRWPVQaKYIKLLTSTEPSERPSASQLLES 283
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
680-886 1.02e-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: 70.41  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYaskdDHRDFA----GELEVLCKLgHHPNIINLLGACEHRGY----- 750
Cdd:cd07849   10 LSYIGEGAYGMVCSAVHKPTGQKV--AIKKISPF----EHQTYClrtlREIKILLRF-KHENIIGILDIQRPPTFesfkd 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAP---HgnlldflrksRVLETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 827
Cdd:cd07849   83 VYIVQELMEtdlY----------KLIKTQH-----------LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 828 NYVAKIADFGLSR---GQEVYVKKTMGRLPVRWM-AIE-SLNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd07849  142 NCDLKICDFGLARiadPEHDHTGFLTEYVATRWYrAPEiMLNSKGYTKAIDIWSVGCILAEMLS 205
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
683-892 1.04e-12

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 70.01  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQV--AVKMMD--LRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRvletdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd06659  105 LTDIVSQTR-----------------LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAqi 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 841 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06659  168 SKDVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPY 217
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
729-942 1.07e-12

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: 69.88  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 729 LCKLGHHPNIINLLGACEHRGYLYLAIEYApHGNLLDFlrkSRVLETDPAFAIANSTAStlssqqllHFAADVARGMDYL 808
Cdd:cd14094   58 ICHMLKHPHIVELLETYSSDGMLYMVFEFM-DGADLCF---EIVKRADAGFVYSEAVAS--------HYMRQILEALRYC 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 809 SQKQFIHRDLAARNILVG--ENYV-AKIADFG----LSRGQEVyvkkTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVL 880
Cdd:cd14094  126 HDNNIIHRDVKPHCVLLAskENSApVKLGGFGvaiqLGESGLV----AGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVI 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 881 LWEIVSlGGTPYCGmTCAELYEKLPQG-YRLEKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14094  202 LFILLS-GCLPFYG-TKERLFEGIIKGkYKMNPRQwsHISESAKDLVRRMLMLDPAERITVYEAL 264
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
788-942 1.20e-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: 69.19  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 788 TLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEV--YVKKTMGRLPvRWMAIESLNY 865
Cdd:cd14189   97 TLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPpeQRKKTICGTP-NYLAPEVLLR 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 866 SVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQ-GYRLekPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14189  176 QGHGPESDVWSLGCVMYTLLC-GNPPFETLDLKETYRCIKQvKYTL--PASLSLPARHLLAGILKRNPGDRLTLDQIL 250
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
676-887 1.35e-12

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: 69.30  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRmdAAIKRMKEYASKDdhRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGEL--AAIKVIKLEPGED--FAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd06645   88 EFCGGGSLQDIYH----------------VTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLAD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 836 FGLSRGQEVYVKKTMGRLPV-RWMAIESLNYSV---YTTNSDVWSYGVLLWEIVSL 887
Cdd:cd06645  152 FGVSAQITATIAKRKSFIGTpYWMAPEVAAVERkggYNQLCDIWAVGITAIELAEL 207
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
676-937 1.51e-12

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 69.14  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHhPNIINLLGACEHRGYLYLAI 755
Cdd:cd06619    2 DIQYQEILGHGNGGTVYKAYHLLTRRIL--AVKVIPLDITVELQKQIMSELEILYKCDS-PYIIGFYGAFFVENRISICT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLlDFLRKsrvletdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd06619   79 EFMDGGSL-DVYRK-------------------IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRGQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIvSLGGTPY-------CGMTCAELYE------ 902
Cdd:cd06619  139 FGVSTQLVNSIAKTYVGTNA-YMAPERISGEQYGIHSDVWSLGISFMEL-ALGRFPYpqiqknqGSLMPLQLLQcivded 216
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 903 --KLPQGYRLEKplncddeVYDLMRQCWREKPYERPS 937
Cdd:cd06619  217 ppVLPVGQFSEK-------FVHFITQCMRKQPKERPA 246
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
683-885 1.91e-12

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: 69.52  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKR-MKEYASKDDHRDFAGELEVLCKLgHHPNIINL----LGACEHrgyLYLAIEY 757
Cdd:cd07856   18 VGMGAFGLVCSARDQLTG--QNVAVKKiMKPFSTPVLAKRTYRELKLLKHL-RHENIISLsdifISPLED---IYFVTEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 AphGNLLDFLRKSRVLETdpafaianstastlssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd07856   92 L--GTDLHRLLTSRPLEK----------------QFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 838 LSRGQEV----YVKKTMGRLPvRWMaiesLNYSVYTTNSDVWSYGVLLWEIV 885
Cdd:cd07856  154 LARIQDPqmtgYVSTRYYRAP-EIM----LTWQKYDVEVDIWSAGCIFAEML 200
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
678-943 1.94e-12

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: 68.82  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKD----GLRMDAAIKRMKEY-------------ASKDDHRDFA------GELEVLCKLgH 734
Cdd:cd14200    3 KLQSEIGKGSYGVVKLAYNESDdkyyAMKVLSKKKLLKQYgfprrppprgskaAQGEQAKPLAplervyQEIAILKKL-D 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEH--RGYLYLaieyaphgnLLDFLRKSRVLETdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQ 812
Cdd:cd14200   82 HVNIVKLIEVLDDpaEDNLYM---------VFDLLRKGPVMEV--------PSDKPFSEDQARLYFRDIVLGIEYLHYQK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 813 FIHRDLAARNILVGENYVAKIADFGLS---RGQEVYVKKTMGRlPVrWMAIESLNYSVYTTNS---DVWSYGVLLWEIVs 886
Cdd:cd14200  145 IVHRDIKPSNLLLGDDGHVKIADFGVSnqfEGNDALLSSTAGT-PA-FMAPETLSDSGQSFSGkalDVWAMGVTLYCFV- 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 887 LGGTPYCGMTCAELYEKLPQgyrleKPL------NCDDEVYDLMRQCWREKPYERPSFAQILV 943
Cdd:cd14200  222 YGKCPFIDEFILALHNKIKN-----KPVefpeepEISEELKDLILKMLDKNPETRITVPEIKV 279
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
682-894 2.06e-12

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 69.19  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDD--HRDFAgELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05574    8 LLGKGDVGRVYLVRLKGTGKLF--AMKVLdKEEMIKRNkvKRVLT-EREILATL-DHPFLPTLYASFQTSTHLCFVMDYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRK--SRVLETDPA-FaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05574   84 PGGELFRLLQKqpGKRLPEEVArF-----------------YAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYT--------TNS----------------------DVWSYGVLLWEIV 885
Cdd:cd05574  147 FDLSKQSSVTPPPVRKSLRKGSRRSSVKSIEKETfvaepsarSNSfvgteeyiapevikgdghgsavDWWTLGILLYEML 226

                 ....*....
gi 759191595 886 sLGGTPYCG 894
Cdd:cd05574  227 -YGTTPFKG 234
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
683-892 2.20e-12

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: 68.98  E-value: 2.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd06656   27 IGQGASGTVYTAIDIATG--QEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd06656  103 LTDVV-----------------TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqi 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 841 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06656  166 TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 215
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
675-884 2.34e-12

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: 68.87  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDglRMDAAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKET--KEIVAIKKFKDSEENEEVKETTlRELKMLRTL-KQENIVELKEAFRRRGKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHgNLLDflrksrVLETDPAFAIANSTASTLSsqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd07848   78 VFEYVEK-NMLE------LLEEMPNGVPPEKVRSYIY--QLI-------KAIHWCHKNDIVHRDIKPENLLISHNDVLKL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 834 ADFGLSRG-QEVYVKKTMGRLPVRWM-AIESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd07848  142 CDFGFARNlSEGSNANYTEYVATRWYrSPELLLGAPYGKAVDMWSVGCILGEL 194
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
683-884 2.68e-12

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: 68.45  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDD-HRDFAGELEVLCKLGH--HPNIINLLGAC-----EHRGYLYLA 754
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFV--ALKSVRVQTNEDGlPLSTVREVALLKRLEAfdHPNIVRLMDVCatsrtDRETKVTLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHgNLLDFLRKSrvletdPAFAIANSTASTLSSQQLlhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd07863   86 FEHVDQ-DLRTYLDKV------PPPGLPAETIKDLMRQFL--------RGLDFLHANCIVHRDLKPENILVTSGGQVKLA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd07863  151 DFGLARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEM 200
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
681-942 2.71e-12

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 68.52  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFAgELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNG--KEYAVKIIEKNAGHSRSRVFR-EVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPAFAIANstastlssqqllhfaaDVARGMDYLSQKQFIHRDLAARNILV-GENYVA--KIADFG 837
Cdd:cd14174   85 GSILAHIQKRKHFNEREASRVVR----------------DIASALDFLHTKGIAHRDLKPENILCeSPDKVSpvKICDFD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRGQEVYVKKTMGRLP--------VRWMAIESLNY-----SVYTTNSDVWSYGVLLWeiVSLGGTP----YCGMTCA-- 898
Cdd:cd14174  149 LGSGVKLNSACTPITTPelttpcgsAEYMAPEVVEVftdeaTFYDKRCDLWSLGVILY--IMLSGYPpfvgHCGTDCGwd 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 899 ----------ELYEKLPQGyRLEKP----LNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14174  227 rgevcrvcqnKLFESIQEG-KYEFPdkdwSHISSEAKDLISKLLVRDAKERLSAAQVL 283
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
675-935 2.93e-12

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: 69.29  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd05594   25 NDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05594  104 MEYANGGELFFHLSRERVFSEDRA----------------RFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEK-LPQGYRL 910
Cdd:cd05594  168 TDFGLCKEgiKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELiLMEEIRF 245
                        250       260
                 ....*....|....*....|....*
gi 759191595 911 EKPLNcdDEVYDLMRQCWREKPYER 935
Cdd:cd05594  246 PRTLS--PEAKSLLSGLLKKDPKQR 268
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
695-930 2.94e-12

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: 68.70  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 695 RIKKDGLRMDAAIKRMKEYAskdDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGNLLD-FLRKSRVL 773
Cdd:cd14085   21 RCRQKGTQKPYAVKKLKKTV---DKKIVRTEIGVLLRL-SHPNIIKLKEIFETPTEISLVLELVTGGELFDrIVEKGYYS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 774 ETDPAFAIanstastlssQQLLHFAAdvargmdYLSQKQFIHRDLAARNILV---GENYVAKIADFGLSR--GQEVYVKK 848
Cdd:cd14085   97 ERDAADAV----------KQILEAVA-------YLHENGIVHRDLKPENLLYatpAPDAPLKIADFGLSKivDQQVTMKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 849 TMGRlPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYcgmtcaelYEKLPQGYRLEKPLNCDdevYDLMRQCW 928
Cdd:cd14085  160 VCGT-P-GYCAPEILRGCAYGPEVDMWSVGVITY-ILLCGFEPF--------YDERGDQYMFKRILNCD---YDFVSPWW 225

                 ..
gi 759191595 929 RE 930
Cdd:cd14085  226 DD 227
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
680-942 2.96e-12

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: 68.38  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKkdGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14169    8 KEKLGEGAFSEVVLAQER--GSQRLVALKCIPKKALRGKEAMVENEIAVLRRI-NHENIVSLEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDflrksRVLETDpafAIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVG---ENYVAKIADF 836
Cdd:cd14169   85 GGELFD-----RIIERG---SYTEKDASQLIGQ--------VLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEK-LPQGYRLEKPL- 914
Cdd:cd14169  149 GLSKIEAQGMLSTACGTPG-YVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFNQiLKAEYEFDSPYw 226
                        250       260
                 ....*....|....*....|....*....
gi 759191595 915 -NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14169  227 dDISESAKDFIRHLLERDPEKRFTCEQAL 255
fn3 pfam00041
Fibronectin type III domain;
494-578 3.49e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  494 PQPENIKISNITDSTAMISWTILDGYS--ISSIIIRYKIQGKNE-DQHIDVKiknATITQYQLKGLEPQTVYQVDIFAEN 570
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNSGEpWNEITVP---GTTTSVTLTGLKPGTEYEVRVQAVN 77

                  ....*...
gi 759191595  571 NIGSSNPT 578
Cdd:pfam00041  78 GGGEGPPS 85
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
683-886 3.50e-12

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 69.39  E-value: 3.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRmdAAIKRMKE-----YASKDDHRdfagELEVLCKLGHHpniiNLLGAcehrgylyLAIEY 757
Cdd:cd07853    8 IGYGAFGVVWSVTDPRDGKR--VALKKMPNvfqnlVSCKRVFR----ELKMLCFFKHD----NVLSA--------LDILQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHgnlLDFLRK----SRVLETDPAFAIANSTAstLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd07853   70 PPH---IDPFEEiyvvTELMQSDLHKIIVSPQP--LSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKI 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 834 ADFGLSRGQEVYVKKTMGRLPVR--WMAIESLNYSV-YTTNSDVWSYGVLLWEIVS 886
Cdd:cd07853  145 CDFGLARVEEPDESKHMTQEVVTqyYRAPEILMGSRhYTSAVDIWSVGCIFAELLG 200
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
683-942 3.61e-12

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: 68.74  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDglRMDAAIKrmKEYA----SKDDHRDFAgELEVLCKLGHHPNIINLLGAceHRGY----LYLA 754
Cdd:cd07852   15 LGKGAYGIVWKAIDKKT--GEVVALK--KIFDafrnATDAQRTFR-EIMFLQELNDHPNIIKLLNV--IRAEndkdIYLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYaphgnlldflrksrvLETDPAFAIansTASTLSSQ-------QLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGE 827
Cdd:cd07852   88 FEY---------------METDLHAVI---RANILEDIhkqyimyQLL-------KALKYLHSGGVIHRDLKPSNILLNS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVAKIADFGLSRgqEVYVKKTMGRLPV-------RWM-AIESLNYSV-YTTNSDVWSYGVLLWEIvsLGGTP------- 891
Cdd:cd07852  143 DCRVKLADFGLAR--SLSQLEEDDENPVltdyvatRWYrAPEILLGSTrYTKGVDMWSVGCILGEM--LLGKPlfpgtst 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 892 ---------YCGMTCAE------------LYEKLPQGYR---LEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07852  219 lnqlekiieVIGRPSAEdiesiqspfaatMLESLPPSRPkslDELFPKASPDALDLLKKLLVFNPNKRLTAEEAL 293
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
683-937 3.66e-12

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 68.09  E-value: 3.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDG-------LRMDA--------AIKrmkeyaskddhrdfagELEVLCKLgHHPNIINLLGA--C 745
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGeivalkkIRLETedegvpstAIR----------------EISLLKEL-NHPNIVRLLDVvhS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 746 EHRgyLYLAIEYaphgnlLDF-LRKsrVLETDPAFAIANSTASTLSSQQLlhfaadvaRGMDYLSQKQFIHRDLAARNIL 824
Cdd:cd07835   70 ENK--LYLVFEF------LDLdLKK--YMDSSPLTGLDPPLIKSYLYQLL--------QGIAFCHSHRVLHRDLKPQNLL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 825 VGENYVAKIADFGLSRGQEVyvkktmgrlPVR---------WM-AIESLNYS-VYTTNSDVWSYGVL------------- 880
Cdd:cd07835  132 IDTEGALKLADFGLARAFGV---------PVRtythevvtlWYrAPEILLGSkHYSTPVDIWSVGCIfaemvtrrplfpg 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 881 ------LWEIVSLGGTP----YCGMTCAELY-EKLPQ--GYRLEKPL-NCDDEVYDLMRQCWREKPYERPS 937
Cdd:cd07835  203 dseidqLFRIFRTLGTPdedvWPGVTSLPDYkPTFPKwaRQDLSKVVpSLDEDGLDLLSQMLVYDPAKRIS 273
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
683-892 4.00e-12

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: 68.07  E-value: 4.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYL------YLAIE 756
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQV--AIKQCRQELSPKNRERWCLEIQIMKRL-NHPNVVAARDVPEGLQKLapndlpLLAME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKsrvletdpafaIANSTAstLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV--GEN-YVAKI 833
Cdd:cd14038   79 YCQGGDLRKYLNQ-----------FENCCG--LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqGEQrLIHKI 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 834 ADFGLSR--GQEVYVKKTMGRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd14038  146 IDLGYAKelDQGSLCTSFVGTL--QYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
677-948 4.98e-12

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: 67.34  E-value: 4.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARikkdgLRMDAAIKRMkeyaskDDHRDFAGEL-----EVLC-KLGHHPNIINLLGACEHrgy 750
Cdd:cd14153    2 LEIGELIGKGRFGQVYHGR-----WHGEVAIRLI------DIERDNEEQLkafkrEVMAyRQTRHENVVLFMGACMS--- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 lylaieyAPHGNLLDFLRKSRVLetdpaFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd14153   68 -------PPHLAIITSLCKGRTL-----YSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AkIADFGL---SRGQEVYVKKTMGRLPVRWMA------IESLNYSV------YTTNSDVWSYGVLLWEIVSLgGTPYCGM 895
Cdd:cd14153  136 V-ITDFGLftiSGVLQAGRREDKLRIQSGWLChlapeiIRQLSPETeedklpFSKHSDVFAFGTIWYELHAR-EWPFKTQ 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 896 TCAELYEKLPQGYrleKP----LNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd14153  214 PAEAIIWQVGSGM---KPnlsqIGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
683-892 5.85e-12

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 67.83  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKAriKKDGLRMDAAIKRMKeyASKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd06655   27 IGQGASGTVFTA--IDVATGQEVAIKQIN--LQKQPKKELIiNEILVMKEL-KNPNIVNFLDSFLVGDELFVVMEYLAGG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR- 840
Cdd:cd06655  102 SLTDVV-----------------TETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAq 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 841 -GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06655  165 iTPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 215
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
677-946 5.89e-12

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: 67.28  E-value: 5.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDG----LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLlGACEHRGYLY 752
Cdd:cd05078    1 LIFNESLGQGTFTKIFKGIRREVGdygqLHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNY-GVCVCGDENI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV------- 825
Cdd:cd05078   80 LVQEYVKFGSLDTYLKKNK---------------NCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLireedrk 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 -GENYVAKIADFGLS---RGQEVYVKktmgRLPvrWMAIESL-NYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCA-- 898
Cdd:cd05078  145 tGNPPFIKLSDPGISitvLPKDILLE----RIP--WVPPECIeNPKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQrk 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 899 -ELYEKlpqgyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd05078  219 lQFYED-----RHQLPAPKWTELANLINNCMDYEPDHRPSFRAIIRDLN 262
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
682-921 7.07e-12

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: 67.69  E-value: 7.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFA-GELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05632    9 VLGKGGFGEVCACQVRATG-KMYACKRLEKKRIKKRKGESMAlNEKQILEKVNSQ-FVVNLAYAYETKDALCLVLTIMNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLldflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS- 839
Cdd:cd05632   87 GDL--------------KFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAv 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 ---RGQEVyvkktMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTcaelyEKLPQgYRLEKPLN 915
Cdd:cd05632  153 kipEGESI-----RGRVgTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRGRK-----EKVKR-EEVDRRVL 220

                 ....*.
gi 759191595 916 CDDEVY 921
Cdd:cd05632  221 ETEEVY 226
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
675-904 7.41e-12

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: 68.49  E-value: 7.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDglRMDAAIKRMK--EYASKDDHRDFAGELEVLCkLGHHPNIINLLGACEHRGYLY 752
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKST--RKVYAMKLLSkfEMIKRSDSAFFWEERDIMA-FANSPWVVQLFYAFQDDRYLY 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05622  150 MVMEYMPGGDLVNLMSNYDVPEKWARF-----------------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK 212
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 833 IADFG--LSRGQEVYVKKTMGRLPVRWMAIESLNYS----VYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKL 904
Cdd:cd05622  213 LADFGtcMKMNKEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML-VGDTPFYADSLVGTYSKI 289
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
682-892 7.93e-12

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 66.94  E-value: 7.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFA-GELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05631    7 VLGKGGFGEVCACQVRATG-KMYACKKLEKKRIKKRKGEAMAlNEKRILEKVNSR-FVVSLAYAYETKDALCLVLTIMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLldflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS- 839
Cdd:cd05631   85 GDL--------------KFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAv 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 840 ---RGQEVyvkktMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05631  151 qipEGETV-----RGRVgTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPF 201
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
681-899 8.58e-12

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 66.96  E-value: 8.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKkdglrMDAAIKRMKEYasKDDHRDFAG-----ELEVLCKLgHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd07871   11 DKLGEGTYATVFKGRSK-----LTENLVALKEI--RLEHEEGAPctairEVSLLKNL-KHANIVTLHDIIHTERCLTLVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYaphgnlldflrksrvLETDPAFAIANsTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd07871   83 EY---------------LDSDLKQYLDN-CGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLAD 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 836 FGLSRGQEVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVSlgGTP-YCGMTCAE 899
Cdd:cd07871  147 FGLARAKSVPTKTYSNEVVTLWYRPPDvlLGSTEYSTPIDMWGVGCILYEMAT--GRPmFPGSTVKE 211
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
683-942 8.80e-12

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: 67.37  E-value: 8.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARikKDGLRMDAAIKRMkEYASKDDH---RDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAp 759
Cdd:cd06633   29 IGHGSFGAVYFAT--NSHTNEVVAIKKM-SYSGKQTNekwQDIIKEVKFLQQL-KHPNTIEYKGCYLKDHTAWLVMEYC- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLR--KSRVLETDpafaIANSTASTLssqqllhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd06633  104 LGSASDLLEvhKKPLQEVE----IAAITHGAL-------------QGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 lSRGQEVYVKKTMGRlPVrWMAIE---SLNYSVYTTNSDVWSYGVllweivslggtpycgmTCAELYEKLPQGYRL---- 910
Cdd:cd06633  167 -SASIASPANSFVGT-PY-WMAPEvilAMDEGQYDGKVDIWSLGI----------------TCIELAERKPPLFNMnams 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 759191595 911 --------EKPLNCDDEVYDLMRQ----CWREKPYERPSFAQIL 942
Cdd:cd06633  228 alyhiaqnDSPTLQSNEWTDSFRGfvdyCLQKIPQERPSSAELL 271
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
683-886 9.19e-12

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: 67.06  E-value: 9.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKeYASKDDHRDFAGELEV-LCKLGHHPNIINLLGACEHRGYLYLAIEYaphg 761
Cdd:cd07861    8 IGEGTYGVVYKGRNKKTG--QIVAMKKIR-LESEEEGVPSTAIREIsLLKELQHPNIVCLEDVLMQENRLYLVFEF---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 nlLDFLRKsRVLETDPAfaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd07861   81 --LSMDLK-KYLDSLPK-------GKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 842 QEVYVKKTMGRLPVRWM-AIESLNYSV-YTTNSDVWSYGVLLWEIVS 886
Cdd:cd07861  151 FGIPVRVYTHEVVTLWYrAPEVLLGSPrYSTPVDIWSIGTIFAEMAT 197
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
682-942 9.89e-12

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: 66.30  E-value: 9.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQ-VLKARIKKDGLRMDAAIKRMKeyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd08221    7 VLGRGAFGEaVLYRKTEDNSLVVWKEVNLSR--LSEKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEMEYCNG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDflrksrvletdpafAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd08221   84 GNLHD--------------KIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 841 --GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPLNCDD 918
Cdd:cd08221  150 vlDSESSMAESIVGTPY-YMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRT-FDATNPLRLAVKIVQGEYEDIDEQYSE 227
                        250       260
                 ....*....|....*....|....
gi 759191595 919 EVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd08221  228 EIIQLVHDCLHQDPEDRPTAEELL 251
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
677-949 1.03e-11

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: 66.53  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARikkdgLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd14152    2 IELGELIGQGRWGKVHRGR-----WHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAkIADF 836
Cdd:cd14152   77 FCKGRTLYSFVRDPKT---------------SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQEVYV---KKTMGRLPVRW---MAIESLNYSV---------YTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELY 901
Cdd:cd14152  141 GLFGISGVVQegrRENELKLPHDWlcyLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYELQA-RDWPLKNQPAEALI 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 902 EKLPQGYRLEKPL---NCDDEVYDLMRQCWREKPYERPSFAQI------LVSLNRML 949
Cdd:cd14152  220 WQIGSGEGMKQVLttiSLGKEVTEILSACWAFDLEERPSFTLLmdmlekLPKLNRRL 276
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
682-892 1.19e-11

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: 66.59  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFA-GELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05630    7 VLGKGGFGEVCACQVRATG-KMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSR-FVVSLAYAYETKDALCLVLTLMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLldflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS- 839
Cdd:cd05630   85 GDL--------------KFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAv 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 840 ---RGQEVyvkktMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05630  151 hvpEGQTI-----KGRVgTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPF 201
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
678-942 1.28e-11

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 66.61  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14168   13 EFKEVLGTGAFSEVVLAEERATGKLF--AVKCIPKKALKGKESSIENEIAVLRKIKHE-NIVALEDIYESPNHLYLVMQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLD-FLRKSRVLETDpafaianstASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV---GENYVAKI 833
Cdd:cd14168   90 VSGGELFDrIVEKGFYTEKD---------ASTLIRQ--------VLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVY-VKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEK-LPQGYRLE 911
Cdd:cd14168  153 SDFGLSKMEGKGdVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQiLKADYEFD 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 912 KPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14168  231 SPYwdDISDSAKDFIRNLMEKDPNKRYTCEQAL 263
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
681-886 1.33e-11

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: 66.60  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLrmdaAIKRMkeyaSKDDHRDFAGELEVLCKLG-HHPNIINLLGAcEHRGY-----LYLA 754
Cdd:cd14141    1 EIKARGRFGCVWKAQLLNEYV----AVKIF----PIQDKLSWQNEYEIYSLPGmKHENILQFIGA-EKRGTnldvdLWLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQK----------QFIHRDLAARNIL 824
Cdd:cd14141   72 TAFHEKGSLTDYLK-----------------ANVVSWNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVL 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 825 VGENYVAKIADFGLSRGQEV--YVKKTMGRLPV-RWMAIESLNYSVYTTNS-----DVWSYGVLLWEIVS 886
Cdd:cd14141  135 LKNNLTACIADFGLALKFEAgkSAGDTHGQVGTrRYMAPEVLEGAINFQRDaflriDMYAMGLVLWELAS 204
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
676-907 1.39e-11

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 66.02  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKfqDVIGEGNFGQVLkaRIKKDGLRMDAAIKRMKeyaSKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:cd14087    4 DIK--ALIGRGSFSRVV--RVEHRVTRQPYAIKMIE---TKCRGREVCeSELNVLRRV-RHTNIIQLIEVFETKERVYMV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDflrksRVletdpafaIANSTASTLSSQQLLHFAADvarGMDYLSQKQFIHRDLAARNILV---GENYVA 831
Cdd:cd14087   76 MELATGGELFD-----RI--------IAKGSFTERDATRVLQMVLD---GVKYLHGLGITHRDLKPENLLYyhpGPDSKI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLS----RGQEVYVKKTMGRlPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG 907
Cdd:cd14087  140 MITDFGLAstrkKGPNCLMKTTCGT-P-EYIAPEILLRKPYTQSVDMWAVGVIAYILLS-GTMPFDDDNRTRLYRQILRA 216
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
683-891 1.40e-11

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 66.30  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLG--HHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd07839    8 IGEGTYGTVFKAKNRETHEIV--ALKRVR--LDDDDEGVPSSALREICLLKelKHKNIVRLYDVLHSDKKLTLVFEYCDQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 gNLLDFLRKSRVlETDPafaianSTASTLSSQQLlhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd07839   84 -DLKKYFDSCNG-DIDP------EIVKSFMFQLL--------KGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 841 GQEVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIvSLGGTP 891
Cdd:cd07839  148 AFGIPVRCYSAEVVTLWYRPPDvlFGAKLYSTSIDMWSAGCIFAEL-ANAGRP 199
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
676-935 1.42e-11

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 66.60  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKfQDVIGEGNFGQVLKARIKKDGLRMDAAI--KRMKEYASKddhrdfagELEVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd14179    9 DLK-DKPLGEGSFSICRKCLHKKTNQEYAVKIvsKRMEANTQR--------EIAALKLCEGHPNIVKLHEVYHDQLHTFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSqqlLHfaaDVArgmdylsqkqFIHRDLAARNILV---GENYV 830
Cdd:cd14179   80 VMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSH---MH---DVG----------VVHRDLKPENLLFtdeSDNSE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRgqevyvKKTMGRLPVR-------WMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY-C---GMTCA- 898
Cdd:cd14179  144 IKIIDFGFAR------LKPPDNQPLKtpcftlhYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFqChdkSLTCTs 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 899 --ELYEKLPQG---YRLEKPLNCDDEVYDLMRQCWREKPYER 935
Cdd:cd14179  217 aeEIMKKIKQGdfsFEGEAWKNVSQEAKDLIQGLLTVDPNKR 258
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
704-942 1.44e-11

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: 66.14  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 704 DAAIKRMKEyaskdDHRDFAG-ELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPhGNLLDFLRKSRVLETDpafaia 782
Cdd:cd13982   27 PVAVKRLLP-----EFFDFADrEVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCA-ASLQDLVESPRESKLF------ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 783 nsTASTLSSQQLLHfaaDVARGMDYLSQKQFIHRDLAARNILV-----GENYVAKIADFGLSR----GQEVYVKKTMGRL 853
Cdd:cd13982   95 --LRPGLEPVRLLR---QIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFGLCKkldvGRSSFSRRSGVAG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 854 PVRWMAIESLNYSVY---TTNSDVWSYGVLLWEIVSLGGTPYCGMtcaelYEK----LPQGYRLEKPL---NCDDEVYDL 923
Cdd:cd13982  170 TSGWIAPEMLSGSTKrrqTRAVDIFSLGCVFYYVLSGGSHPFGDK-----LEReaniLKGKYSLDKLLslgEHGPEAQDL 244
                        250
                 ....*....|....*....
gi 759191595 924 MRQCWREKPYERPSFAQIL 942
Cdd:cd13982  245 IERMIDFDPEKRPSAEEVL 263
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
683-942 1.63e-11

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: 65.61  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIK-------RMKEYASKDDHRDfaGELEVLCKlghHPNIINLLGACEHRGYLYLAI 755
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKV--AIKvidkkkaKKDSYVTKNLRRE--GRIQQMIR---HPNITQLLDILETENSYYLVM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSRVLETDPAfaiANSTASTLSSQQLLHFAAdvargmdylsqkqFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd14070   83 ELCPGGNLMHRIYDKKRLEEREA---RRYIRQLVSAVEHLHRAG-------------VVHRDLKIENLLLDENDNIKLID 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSR-------GQEVYvkkTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYC--GMTCAELYEKLPQ 906
Cdd:cd14070  147 FGLSNcagilgySDPFS---TQCGSPA-YAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTvePFSLRALHQKMVD 221
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 907 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14070  222 KEMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQAL 257
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
683-892 1.63e-11

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: 66.29  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKeYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd06654   28 IGQGASGTVYTAMDVATG--QEVAIRQMN-LQQQPKKELIINEILVM-RENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd06654  104 LTDVV-----------------TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqi 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 841 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06654  167 TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY 216
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
682-942 1.65e-11

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: 66.62  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKE-----YASKDDHRdfagELEVLcKLGHHPNIINLLGAcehrgylylaie 756
Cdd:cd07855   12 TIGSGAYGVVCSAIDTKSGQKV--AIKKIPNafdvvTTAKRTLR----ELKIL-RHFKHDNIIAIRDI------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVL---ETDPAFAIANStaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd07855   73 LRPKVPYADFKDVYVVLdlmESDLHHIIHSD--QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRG----QEVYVKKTMGRLPVRWMAIESLNYSV--YTTNSDVWSYGVLLWE-------------------IVSLG 888
Cdd:cd07855  151 GDFGMARGlctsPEEHKYFMTEYVATRWYRAPELMLSLpeYTQAIDMWSVGCIFAEmlgrrqlfpgknyvhqlqlILTVL 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 889 GTPYCGM---TCAELYEKLPQGY--RLEKPLN-----CDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd07855  231 GTPSQAVinaIGADRVRRYIQNLpnKQPVPWEtlypkADQQALDLLSQMLRFDPSERITVAEAL 294
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
735-942 1.70e-11

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: 65.72  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEHRGYLYLAIEYAPHGNLLDfLRKSRVLETDPafaianstastlssqQLLHFAADVARGMDYLSQKQFI 814
Cdd:cd14187   66 HQHVVGFHGFFEDNDFVYVVLELCRRRSLLE-LHKRRKALTEP---------------EARYYLRQIILGCQYLHRNRVI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 815 HRDLAARNILVGENYVAKIADFGLSRGQEV--YVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPY 892
Cdd:cd14187  130 HRDLKLGNLFLNDDMEVKIGDFGLATKVEYdgERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPF 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 893 CGMTCAELYEKLPQG-YRLEKPLNcdDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14187  208 ETSCLKETYLRIKKNeYSIPKHIN--PVAASLIQKMLQTDPTARPTINELL 256
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
680-891 1.88e-11

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 65.76  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLR-----MDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd14181   15 KEVIGRGVSSVVRRCVHRHTGQEfavkiIEVTAERLSPEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd14181   95 FDLMRRGELFDYL----------------TEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 835 DFGLSRGQEVYVK-KTMGRLPvRWMAIESLNYSV------YTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd14181  159 DFGFSCHLEPGEKlRELCGTP-GYLAPEILKCSMdethpgYGKEVDLWACGVILFTL--LAGSP 219
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
664-948 1.98e-11

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: 65.82  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 664 PDPTIYPVLDWN---DIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDD--HRDFAGELEVLCKLgHHPNI 738
Cdd:cd08229   10 PQKALRPDMGYNtlaNFRIEKKIGRGQFSEVYRATCLLDGVPV--ALKKVQIFDLMDAkaRADCIKEIDLLKQL-NHPNV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 739 INLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDL 818
Cdd:cd08229   87 IKYYASFIEDNELNIVLELADAGDLSRMIKHFK------------KQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 819 AARNILVGENYVAKIADFGLSR--GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCG-- 894
Cdd:cd08229  155 KPANVFITATGVVKLGDLGLGRffSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGdk 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 895 MTCAELYEKLPQ-GYrleKPLNCD---DEVYDLMRQCWREKPYERPSFAQILVSLNRM 948
Cdd:cd08229  233 MNLYSLCKKIEQcDY---PPLPSDhysEELRQLVNMCINPDPEKRPDITYVYDVAKRM 287
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
678-942 2.84e-11

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 65.05  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14184    4 KIGKVIGDGNFAVVKECVERSTG--KEFALKIIDKAKCCGKEHLIENEVSILRRV-KHPNIIMLIEEMDTPAELYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDflrksrvletdpafAIANSTASTLSSQQLLHFaaDVARGMDYLSQKQFIHRDLAARNILVGE----NYVAKI 833
Cdd:cd14184   81 VKGGDLFD--------------AITSSTKYTERDASAMVY--NLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTMGRlPVrWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTC--AELYEKLPQGyRLE 911
Cdd:cd14184  145 GDFGLATVVEGPLYTVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRSENNlqEDLFDQILLG-KLE 220
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 912 KPL----NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14184  221 FPSpywdNITDSAKELISHMLQVNVEARYTAEQIL 255
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
683-942 3.30e-11

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: 65.14  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDdHRDFAGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARD-HQKLEREARI-CRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LL-DFLRKSRVLETDPAFAIanstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVG---ENYVAKIADFGL 838
Cdd:cd14086   87 LFeDIVAREFYSEADASHCI----------QQILE-------SVNHCHQNGIVHRDLKPENLLLAsksKGAAVKLADFGL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 ----SRGQEVY--VKKTMGrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG-YRLE 911
Cdd:cd14086  150 aievQGDQQAWfgFAGTPG-----YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDEDQHRLYAQIKAGaYDYP 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 912 KPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14086  224 SPEwdTVTPEAKDLINQMLTVNPAKRITAAEAL 256
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
682-884 3.45e-11

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 65.53  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd06615    8 ELGAGNGGVVTKVLHRPSGLIM--ARKLIHLEIKPAIRNQIIRELKVLHEC-NSPYIVGFYGAFYSDGEISICMEHMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQK-QFIHRDLAARNILVGENYVAKIADFGLSr 840
Cdd:cd06615   85 SLDQVLKK----------------AGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVS- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 759191595 841 GQEVyvkKTMGRLPV---RWMAIESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd06615  148 GQLI---DSMANSFVgtrSYMSPERLQGTHYTVQSDIWSLGLSLVEM 191
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
683-925 3.90e-11

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 65.28  E-value: 3.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAI--KRMKEYASKddhrdfagELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIisRRMEANTQR--------EVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPAFAIANSTASTLSsqqllhfaadvargmdYLSQKQFIHRDLAARNILV---GENYVAKIADFG 837
Cdd:cd14180   86 GELLDRIKKKARFSESEASQLMRSLVSAVS----------------FMHEAGVVHRDLKPENILYadeSDGAVLKVIDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRgqevyvKKTMGRLP-------VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMT-------CAELYEK 903
Cdd:cd14180  150 FAR------LRPQGSRPlqtpcftLQYAAPELFSNQGYDESCDLWSLGVILYTMLS-GQVPFQSKRgkmfhnhAADIMHK 222
                        250       260
                 ....*....|....*....|....*
gi 759191595 904 LPQG-YRLEKPL--NCDDEVYDLMR 925
Cdd:cd14180  223 IKEGdFSLEGEAwkGVSEEAKDLVR 247
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
683-885 4.45e-11

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: 64.78  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEV-LCKLGHHPNIIN-------LLGACEHRGYLyLA 754
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYV--AIKKCRQELSPSDKNRERWCLEVqIMKKLNHPNVVSardvppeLEKLSPNDLPL-LA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL---VGENYVA 831
Cdd:cd13989   78 MEYCSGGDLRKVLNQP-------------ENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVlqqGGGRVIY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 832 KIADFGLSR--GQEVYVKKTMGRLpvRWMAIESLNYSVYTTNSDVWSYGVLLWEIV 885
Cdd:cd13989  145 KLIDLGYAKelDQGSLCTSFVGTL--QYLAPELFESKKYTCTVDYWSFGTLAFECI 198
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
683-892 4.47e-11

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: 64.43  E-value: 4.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQV---LKARIKKDGLRMDAAIKRMKEYASKDDHRD--FAGELEVLCKLGHhPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14076    9 LGEGEFGKVklgWPLPKANHRSGVQVAIKLIRRDTQQENCQTskIMREINILKGLTH-PNIVRLLDVLKTKKYIGIVLEF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLEtdpafaiaNSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd14076   88 VSGGELFDYILARRRLK--------DSVACRLFAQ--------LISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFG 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 838 ------LSRGQevyVKKTMGRLPVrWMAIESLNY-SVYT-TNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd14076  152 fantfdHFNGD---LMSTSCGSPC-YAAPELVVSdSMYAgRKADIWSCGVILYAMLA-GYLPF 209
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
683-886 4.62e-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: 64.70  E-value: 4.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEyaSKDD---HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIV--AIKKFVE--SEDDpviKKIALREIRMLKQL-KHPNLVNLIEVFRRKRKLHLVFEYCD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HgNLLDflrksrVLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd07847   84 H-TVLN------ELEKNP---------RGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFA 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 840 R---GQEV----YVKktmgrlpVRWM-AIESL-NYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd07847  148 RiltGPGDdytdYVA-------TRWYrAPELLvGDTQYGPPVDVWAIGCVFAELLT 196
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
667-894 5.59e-11

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 65.06  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 667 TIYPVLDwndiKFQDV--IGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLG 743
Cdd:cd07877   11 TIWEVPE----RYQNLspVGSGAYGSVCAAFDTKTGLRV--AVKKLsRPFQSIIHAKRTYRELRLL-KHMKHENVIGLLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 744 AcehrgylylaieYAPHGNLLDFlrKSRVLETDPAFAIANSTA--STLSSQQLLHFAADVARGMDYLSQKQFIHRDLAAR 821
Cdd:cd07877   84 V------------FTPARSLEEF--NDVYLVTHLMGADLNNIVkcQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 822 NILVGENYVAKIADFGLSRGQEvyvKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd07877  150 NLAVNEDCELKILDFGLARHTD---DEMTGYVATRWYRAPEimLNWMHYNQTVDIWSVGCIMAELLT-GRTLFPG 220
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
672-931 6.00e-11

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: 65.80  E-value: 6.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYL 751
Cdd:cd05624   69 LHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVN-GDCQWITTLHYAFQDENYL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRK--SRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd05624  148 YLVMDYYVGGDLLTLLSKfeDKLPEDMARF-----------------YIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNG 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFG--LSRGQEVYVKKTMGRLPVRWMAIESLN-----YSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYE 902
Cdd:cd05624  211 HIRLADFGscLKMNDDGTVQSSVAVGTPDYISPEILQamedgMGKYGPECDWWSLGVCMYEML-YGETPFYAESLVETYG 289
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 903 K-LPQGYRLEKPLNCDD---EVYDLMRQ--CWREK 931
Cdd:cd05624  290 KiMNHEERFQFPSHVTDvseEAKDLIQRliCSRER 324
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
683-885 6.34e-11

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: 64.47  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLgACEH-----RGYLYLAIEY 757
Cdd:cd07837    9 IGEGTYGKVYKARDKNTG-KLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIYIVRLL-DVEHveengKPLLYLVFEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 ApHGNLLDFLRKSRvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVG-ENYVAKIADF 836
Cdd:cd07837   87 L-DTDLKKFIDSYG-----------RGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 837 GLSRGQEVYVKKTMGRLPVRWM-AIES-LNYSVYTTNSDVWSYGVLLWEIV 885
Cdd:cd07837  155 GLGRAFTIPIKSYTHEIVTLWYrAPEVlLGSTHYSTPVDMWSVGCIFAEMS 205
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
683-892 6.61e-11

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 64.27  E-value: 6.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLV--AVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVLETDpafaIANSTASTLSSQQLLHfaadvARGMdylsqkqfIHRDLAARNILVGENYVAKIADFGLSR-- 840
Cdd:cd06657  104 LTDIVTHTRMNEEQ----IAAVCLAVLKALSVLH-----AQGV--------IHRDIKSDSILLTHDGRVKLSDFGFCAqv 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759191595 841 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd06657  167 SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 216
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
682-935 6.80e-11

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: 64.16  E-value: 6.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFAG-ELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05607    9 VLGKGGFGEVCAVQVKNTG-QMYACKKLDKKRLKKKSGEKMALlEKEILEKV-NSPFIVSLAYAFETKTHLCLVMSLMNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLldflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS- 839
Cdd:cd05607   87 GDL--------------KYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAv 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 ---RGQEVYVKK-TMGrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYcgmtcAELYEKLPQGYRLEKPL- 914
Cdd:cd05607  153 evkEGKPITQRAgTNG-----YMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF-----RDHKEKVSKEELKRRTLe 221
                        250       260
                 ....*....|....*....|....*....
gi 759191595 915 --------NCDDEVYDLMRQCWREKPYER 935
Cdd:cd05607  222 devkfehqNFTEEAKDICRLFLAKKPENR 250
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
682-901 6.90e-11

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: 64.72  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKkdGLRMDAAIKRMKE--YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05587    3 VLGKGSFGKVMLAERK--GTDELYAIKILKKdvIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRK-SRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05587   81 GGDLMYHIQQvGKFKEPVAVF-----------------YAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGM 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 839 SRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELY 901
Cdd:cd05587  144 CKEgiFGGKTTRTFCGTP-DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELF 206
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
682-935 7.19e-11

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: 64.51  E-value: 7.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARiKKDGLRMdAAIKRMKE--YASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05585    1 VIGKGSFGKVMQVR-KKDTSRI-YALKTIRKahIVSRSEVTHTLAERTVLAQV-DCPFIVPLKFSFQSPEKLYLVLAFIN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFL-RKSRVLETDPAFAIAnstastlssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVgeNYVAKIA--DF 836
Cdd:cd05585   78 GGELFHHLqREGRFDLSRARFYTA----------ELL-------CALECLHKFNVIYRDLKPENILL--DYTGHIAlcDF 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSR--GQEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpqgyrLEKPL 914
Cdd:cd05585  139 GLCKlnMKDDDKTNTFCGTP-EYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPFYDENTNEMYRKI-----LQEPL 211
                        250       260
                 ....*....|....*....|....*
gi 759191595 915 ----NCDDEVYDLMRQCWREKPYER 935
Cdd:cd05585  212 rfpdGFDRDAKDLLIGLLNRDPTKR 236
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
681-897 9.22e-11

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 63.97  E-value: 9.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLrmDAAIKRMKEYASKDDHRDFAgELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14090    8 ELLGEGAYASVQTCINLYTGK--EYAVKIIEKHPGHSRSRVFR-EVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV---AKIADFG 837
Cdd:cd14090   85 GPLLSHIEKRV----------------HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRGqevyVKKTMGRL----------PV---RWMAIESLNY-----SVYTTNSDVWSYGVLLWeIVSLGGTPY---CGMT 896
Cdd:cd14090  149 LGSG----IKLSSTSMtpvttpelltPVgsaEYMAPEVVDAfvgeaLSYDKRCDLWSLGVILY-IMLCGYPPFygrCGED 223

                 .
gi 759191595 897 C 897
Cdd:cd14090  224 C 224
PHA02988 PHA02988
hypothetical protein; Provisional
737-945 1.04e-10

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 63.61  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 737 NIINLLG----ACEHRGYLYLAIEYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQK- 811
Cdd:PHA02988  79 NILKIYGfiidIVDDLPRLSLILEYCTRGYLREVLDKEK----------------DLSFKTKLDMAIDCCKGLYNLYKYt 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 812 QFIHRDLAARNILVGENYVAKIADFGLsrgqevyvKKTMGRLP---VRWMAIESLN-----YSVYTTNSDVWSYGVLLWE 883
Cdd:PHA02988 143 NKPYKNLTSVSFLVTENYKLKIICHGL--------EKILSSPPfknVNFMVYFSYKmlndiFSEYTIKDDIYSLGVVLWE 214
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 884 IVSlGGTPYCGMTCAELYEKL-PQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 945
Cdd:PHA02988 215 IFT-GKIPFENLTTKEIYDLIiNKNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNL 276
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
676-936 1.07e-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: 63.92  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDV--IGEGNFGQVLKARIKKDGLRMdaaIKRMKEYASKDDHRD-FAGELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd06650    4 DDDFEKIseLGAGNGGVVFKVSHKPSGLVM---ARKLIHLEIKPAIRNqIIRELQVLHEC-NSPYIVGFYGAFYSDGEIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQK-QFIHRDLAARNILVGENYVA 831
Cdd:cd06650   80 ICMEHMDGGSLDQVLKK----------------AGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSrGQEVyvkKTMGRLPV---RWMAIESLNYSVYTTNSDVWSYGVLLWEIvSLGGTPYcgmtcaelyeKLPQGY 908
Cdd:cd06650  144 KLCDFGVS-GQLI---DSMANSFVgtrSYMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYPI----------PPPDAK 208
                        250       260
                 ....*....|....*....|....*...
gi 759191595 909 RLEKPLNCDDEvYDLMRQCWREKPYERP 936
Cdd:cd06650  209 ELELMFGCQVE-GDAAETPPRPRTPGRP 235
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
683-892 1.10e-10

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: 63.70  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd05577    1 LGRGGFGEVCACQVKATG-KMYACKKLDKKRIKKKKGETMAlNEKIILEKV-SSPFIVSLAYAFETKDKLCLVLTLMNGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLldflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS-- 839
Cdd:cd05577   79 DL--------------KYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAve 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 840 -RGQevyvKKTMGRL-PVRWMAIESLNYSV-YTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05577  145 fKGG----KKIKGRVgTHGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIA-GRSPF 195
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
681-886 1.30e-10

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: 63.51  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLrmdaAIKRMkeyaSKDDHRDFAGELEVLCKLG-HHPNIINLLGAcEHRGY-----LYLA 754
Cdd:cd14140    1 EIKARGRFGCVWKAQLMNEYV----AVKIF----PIQDKQSWQSEREIFSTPGmKHENLLQFIAA-EKRGSnlemeLWLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQK-----------QFIHRDLAARNI 823
Cdd:cd14140   72 TAFHDKGSLTDYLK-----------------GNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNV 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 824 LVGENYVAKIADFGLSrgqevyVKKTMGRLP---------VRWMAIESLNYSV-YTTNS----DVWSYGVLLWEIVS 886
Cdd:cd14140  135 LLKNDLTAVLADFGLA------VRFEPGKPPgdthgqvgtRRYMAPEVLEGAInFQRDSflriDMYAMGLVLWELVS 205
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
683-885 1.37e-10

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 63.91  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKdgLRMDAAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLGAcehrgylylaieYAPHG 761
Cdd:cd07878   23 VGSGAYGSVCSAYDTR--LRQKVAVKKLsRPFQSLIHARRTYRELRLL-KHMKHENVIGLLDV------------FTPAT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFlrKSRVLETDPAFAIANSTA--STLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd07878   88 SIENF--NEVYLVTNLMGADLNNIVkcQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLA 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 759191595 840 RGQEvyvKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIV 885
Cdd:cd07878  166 RQAD---DEMTGYVATRWYRAPEimLNWMHYNQTVDIWSVGCIMAELL 210
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
681-943 1.65e-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: 63.00  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRmdaAIKRM----KEYASKDDhrdFAGELEVLCKLGHHPNIINLLGA--CEHRGYLYLA 754
Cdd:cd14131    7 KQLGKGGSSKVYKVLNPKKKIY---ALKRVdlegADEQTLQS---YKNEIELLKKLKGSDRIIQLYDYevTDEDDYLYMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYApHGNLLDFLRKSRVLETDPAFaIANSTASTLSSQQLLHfaadvargmdylsQKQFIHRDLAARNILVGENYVaKIA 834
Cdd:cd14131   81 MECG-EIDLATILKKKRPKPIDPNF-IRYYWKQMLEAVHTIH-------------EEGIVHSDLKPANFLLVKGRL-KLI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRG-QE----VYVKKTMGRLpvRWMAIESLNYSVYTTN----------SDVWSYGVLLWEIVsLGGTPYCGMTcaE 899
Cdd:cd14131  145 DFGIAKAiQNdttsIVRDSQVGTL--NYMSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQMV-YGKTPFQHIT--N 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 900 LYEKL-----PqGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILV 943
Cdd:cd14131  220 PIAKLqaiidP-NHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLN 267
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
675-904 1.69e-10

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 63.92  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLA 754
Cdd:cd05627    2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVE-ADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd05627   81 MEFLPGGDMMTLLMKK----------------DTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 835 DFGLSRG------QEVYV------------------------KKTMGRLPVR------WMAIESLNYSVYTTNSDVWSYG 878
Cdd:cd05627  145 DFGLCTGlkkahrTEFYRnlthnppsdfsfqnmnskrkaetwKKNRRQLAYStvgtpdYIAPEVFMQTGYNKLCDWWSLG 224
                        250       260
                 ....*....|....*....|....*.
gi 759191595 879 VLLWEIVsLGGTPYCGMTCAELYEKL 904
Cdd:cd05627  225 VIMYEML-IGYPPFCSETPQETYRKV 249
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
682-942 1.98e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 64.51  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAgelEVLCKLghHPNIINLLGACEHRGY----------- 750
Cdd:PTZ00283  39 VLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQA---EVCCLL--NCDFFSIVKCHEDFAKkdprnpenvlm 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLrKSRVlETDPAFAiaNSTASTLSSQQLLhfaadvarGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:PTZ00283 114 IALVLDYANAGDLRQEI-KSRA-KTNRTFR--EHEAGLLFIQVLL--------AVHHVHSKHMIHRDIKSANILLCSNGL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRGQEVYVKKTMGR----LPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQ 906
Cdd:PTZ00283 182 VKLGDFGFSKMYAATVSDDVGRtfcgTPY-YVAPEIWRRKPYSKKADMFSLGVLLYELLTL-KRPFDGENMEEVMHKTLA 259
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 759191595 907 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:PTZ00283 260 GRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
681-840 2.04e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.43  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKArikKDgLRMD--AAIKRMK-EYASKDD-HRDF------AGELEvlcklghHPNIINLLGACEHRGY 750
Cdd:NF033483  13 ERIGRGGMAEVYLA---KD-TRLDrdVAVKVLRpDLARDPEfVARFrreaqsAASLS-------HPNIVSVYDVGEDGGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRVLetdpafaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:NF033483  82 PYIVMEYVDGRTLKDYIREHGPL----------------SPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR 145
                        170
                 ....*....|
gi 759191595 831 AKIADFGLSR 840
Cdd:NF033483 146 VKVTDFGIAR 155
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
388-594 2.09e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.64  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 388 RFTTASIGLPPPRGLSLLPKSQTTLNLTWQPifPSSED-DFYvEVERRsvqmNSDQQNIKVPGNL--TSVLLNNLHP--R 462
Cdd:COG3401  225 SVTTPTTPPSAPTGLTATADTPGSVTLSWDP--VTESDaTGY-RVYRS----NSGDGPFTKVATVttTSYTDTGLTNgtT 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 463 EQYVVRARVNTKAQGEWSEDLTAwTLSDILPPQPENIKISNITDSTAMISWTildgYSISSIIIRYKIQGKNEDQHIDVK 542
Cdd:COG3401  298 YYYRVTAVDAAGNESAPSNVVSV-TTDLTPPAAPSGLTATAVGSSSITLSWT----ASSDADVTGYNVYRSTSGGGTYTK 372
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 543 I-KNATITQYQLKGLEPQTVYQVDIFAENNIGSSNPtFSHELTTLSESQVPAE 594
Cdd:COG3401  373 IaETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESA-PSEEVSATTASAASGE 424
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
675-887 2.19e-10

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: 62.35  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRmdAAIKRMKeYASKDDHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLA 754
Cdd:cd06646    9 HDYELIQRVGSGTYGDVYKARNLHTGEL--AAVKIIK-LEPGDDFSLIQQEIFMVKECKHC-NIVAYFGSYLSREKLWIC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKsrvleTDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd06646   85 MEYCGGGSLQDIYHV-----TGP-----------LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 835 DFGLSRGQEVYVKKTMGRLPV-RWMAIESLNYSV---YTTNSDVWSYGVLLWEIVSL 887
Cdd:cd06646  149 DFGVAAKITATIAKRKSFIGTpYWMAPEVAAVEKnggYNQLCDIWAVGITAIELAEL 205
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
682-915 2.29e-10

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 63.10  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYA--SKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLY--AVKVLQKKAilKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRV-LETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILV-GENYVaKIADFG 837
Cdd:cd05575   80 GGELFFHLQRERHfPEPRARF-----------------YAAEIASALGYLHSLNIIYRDLKPENILLdSQGHV-VLTDFG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 LSRgQEVYVKKTMGRL---PvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpqgyrLEKPL 914
Cdd:cd05575  142 LCK-EGIEPSDTTSTFcgtP-EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLY-GLPPFYSRDTAEMYDNI-----LHKPL 213

                 .
gi 759191595 915 N 915
Cdd:cd05575  214 R 214
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
683-895 2.30e-10

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


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 62.79  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEyaskDDHRDFAGELEV-LCKLGHHPNIINLLGACEHRGYLYLAIEYApHG 761
Cdd:cd07869   13 LGEGSYATVYKGKSKVNGKLVALKVIRLQE----EEGTPFTAIREAsLLKGLKHANIVLLHDIIHTKETLTLVFEYV-HT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 841
Cdd:cd07869   88 DLCQYMDKH---------------PGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 842 QEVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM 895
Cdd:cd07869  153 KSVPSHTYSNEVVTLWYRPPDvlLGSTEYSTCLDMWGVGCIFVEMIQ-GVAAFPGM 207
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
680-898 2.43e-10

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 62.74  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQV---LKARIKKDglrmdAAIKRMKEYASKDDHRDFAgELEVLCKLGHHPNIINLLGACEHRGYLYLAIE 756
Cdd:cd14173    7 EEVLGEGAYARVqtcINLITNKE-----YAVKIIEKRPGHSRSRVFR-EVEMLYQCQGHRNVLELIEFFEEEDKFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVL-ETDPAFAIAnstastlssqqllhfaaDVARGMDYLSQKQFIHRDLAARNILV-GENYVA--K 832
Cdd:cd14173   81 KMRGGSILSHIHRRRHFnELEASVVVQ-----------------DIASALDFLHNKGIAHRDLKPENILCeHPNQVSpvK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFGLSRGQEVYVKKTMGRLP--------VRWMA---IESLN--YSVYTTNSDVWSYGVLLWEIVSlGGTPY---CGMT 896
Cdd:cd14173  144 ICDFDLGSGIKLNSDCSPISTPelltpcgsAEYMApevVEAFNeeASIYDKRCDLWSLGVILYIMLS-GYPPFvgrCGSD 222

                 ..
gi 759191595 897 CA 898
Cdd:cd14173  223 CG 224
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
681-899 2.55e-10

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: 62.71  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIK-KDGLrmdAAIKRMKEyaskdDHRDFAG-----ELEVLCKLgHHPNIINLLGACEHRGYLYLA 754
Cdd:cd07873    8 DKLGEGTYATVYKGRSKlTDNL---VALKEIRL-----EHEEGAPctairEVSLLKDL-KHANIVTLHDIIHTEKSLTLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYaphgnlldfLRKSRVLETDPAFAIANSTASTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIA 834
Cdd:cd07873   79 FEY---------LDKDLKQYLDDCGNSINMHNVKLFLFQLL-------RGLAYCHRRKVLHRDLKPQNLLINERGELKLA 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 835 DFGLSRGQEVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVSlgGTP-YCGMTCAE 899
Cdd:cd07873  143 DFGLARAKSIPTKTYSNEVVTLWYRPPDilLGSTDYSTQIDMWGVGCIFYEMST--GRPlFPGSTVEE 208
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
672-892 2.61e-10

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 63.12  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRmKEYASKDDHRDFA-GELEVLCKLGHHPNIINLLGACEHRGY 750
Cdd:cd05617   12 LGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVK-KELVHDDEDIDWVqTEKHVFEQASSNPFLVGLHSCFQTTSR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05617   91 LFLVIEYVNGGDLMFHMQRQRKLPEEHA----------------RFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 831 AKIADFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05617  155 IKLTDYGMCKEglGPGDTTSTFCGTP-NYIAPEILRGEEYGFSVDWWALGVLMFEMMA-GRSPF 216
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
679-942 2.98e-10

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: 62.05  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGElEVLC-KLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14074    7 LEETLGRGHFAVVKLARHVFTGEKV--AVKVIDKTKLDDVSKAHLFQ-EVRCmKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY-VAKIADF 836
Cdd:cd14074   84 GDGGDMYDYIMKH---------------ENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSR----GQEvyVKKTMGRLPvrWMAIESLNYSVYTTNS-DVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLE 911
Cdd:cd14074  149 GFSNkfqpGEK--LETSCGSLA--YSAPEILLGDEYDAPAvDIWSLGVILYMLVC-GQPPFQEANDSETLTMIMDC-KYT 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14074  223 VPAHVSPECKDLIRRMLIRDPKKRASLEEIE 253
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
681-886 3.47e-10

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: 62.32  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIK-KDGLrmdAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYap 759
Cdd:cd07872   12 EKLGEGTYATVFKGRSKlTENL---VALKEIRLEHEEGAPCTAIREVSLLKDL-KHANIVTLHDIVHTDKSLTLVFEY-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 hgnlLDFLRKSRVletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd07872   86 ----LDKDLKQYM----------DDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 840 RGQEVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd07872  152 RAKSVPTKTYSNEVVTLWYRPPDvlLGSSEYSTQIDMWGVGCIFFEMAS 200
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
672-892 4.13e-10

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 62.74  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIKFQDVIGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKDDHRDFA-GELEVLCKLGHHPNIINLLGACEHRGY 750
Cdd:cd05618   17 LGLQDFDLLRVIGRGSYAKVLLVRLKKTE-RIYAMKVVKKELVNDDEDIDWVqTEKHVFEQASNHPFLVGLHSCFQTESR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05618   96 LFFVIEYVNGGDLMFHMQRQR----------------KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 831 AKIADFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05618  160 IKLTDYGMCKEglRPGDTTSTFCGTP-NYIAPEILRGEDYGFSVDWWALGVLMFEMMA-GRSPF 221
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
676-930 5.20e-10

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 62.73  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd05623   73 DFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVN-GDSQWITTLHYAFQDDNNLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRK--SRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05623  152 DYYVGGDLLTLLSKfeDRLPEDMARF-----------------YLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFG--LSRGQEVYVKKTMGRLPVRWMAIESLNY-----SVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEK-LP 905
Cdd:cd05623  215 ADFGscLKLMEDGTVQSSVAVGTPDYISPEILQAmedgkGKYGPECDWWSLGVCMYEML-YGETPFYAESLVETYGKiMN 293
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 906 QGYRLEKPLNCDD---EVYDLMRQ--CWRE 930
Cdd:cd05623  294 HKERFQFPTQVTDvseNAKDLIRRliCSRE 323
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
673-904 6.17e-10

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: 62.32  E-value: 6.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWNDIKfqdVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCkLGHHPNIINLLGACEHRGYLY 752
Cdd:cd05621   53 DYDVVK---VIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMA-FANSPWVVQLFCAFQDDKYLY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 832
Cdd:cd05621  129 MVMEYMPGGDLVNLMSNYDVPEKWAKF-----------------YTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLK 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 833 IADFG----LSRGQEVYVKKTMGrlPVRWMAIESLNYS----VYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKL 904
Cdd:cd05621  192 LADFGtcmkMDETGMVHCDTAVG--TPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEML-VGDTPFYADSLVGTYSKI 268
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
683-913 6.55e-10

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: 61.30  E-value: 6.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKArIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVL-----CKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14096    9 IGEGAFSNVYKA-VPLRNTGKPVAIKVVRKADLSSDNLKGSSRANILkevqiMKRLSHPNIVKLLDFQESDEYYYIVLEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRKSRVLETDpafaianstastLSSqqllHFAADVARGMDYLSQKQFIHRDLAARNILV------------ 825
Cdd:cd14096   88 ADGGEIFHQIVRLTYFSED------------LSR----HVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivkl 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 ---------------------GENYVAKIADFGLSRgqEVYVKKTMgrLP---VRWMAIESLNYSVYTTNSDVWSYGVLL 881
Cdd:cd14096  152 rkadddetkvdegefipgvggGGIGIVKLADFGLSK--QVWDSNTK--TPcgtVGYTAPEVVKDERYSKKVDMWALGCVL 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 882 WEIVSlGGTPYCGMTCAELYEKLPQG-YRLEKP 913
Cdd:cd14096  228 YTLLC-GFPPFYDESIETLTEKISRGdYTFLSP 259
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
679-963 7.74e-10

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: 61.19  E-value: 7.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDV--IGEGNFGQVLKAR-IKKDGLrmdAAIKRMkEYASKDDH---RDFAGELEVLCKLgHHPNIINLLGAC--EHRGY 750
Cdd:cd06634   17 FSDLreIGHGSFGAVYFARdVRNNEV---VAIKKM-SYSGKQSNekwQDIIKEVKFLQKL-RHPNTIEYRGCYlrEHTAW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSrvletdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd06634   92 LVMEYCLGSASDLLEVHKKP------------------LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGlsRGQEVYVKKTMGRLPVrWMAIE---SLNYSVYTTNSDVWSYGVllweivslggtpycgmTCAELYEKLPQG 907
Cdd:cd06634  154 VKLGDFG--SASIMAPANSFVGTPY-WMAPEvilAMDEGQYDGKVDVWSLGI----------------TCIELAERKPPL 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 908 YRL------------EKPL----NCDDEVYDLMRQCWREKPYERPSfAQILVSLNRMLEERKTYVNTTLYEK 963
Cdd:cd06634  215 FNMnamsalyhiaqnESPAlqsgHWSEYFRNFVDSCLQKIPQDRPT-SDVLLKHRFLLRERPPTVIMDLIQR 285
fn3 pfam00041
Fibronectin type III domain;
298-373 7.85e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 7.85e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595  298 PKPLNaPNVIDTGHNFAVINISsEPYFGDGPIKSKKLLYKPVNHYEAWRQIQVTNEI--VTLNYLEPRTEYELCVQLV 373
Cdd:pfam00041   1 SAPSN-LTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAV 76
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
677-946 8.07e-10

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: 60.69  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQV---LKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIInLLGACEHRGYLYL 753
Cdd:cd14208    1 LTFMESLGKGSFTKIyrgLRTDEEDDERCETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVL-LHGVCVGKDSIMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AiEYAPHGNLLDFLRKsrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV------GE 827
Cdd:cd14208   80 Q-EFVCHGALDLYLKK-------------QQQKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLsregdkGS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 828 NYVAKIADFGLSrgQEVYVKKTMG-RLPvrWMAIESL-NYSVYTTNSDVWSYGVLLWEIVSLGGTPycgMTCAELYEKLp 905
Cdd:cd14208  146 PPFIKLSDPGVS--IKVLDEELLAeRIP--WVAPECLsDPQNLALEADKWGFGATLWEIFSGGHMP---LSALDPSKKL- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759191595 906 QGY--RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLN 946
Cdd:cd14208  218 QFYndRKQLPAPHWIELASLIQQCMSYNPLLRPSFRAIIRDLN 260
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
788-891 9.83e-10

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 61.23  E-value: 9.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 788 TLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWM-AIES-LNY 865
Cdd:cd07858  104 TLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYrAPELlLNC 183
                         90       100
                 ....*....|....*....|....*.
gi 759191595 866 SVYTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd07858  184 SEYTTAIDVWSVGCIFAEL--LGRKP 207
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
397-487 1.07e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRAR-VNTKA 475
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGGG 81
                         90
                 ....*....|..
gi 759191595 476 QGEWSEDLTAWT 487
Cdd:cd00063   82 ESPPSESVTVTT 93
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
675-903 1.14e-09

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 61.09  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 675 NDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMK--EYASKD--DH----RDFAGElevlcklGHHPNIINLLGACE 746
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVY--AMKKLRksEMLEKEqvAHvraeRDILAE-------ADNPWVVKLYYSFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 747 HRGYLYLAIEYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVG 826
Cdd:cd05599   72 DEENLYLIMEFLPGGDMMTLLMKK----------------DTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 827 ENYVAKIADFGLSRGqevyVKK------TMGRlPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAEL 900
Cdd:cd05599  136 ARGHIKLSDFGLCTG----LKKshlaysTVGT-P-DYIAPEVFLQKGYGKECDWWSLGVIMYEML-IGYPPFCSDDPQET 208

                 ...
gi 759191595 901 YEK 903
Cdd:cd05599  209 CRK 211
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
683-884 1.21e-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: 60.83  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaaIKRMKEYASKDDHRD-FAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd06649   13 LGAGNGGVVTKVQHKPSGLIM---ARKLIHLEIKPAIRNqIIRELQVLHEC-NSPYIVGFYGAFYSDGEISICMEHMDGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQK-QFIHRDLAARNILVGENYVAKIADFGLSr 840
Cdd:cd06649   89 SLDQVLKEAK----------------RIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVS- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 759191595 841 GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd06649  152 GQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEL 195
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
676-904 1.24e-09

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 61.21  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLAI 755
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVE-ADSLWVVKMFYSFQDKLNLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd05628   81 EFLPGGDMMTLLMKK----------------DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLSRG-----QEVYVKKTMGRLPV-------------------------------RWMAIESLNYSVYTTNSDVWSYGV 879
Cdd:cd05628  145 FGLCTGlkkahRTEFYRNLNHSLPSdftfqnmnskrkaetwkrnrrqlafstvgtpDYIAPEVFMQTGYNKLCDWWSLGV 224
                        250       260
                 ....*....|....*....|....*
gi 759191595 880 LLWEIVsLGGTPYCGMTCAELYEKL 904
Cdd:cd05628  225 IMYEML-IGYPPFCSETPQETYKKV 248
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
724-922 1.30e-09

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: 60.26  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 724 GELEVLCKlghhpNIINLLGACEHRGYLYLAIEYAPHGNLL---DFLRKSRVLEtdpafaIANSTASTLSSQQLLHFAAD 800
Cdd:cd14104   37 GADQVLVK-----KEISILNIARHRNILRLHESFESHEELVmifEFISGVDIFE------RITTARFELNEREIVSYVRQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 801 VARGMDYLSQKQFIHRDLAARNIL--VGENYVAKIADFGLSR----GQEVYVKKTMGRlpvrWMAIESLNYSVYTTNSDV 874
Cdd:cd14104  106 VCEALEFLHSKNIGHFDIRPENIIycTRRGSYIKIIEFGQSRqlkpGDKFRLQYTSAE----FYAPEVHQHESVSTATDM 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 875 WSYGVLLWeiVSLGGT-PYCGMTCAELYEKLpqgyrLEKPLNCDDEVYD 922
Cdd:cd14104  182 WSLGCLVY--VLLSGInPFEAETNQQTIENI-----RNAEYAFDDEAFK 223
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
659-942 1.41e-09

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: 60.83  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 659 KAKNNPDPTIYPVLDWNDIK--FQDV--IGEGNFGQVLKARIKKDGLRMdaAIKRMkEYASKDDH---RDFAGELEVLCK 731
Cdd:cd06635    5 RAGSLKDPDIAELFFKEDPEklFSDLreIGHGSFGAVYFARDVRTSEVV--AIKKM-SYSGKQSNekwQDIIKEVKFLQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 732 LgHHPNIINLLGAC--EHRGYLYLAIEYAPHGNLLDfLRKSRVLETDpafaIANSTASTLssqqllhfaadvaRGMDYLS 809
Cdd:cd06635   82 I-KHPNSIEYKGCYlrEHTAWLVMEYCLGSASDLLE-VHKKPLQEIE----IAAITHGAL-------------QGLAYLH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 810 QKQFIHRDLAARNILVGENYVAKIADFGlsRGQEVYVKKTMGRLPVrWMAIE---SLNYSVYTTNSDVWSYGVllweivs 886
Cdd:cd06635  143 SHNMIHRDIKAGNILLTEPGQVKLADFG--SASIASPANSFVGTPY-WMAPEvilAMDEGQYDGKVDVWSLGI------- 212
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 887 lggtpycgmTCAELYEKLPQGYRL------------EKPLNCDDEVYDLMRQ----CWREKPYERPSFAQIL 942
Cdd:cd06635  213 ---------TCIELAERKPPLFNMnamsalyhiaqnESPTLQSNEWSDYFRNfvdsCLQKIPQDRPTSEELL 275
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
683-892 1.43e-09

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: 60.58  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEH---RGYLyLAIEYAP 759
Cdd:cd13988    1 LGQGATANVFRGRHKKTG--DLYAVKVFNNLSFMRPLDVQMREFEVLKKL-NHKNIVKLFAIEEElttRHKV-LVMELCP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDflrksrVLEtDPafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL--VGEN--YVAKIAD 835
Cdd:cd13988   77 CGSLYT------VLE-EP------SNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDgqSVYKLTD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 836 FGLSR------------GQEVYVKKTMGRLPVRWMAIESLnysvYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd13988  144 FGAAReleddeqfvslyGTEEYLHPDMYERAVLRKDHQKK----YGATVDLWSIGVTFYHAAT-GSLPF 207
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
735-942 1.44e-09

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: 60.41  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGAC-EHRGYLYLAIE--YAPHGNLLdflRKSRVLETDPAFaIANSTASTLSSQQLLHfaaDVARGMDYL-SQ 810
Cdd:cd14011   61 HPRILTVQHPLeESRESLAFATEpvFASLANVL---GERDNMPSPPPE-LQDYKLYDVEIKYGLL---QISEALSFLhND 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 811 KQFIHRDLAARNILVGENYVAKIADFGLS------RGQEVYVKKTMGRLPVrwMAIESLNY--------SVYTTNSDVWS 876
Cdd:cd14011  134 VKLVHGNICPESVVINSNGEWKLAGFDFCisseqaTDQFPYFREYDPNLPP--LAQPNLNYlapeyilsKTCDPASDMFS 211
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 877 YGVLLWEIVSLGGTPY-CGMTCAELYEKLPQGYRLEKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14011  212 LGVLIYAIYNKGKPLFdCVNNLLSYKKNSNQLRQLSLSLleKVPEELRDHVKTLLNVTPEVRPDAEQLS 280
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
682-942 1.94e-09

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: 59.48  E-value: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIK-----RMKEYASKDDHRDFAGE---LEVLCKLGHHPNIINLLGACEHRGYLYL 753
Cdd:cd14101    7 LLGKGGFGTVYAGHRISDGLQV--AIKqisrnRVQQWSKLPGVNPVPNEvalLQSVGGGPGHRGVIRLLDWFEIPEGFLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHG-NLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVG-ENYVA 831
Cdd:cd14101   85 VLERPQHCqDLFDYITERGALDESLA----------------RRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFG--LSRGQEVYVKKTMGRL--PVRWmaIESLNYsvYTTNSDVWSYGVLLWEIVslggtpyCGMTCAELYEKLPQG 907
Cdd:cd14101  149 KLIDFGsgATLKDSMYTDFDGTRVysPPEW--ILYHQY--HALPATVWSLGILLYDMV-------CGDIPFERDTDILKA 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 908 yRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14101  218 -KPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQIL 251
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
683-886 2.26e-09

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 60.35  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMkeyaskddHRDFAGELEV--------LCKLGHHPNIINLLGAcehrgylyla 754
Cdd:cd07880   23 VGSGAYGTVCSALDRRTGAKV--AIKKL--------YRPFQSELFAkrayrelrLLKHMKHENVIGLLDV---------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 ieYAPHGNLLDFLRKSRVLE---TDPAFAIANSTastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd07880   83 --FTPDLSLDRFHDFYLVMPfmgTDLGKLMKHEK---LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCEL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 832 KIADFGLSRGQEvyvKKTMGRLPVRWM-AIES-LNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd07880  158 KILDFGLARQTD---SEMTGYVVTRWYrAPEViLNWMHYTQTVDIWSVGCIMAEMLT 211
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
683-892 2.34e-09

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 60.01  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGlrmdaaikrmKEYASKDDHR--DFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd14092   14 LGDGSFSVCRKCVHKKTG----------QEFAVKIVSRrlDTSREVQLLRLCQGHPNIVKLHEVFQDELHTYLVMELLRG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRK-SRVLEtdpafaianSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADF 836
Cdd:cd14092   84 GELLERIRKkKRFTE---------SEASRIMRQ--------LVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDF 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 837 GLSR-GQEVYVKKTmgrlP---VRWMAIESLNYSV----YTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd14092  147 GFARlKPENQPLKT----PcftLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLS-GQVPF 205
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
681-942 2.49e-09

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 59.20  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKAriKKDGLRMDAAIKRMKEyaSKDDHRDFAGELEVLCKLGHHP-----NIINLLGACEHRGYLYLAI 755
Cdd:cd14133    5 EVLGKGTFGQVVKC--YDLLTGEEVALKIIKN--NKDYLDQSLDEIRLLELLNKKDkadkyHIVRLKDVFYFKNHLCIVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHgNLLDFLRKSRVletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN--YVAKI 833
Cdd:cd14133   81 ELLSQ-NLYEFLKQNKF--------------QYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYsrCQIKI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFG----LSRGQEVYVKKTMGRLPvrwmaiESLNYSVYTTNSDVWSYGVLLWEIVS-----LGGTPYCGMTC-AELYEK 903
Cdd:cd14133  146 IDFGsscfLTQRLYSYIQSRYYRAP------EVILGLPYDEKIDMWSLGCILAELYTgeplfPGASEVDQLARiIGTIGI 219
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 904 LPQgYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14133  220 PPA-HMLDQGKADDELFVDFLKKLLEIDPKERPTASQAL 257
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
683-886 3.33e-09

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: 59.13  E-value: 3.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAaIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRSYAVKL-FKQEKKMQWKKHWKRFLSELEVL-LLFQHPNILELAAYFTETEKFCLVYPYMQNGT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFLRKSRVleTDPafaianstastLSSQQLLHFAADVARGMDYLSQKQ---FIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd14160   79 LFDRLQCHGV--TKP-----------LSWHERINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALA 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759191595 840 RGQEVYVKK-------TMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd14160  146 HFRPHLEDQsctinmtTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT 199
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
673-904 3.39e-09

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 59.86  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWNDIKfqdVIGEGNFGQVLKARIKKDG--LRMDAAIKrmKEYASKDDHRDFAGELEVLCKlGHHPNIINLLGACEHRGY 750
Cdd:cd05629    2 DFHTVK---VIGKGAFGEVRLVQKKDTGkiYAMKTLLK--SEMFKKDQLAHVKAERDVLAE-SDSPWVVSLYYSFQDAQY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 LYLAIEYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 830
Cdd:cd05629   76 LYLIMEFLPGGDLMTMLIKY----------------DTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 831 AKIADFGLSRG-----QEVYVKK-------TMGRLPVRWMAIESLN--------------------YSV----------- 867
Cdd:cd05629  140 IKLSDFGLSTGfhkqhDSAYYQKllqgksnKNRIDNRNSVAVDSINltmsskdqiatwkknrrlmaYSTvgtpdyiapei 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 868 -----YTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKL 904
Cdd:cd05629  220 flqqgYGQECDWWSLGAIMFECL-IGWPPFCSENSHETYRKI 260
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
676-892 3.76e-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: 58.83  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 676 DIKFQDV--IGEGNFGQVLKARIKkdGLRMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGYLYL 753
Cdd:cd14113    6 DSFYSEVaeLGRGRFSVVKKCDQR--GTKRAVATKFVNKKLMKRDQ--VTHELGVLQSL-QHPQLVGLLDTFETPTSYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHGNLLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY---V 830
Cdd:cd14113   81 VLEMADQGRLLDYVVR----------------WGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpT 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 831 AKIADFG--LSRGQEVYVKKTMGRlpVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd14113  145 IKLADFGdaVQLNTTYYIHQLLGS--PEFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPF 205
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
739-942 3.85e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 60.03  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 739 INLLGACEHRGY------------LYLAIEYAPHGNLLDFLrKSRVLETDPafaIANSTASTLSSQQLLhfaadvarGMD 806
Cdd:PTZ00267 116 LHCLAACDHFGIvkhfddfksddkLLLIMEYGSGGDLNKQI-KQRLKEHLP---FQEYEVGLLFYQIVL--------ALD 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 807 YLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGR----LPVrWMAIESLNYSVYTTNSDVWSYGVLLW 882
Cdd:PTZ00267 184 EVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASsfcgTPY-YLAPELWERKRYSKKADMWSLGVILY 262
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 883 EIVSLgGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:PTZ00267 263 ELLTL-HRPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
683-952 3.87e-09

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: 59.29  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKkdGLRMDAAIKRMKEYASkddhrdFAGELEVL-CKLGHHPNIINLLGAcEHRG-----YLYLAIE 756
Cdd:cd14219   13 IGKGRYGEVWMGKWR--GEKVAVKVFFTTEEAS------WFRETEIYqTVLMRHENILGFIAA-DIKGtgswtQLYLITD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLrKSRVLETDPAFAIANSTASTLSSqqlLHFAADVARGMDYLSqkqfiHRDLAARNILVGENYVAKIADF 836
Cdd:cd14219   84 YHENGSLYDYL-KSTTLDTKAMLKLAYSSVSGLCH---LHTEIFSTQGKPAIA-----HRDLKSKNILVKKNGTCCIADL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GL-----SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTN------SDVWSYGVLLWEIVS---LGGT------PYCGMT 896
Cdd:cd14219  155 GLavkfiSDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHfqsyimADMYSFGLILWEVARrcvSGGIveeyqlPYHDLV 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 897 CAE-LYEKLPQGYRLEK----------PLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEER 952
Cdd:cd14219  235 PSDpSYEDMREIVCIKRlrpsfpnrwsSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQ 301
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
725-891 4.13e-09

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: 58.77  E-value: 4.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 725 ELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKsrvletdpafaiaNSTASTLSSQQLLHFAADVarg 804
Cdd:cd14182   59 EIDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTE-------------KVTLSEKETRKIMRALLEV--- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 805 MDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS----RGQEVY-VKKTMGrlpvrWMAIESLNYSV------YTTNSD 873
Cdd:cd14182  123 ICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFScqldPGEKLReVCGTPG-----YLAPEIIECSMddnhpgYGKEVD 197
                        170
                 ....*....|....*...
gi 759191595 874 VWSYGVLLWEIvsLGGTP 891
Cdd:cd14182  198 MWSTGVIMYTL--LAGSP 213
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
682-886 4.19e-09

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: 59.29  E-value: 4.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlrMDAAIKRMKE--YASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05571    2 VLGKGTFGKVILCREKATG--ELYAIKILKKevIIAKDEVAHTLTENRVLQNT-RHPFLTSLKYSFQTNDRLCFVMEYVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPA-FaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd05571   79 GGELFFHLSRERVFSEDRTrF-----------------YGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRGQEVY--VKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd05571  142 CKEEISYgaTTKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 190
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
683-937 5.14e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 58.50  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14138   13 IGSGEFGSVFKCVKRLDGCIY--AIKRSKKpLAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQNEYCNGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV---------------- 825
Cdd:cd14138   91 SLAD------------AISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegded 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 ---GENYVAKIADFG-LSRGQEVYVKKTmgrlPVRWMAIESL--NYSvYTTNSDVWSYGVLLWeiVSLGGTPYcgMTCAE 899
Cdd:cd14138  159 ewaSNKVIFKIGDLGhVTRVSSPQVEEG----DSRFLANEVLqeNYT-HLPKADIFALALTVV--CAAGAEPL--PTNGD 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 759191595 900 LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPS 937
Cdd:cd14138  230 QWHEIRQGKLPRIPQVLSQEFLDLLKVMIHPDPERRPS 267
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
683-884 5.24e-09

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 58.87  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyaSKDDHRDFAG-ELEVLCKLGHHP-----NIINLLGACEHRGYLYLAIE 756
Cdd:cd14226   21 IGKGSFGQVVKAYDHVEQEWV--AIKIIK---NKKAFLNQAQiEVRLLELMNKHDtenkyYIVRLKRHFMFRNHLCLVFE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHgNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQK--QFIHRDLAARNI-LVGENYVA-K 832
Cdd:cd14226   96 LLSY-NLYDLLR--------------NTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENIlLCNPKRSAiK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 833 IADFGLS--RGQEV--YVKKTMGRLPvrwmaiESLNYSVYTTNSDVWSYGVLLWEI 884
Cdd:cd14226  161 IIDFGSScqLGQRIyqYIQSRFYRSP------EVLLGLPYDLAIDMWSLGCILVEM 210
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
677-952 6.21e-09

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: 58.29  E-value: 6.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 677 IKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMkeyASKDDHRDFA--GELEVLCKLGHHPNIINLLGAC-------EH 747
Cdd:cd14036    2 LRIKRVIAEGGFAFVYEAQDVGTG--KEYALKRL---LSNEEEKNKAiiQEINFMKKLSGHPNIVQFCSAAsigkeesDQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 RGYLYLAIEYAPHGNLLDFLRKsrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARNILV 825
Cdd:cd14036   77 GQAEYLLLTELCKGQLVDFVKK-------------VEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GENYVAKIADFGlSRGQEVYVKKTMGRLPVRWMAIESLN---------------YSVYTTN--SDVWSYGVLLWeivslg 888
Cdd:cd14036  144 GNQGQIKLCDFG-SATTEAHYPDYSWSAQKRSLVEDEITrnttpmyrtpemidlYSNYPIGekQDIWALGCILY------ 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 889 gtpycgMTCaelYEKLP--QGYRLeKPLNC------DDEVY----DLMRQCWREKPYERPSFAQILVSLNRMLEER 952
Cdd:cd14036  217 ------LLC---FRKHPfeDGAKL-RIINAkytippNDTQYtvfhDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
683-894 7.20e-09

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: 58.76  E-value: 7.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMkeyaskddHRDFAGEL--------EVLCKLGHHPNIINLL----GACEHRGY 750
Cdd:cd07879   23 VGSGAYGSVCSAIDKRTGEKV--AIKKL--------SRPFQSEIfakrayreLTLLKHMQHENVIGLLdvftSAVSGDEF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 --LYLAIEYaphgnlldflrksrvLETDpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 828
Cdd:cd07879   93 qdFYLVMPY---------------MQTD----LQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNED 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 829 YVAKIADFGLSRGQEVyvkKTMGRLPVRWM-AIES-LNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd07879  154 CELKILDFGLARHADA---EMTGYVVTRWYrAPEViLNWMHYNQTVDIWSVGCIMAEMLT-GKTLFKG 217
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
683-907 7.32e-09

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: 58.74  E-value: 7.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARiKKDGLRMdAAIKRM--KEYASKDDHRDFAGELEVLCK--LGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd05586    1 IGKGTFGQVYQVR-KKDTRRI-YAMKVLskKVIVAKKEVAHTIGERNILVRtaLDESPFIVGLKFSFQTPTDLYLVTDYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRKSRVLETDPA-FAIAnstastlssqqllhfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd05586   79 SGGELFWHLQKEGRFSEDRAkFYIA-----------------ELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFG 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 838 LSRGqEVYVKKTMGRL--PVRWMAIES-LNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG 907
Cdd:cd05586  142 LSKA-DLTDNKTTNTFcgTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCC-GWSPFYAEDTQQMYRNIAFG 212
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
397-475 7.45e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 7.45e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595   397 PPPRGLSLLPKSQTTLNLTWQPIFPSSEDDFYVEVERRSVQMNSDQQNIKVPGNLTSVLLNNLHPREQYVVRARVNTKA 475
Cdd:smart00060   2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
683-886 7.77e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 58.29  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeYASKDDHRDFAGELEV-LCKLGHHPNIINLLGACEHRGYLYLAIEYaphg 761
Cdd:PLN00009  10 IGEGTYGVVYKARDRVTNETI--ALKKIR-LEQEDEGVPSTAIREIsLLKEMQHGNIVRLQDVVHSEKRLYLVFEY---- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 nlLDF-LRKSrvLETDPAFAIANSTASTLSSQQLlhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVA-KIADFGLS 839
Cdd:PLN00009  83 --LDLdLKKH--MDSSPDFAKNPRLIKTYLYQIL--------RGIAYCHSHRVLHRDLKPQNLLIDRRTNAlKLADFGLA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 759191595 840 RGQEVYVKKTMGRLPVRWM-AIESLNYS-VYTTNSDVWSYGVLLWEIVS 886
Cdd:PLN00009 151 RAFGIPVRTFTHEVVTLWYrAPEILLGSrHYSTPVDIWSVGCIFAEMVN 199
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
682-942 9.71e-09

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: 57.34  E-value: 9.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAG-ELEV-LCKLGHHPNIINLLGAC---EHRGyLYLAI 755
Cdd:cd06653    9 LLGRGAFGEVYLCYDADTGREL--AVKQVPfDPDSQETSKEVNAlECEIqLLKNLRHDRIVQYYGCLrdpEEKK-LSIFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYAPHGNLLDFLRksrvletdpAFAIANSTASTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 835
Cdd:cd06653   86 EYMPGGSVKDQLK---------AYGALTENVTRRYTRQIL-------QGVSYLHSNMIVHRDIKGANILRDSAGNVKLGD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 836 FGLS-RGQEVYVK----KTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC-AELYEKLPQGYR 909
Cdd:cd06653  150 FGASkRIQTICMSgtgiKSVTGTPY-WMSPEVISGEGYGRKADVWSVACTVVEMLT-EKPPWAEYEAmAAIFKIATQPTK 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 759191595 910 LEKPLNCDDEVYDLMRQCWREKpYERPSFAQIL 942
Cdd:cd06653  228 PQLPDGVSDACRDFLRQIFVEE-KRRPTAEFLL 259
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
682-930 1.21e-08

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 57.74  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlrmdaaikrmKEYASKDDHR----------DFAGELEVLCKlGHHPNIINLLGACEHRGYL 751
Cdd:cd05597    8 VIGRGAFGEVAVVKLKSTE----------KVYAMKILNKwemlkraetaCFREERDVLVN-GDRRWITKLHYAFQDENYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDFLRK--SRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd05597   77 YLVMDYYCGGDLLTLLSKfeDRLPEEMARF-----------------YLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 830 VAKIADFG----LSRGQEVYVKKTMGR----LPVRWMAIESlNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELY 901
Cdd:cd05597  140 HIRLADFGsclkLREDGTVQSSVAVGTpdyiSPEILQAMED-GKGRYGPECDWWSLGVCMYEML-YGETPFYAESLVETY 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 759191595 902 EKLPQ-GYRLEKPLNCDD---EVYDLMRQ--CWRE 930
Cdd:cd05597  218 GKIMNhKEHFSFPDDEDDvseEAKDLIRRliCSRE 252
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
683-903 1.43e-08

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: 57.71  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARiKKDG--------LRMDAAIKRmKEYASKDDHRDFAGELEvlcklghHPNIINLLGACEHRGYLYLA 754
Cdd:cd05598    9 IGVGAFGEVSLVR-KKDTnalyamktLRKKDVLKR-NQVAHVKAERDILAEAD-------NEWVVKLYYSFQDKENLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 755 IEYAPHGNLLDFLRKSRVLETDPA-FAIAnstastlssqqllhfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 833
Cdd:cd05598   80 MDYIPGGDLMSLLIKKGIFEEDLArFYIA-----------------ELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKL 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 834 ADFGLSRG------QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEK 903
Cdd:cd05598  143 TDFGLCTGfrwthdSKYYLAHSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEML-VGQPPFLAQTPAETQLK 216
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
678-886 1.64e-08

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: 56.85  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGlRMDAAikRMKEYASKDDHRDFAgELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14110    6 AFQTEINRGRFSVVRQCEEKRSG-QMLAA--KIIPYKPEDKQLVLR-EYQVLRRL-SHPRIAQLHSAYLSPRHLVLIEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLdflrksrvletdPAFAIANStastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd14110   81 CSGPELL------------YNLAERNS----YSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759191595 838 ----LSRGQEVYVKKTMGRlpVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:cd14110  145 naqpFNQGKVLMTDKKGDY--VETMAPELLEGQGAGPQTDIWAIGVTAFIMLS 195
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
682-904 2.11e-08

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: 56.92  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQ--VLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAGELeVLCKLGHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd08216    5 EIGKCFKGGgvVHLAKHKPTNTLV--AVKKINlESDSKEDLKFLQQEI-LTSRQLQHPNILPYVTSFVVDNDLYVVTPLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLrKSRVLETDPAFAIANstasTLSsqqllhfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG- 837
Cdd:cd08216   82 AYGSCRDLL-KTHFPEGLPELAIAF----ILR---------DVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRy 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 ----LSRGQEvyvKKTMGRLPVR------WMAIESL--NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELY-EKL 904
Cdd:cd08216  148 aysmVKHGKR---QRVVHDFPKSseknlpWLSPEVLqqNLLGYNEKSDIYSVGITACELAN-GVVPFSDMPATQMLlEKV 223
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
681-942 3.23e-08

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: 55.79  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDdhrdfageLEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd13995   10 DFIPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSD--------VEIQACF-RHENIAELYGALLWEETVHLFMEAGEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIlVGENYVAKIADFGLS- 839
Cdd:cd13995   81 GSVLEKLE----------------SCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNI-VFMSTKAVLVDFGLSv 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 -RGQEVYVKKTMgRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYC-----GMTCAELYEKLPQGYRLEK- 912
Cdd:cd13995  144 qMTEDVYVPKDL-RGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQT-GSPPWVrryprSAYPSYLYIIHKQAPPLEDi 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 759191595 913 PLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd13995  222 AQDCSPAMRELLEAALERNPNHRSSAAELL 251
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
682-942 3.25e-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: 55.86  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEV-LCKLGHHPNIINLLGACEHRGYLYLAI--EYA 758
Cdd:cd06651   14 LLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIqLLKNLQHERIVQYYGCLRDRAEKTLTIfmEYM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLLDFLRksrvletdpAFAIANSTASTLSSQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 838
Cdd:cd06651   94 PGGSVKDQLK---------AYGALTESVTRKYTRQILE-------GMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 SRGQEVYVKKTMGRLPVR----WMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC-AELYEKLPQGYRLEKP 913
Cdd:cd06651  158 SKRLQTICMSGTGIRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAmAAIFKIATQPTNPQLP 236
                        250       260
                 ....*....|....*....|....*....
gi 759191595 914 LNCDDEVYDLMRQCWREKPyERPSFAQIL 942
Cdd:cd06651  237 SHISEHARDFLGCIFVEAR-HRPSAEELL 264
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
682-892 3.31e-08

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: 56.35  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKkdGLRMDAAIKRMKEYA--SKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05591    2 VLGKGSFGKVMLAERK--GTDEVYAIKVLKKDVilQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05591   80 GGDLMFQIQRARKFDEPRA----------------RFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 840 RG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05591  144 KEgiLNGKTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 196
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
683-891 3.66e-08

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: 55.95  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGn 762
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIV--ALKEIHLDAEEGTPSTAIREISLMKEL-KHENIVRLHDVIHTENKLMLVFEYMDKD- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 lldfLRKSRVLETDPAFAIANSTASTLssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 842
Cdd:cd07836   84 ----LKKYMDTHGVRGALDPNTVKSFT--YQLL-------KGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759191595 843 EVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVSlgGTP 891
Cdd:cd07836  151 GIPVNTFSNEVVTLWYRAPDvlLGSRTYSTSIDIWSVGCIMAEMIT--GRP 199
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
683-893 3.89e-08

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: 56.00  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARikKDGlrMDAAIKRMKEYA---SKDDHRDFAGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14157    1 ISEGTFADIYKGY--RHG--KQYVIKRLKETEcesPKSTERFFQTEVQI-CFRCCHPNILPLLGFCVESDCHCLIYPYMP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRvlETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL- 838
Cdd:cd14157   76 NGSLQDRLQQQG--GSHP-----------LPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLr 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 -----SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIvsLGGTPYC 893
Cdd:cd14157  143 lcpvdKKSVYTMMKTKVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEI--LTGIKAM 200
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
682-892 3.99e-08

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 55.82  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlRMdAAIKRMKEYASKDDHRDFAG--ELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05605    7 VLGKGGFGEVCACQVRATG-KM-YACKKLEKKRIKKRKGEAMAlnEKQILEKV-NSRFVVSLAYAYETKDALCLVLTIMN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLldflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05605   84 GGDL--------------KFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLA 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 840 rgqeVYVKK---TMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05605  150 ----VEIPEgetIRGRVgTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIE-GQAPF 201
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
681-942 4.01e-08

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 56.01  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEyaSKDDHRDFAGELEVLCKLGHH-----PNIINLLGACEHRGYLYLAI 755
Cdd:cd14210   19 SVLGKGSFGQVVKCLDHKTG--QLVAIKIIRN--KKRFHQQALVEVKILKHLNDNdpddkHNIVRYKDSFIFRGHLCIVF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 756 EYApHGNLLDFLRKSRvletdpaFAianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA--KI 833
Cdd:cd14210   95 ELL-SINLYELLKSNN-------FQ-------GLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSsiKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLS--RGQEVYVkktmgrlpvrwmAIESLNYSV--------YTTNSDVWSYGVLLWEIVSlgGTP------------ 891
Cdd:cd14210  160 IDFGSScfEGEKVYT------------YIQSRFYRApevilglpYDTAIDMWSLGCILAELYT--GYPlfpgeneeeqla 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 892 ----YCGMTCAELYEKLPQGYR-------------------------LEKPLNCDDEVY-DLMRQCWREKPYERPSFAQI 941
Cdd:cd14210  226 cimeVLGVPPKSLIDKASRRKKffdsngkprpttnskgkkrrpgsksLAQVLKCDDPSFlDFLKKCLRWDPSERMTPEEA 305

                 .
gi 759191595 942 L 942
Cdd:cd14210  306 L 306
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
678-926 4.14e-08

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: 55.77  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGqVLKARIKKDGLRmDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14183    9 KVGRTIGDGNFA-VVKECVERSTGR-EYALKIINKSKCRGKEHMIQNEVSILRRV-KHPNIVLLIEEMDMPTELYLVMEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDflrksrvletdpAFAIANSTASTLSSQQLLHFAAdvarGMDYLSQKQFIHRDLAARNILVGENYVA----KI 833
Cdd:cd14183   86 VKGGDLFD------------AITSTNKYTERDASGMLYNLAS----AIKYLHSLNIVHRDIKPENLLVYEHQDGskslKL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 834 ADFGLSRGQEVYVKKTMGRlPVrWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAE--LYEKLPQGyRLE 911
Cdd:cd14183  150 GDFGLATVVDGPLYTVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRGSGDDQevLFDQILMG-QVD 225
                        250
                 ....*....|....*
gi 759191595 912 KPLNCDDEVYDLMRQ 926
Cdd:cd14183  226 FPSPYWDNVSDSAKE 240
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
678-891 5.66e-08

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: 55.94  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMK---EYASkDDHRdFAGELEVLcKLGHHPNII---NLLGACEHRGY- 750
Cdd:cd07859    3 KIQEVIGKGSYGVVCSAIDTHTGEKV--AIKKINdvfEHVS-DATR-ILREIKLL-RLLRHPDIVeikHIMLPPSRREFk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 751 -LYLAIEyaphgnlldflrksrVLETDPAFAIANSTASTLSSQQLlhFAADVARGMDYLSQKQFIHRDLAARNILVGENY 829
Cdd:cd07859   78 dIYVVFE---------------LMESDLHQVIKANDDLTPEHHQF--FLYQLLRALKYIHTANVFHRDLKPKNILANADC 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 830 VAKIADFGLSRgqeVYVKKTMGRL------PVRWMAIESLN---YSVYTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd07859  141 KLKICDFGLAR---VAFNDTPTAIfwtdyvATRWYRAPELCgsfFSKYTPAIDIWSIGCIFAEV--LTGKP 206
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
673-889 7.92e-08

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: 54.89  E-value: 7.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWndikFQD--VIGEGNFGQVLKARIKKDGlRMDAAIKRMKEYASKddHRDFAG---ELEVLCKLgHHPNIINLLGACEH 747
Cdd:cd05608    1 DW----FLDfrVLGKGGFGEVSACQMRATG-KLYACKKLNKKRLKK--RKGYEGamvEKRILAKV-HSRFIVSLAYAFQT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 748 RGYLYLAIEYAPHGNLLDFLRKsrVLETDPAFaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 827
Cdd:cd05608   73 KTDLCLVMTIMNGGDLRYHIYN--VDEENPGF----------QEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDD 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 828 NYVAKIADFGLSRGQEVYVKKTMGRLPVR-WMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGG 889
Cdd:cd05608  141 DGNVRISDLGLAVELKDGQTKTKGYAGTPgFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARG 203
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
701-885 8.74e-08

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 55.48  E-value: 8.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 701 LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGAcehrgylylaieYAPHGNLLDFLRKSRVLETDPAfA 780
Cdd:cd07874   41 LDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNV------------FTPQKSLEEFQDVYLVMELMDA-N 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 781 IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAI 860
Cdd:cd07874  108 LCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAP 187
                        170       180
                 ....*....|....*....|....*
gi 759191595 861 ESLNYSVYTTNSDVWSYGVLLWEIV 885
Cdd:cd07874  188 EVILGMGYKENVDIWSVGCIMGEMV 212
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
678-896 1.31e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 55.04  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDVIGEGNFGQVLKArIKKDGLRMDAAIKRMKEYASKDDhrdfagELEVLCKLgHHPNIINL--------LGACEHRG 749
Cdd:PTZ00036  69 KLGNIIGNGSFGVVYEA-ICIDTSEKVAIKKVLQDPQYKNR------ELLIMKNL-NHINIIFLkdyyytecFKKNEKNI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAP---HGNLLDFLRKSRVLetdPAFAIanstasTLSSQQLlhfaadvARGMDYLSQKQFIHRDLAARNILVG 826
Cdd:PTZ00036 141 FLNVVMEFIPqtvHKYMKHYARNNHAL---PLFLV------KLYSYQL-------CRALAYIHSKFICHRDLKPQNLLID 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 827 EN-YVAKIADFGLSR----GQE--VYVKKTMGRLPVrwMAIESLNysvYTTNSDVWSYGVLLWEIVsLGGTPYCGMT 896
Cdd:PTZ00036 205 PNtHTLKLCDFGSAKnllaGQRsvSYICSRFYRAPE--LMLGATN---YTTHIDLWSLGCIIAEMI-LGYPIFSGQS 275
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
683-840 1.34e-07

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 54.89  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARiKKDGLRMdAAIKRMK--EYASKDDHRDFAGELEVLCkLGHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:cd05610   12 ISRGAFGKVYLGR-KKNNSKL-YAVKVVKkaDMINKNMVHQVQAERDALA-LSKSPFIVHLYYSLQSANNVYLVMEYLIG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 840
Cdd:cd05610   89 GDVKSLLHIYGYFDEEMA----------------VKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSK 152
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
701-909 1.35e-07

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: 54.67  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 701 LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGAcehrgylylaieYAPHGNLLDFLRKSRVLETDPAfA 780
Cdd:cd07875   48 LERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNV------------FTPQKSLEEFQDVYIVMELMDA-N 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 781 IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAI 860
Cdd:cd07875  115 LCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAP 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595 861 ESLNYSVYTTNSDVWSYGVLLWEIVSLG----GTPYC----------GMTCAELYEKLPQGYR 909
Cdd:cd07875  195 EVILGMGYKENVDIWSVGCIMGEMIKGGvlfpGTDHIdqwnkvieqlGTPCPEFMKKLQPTVR 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
683-892 1.71e-07

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: 53.45  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQvlkARIKKDglRMDAAIKRMKeYASKDDHRDFAGELEVLCKLG-HHPNIINLLGACEHRGYLYLAIEYAPHG 761
Cdd:cd14665    8 IGSGNFGV---ARLMRD--KQTKELVAVK-YIERGEKIDENVQREIINHRSlRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 762 NLLDflrksrvletdpafAIANstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA--KIADFGLS 839
Cdd:cd14665   82 ELFE--------------RICN--AGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPrlKICDFGYS 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 840 RGQEVYV--KKTMGRlPVrWMAIESLNYSVYTTN-SDVWSYGVLLWeIVSLGGTPY 892
Cdd:cd14665  146 KSSVLHSqpKSTVGT-PA-YIAPEVLLKKEYDGKiADVWSCGVTLY-VMLVGAYPF 198
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
673-894 2.34e-07

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: 52.98  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 673 DWNDIkfQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRdfagELEVLCKLgHHPNIINLLGACEHRGYLY 752
Cdd:cd14108    2 DYYDI--HKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARR----ELALLAEL-DHKSIVRFHDAFEKRRVVI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 753 LAIEYAPHGNLLDFLRKSRVLETDPAFAIanstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILV---GENY 829
Cdd:cd14108   75 IVTELCHEELLERITKRPTVCESEVRSYM----------RQLLE-------GIEYLHQNDVLHLDLKPENLLMadqKTDQ 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 830 VaKIADFG----LSRGQEVYVKKTMGrlpvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd14108  138 V-RICDFGnaqeLTPNEPQYCKYGTP----EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLT-GISPFVG 200
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
701-885 2.47e-07

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: 53.88  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 701 LRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGAcehrgylylaieYAPHGNLLDFLRKSRVLETDPAfA 780
Cdd:cd07876   45 LGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNV------------FTPQKSLEEFQDVYLVMELMDA-N 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 781 IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAI 860
Cdd:cd07876  112 LCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAP 191
                        170       180
                 ....*....|....*....|....*
gi 759191595 861 ESLNYSVYTTNSDVWSYGVLLWEIV 885
Cdd:cd07876  192 EVILGMGYKENVDIWSVGCIMGELV 216
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
683-892 3.22e-07

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 52.85  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKD-----------GLRMDAAIKRmkeyaSKDDHRDFagelevlcklgHHPNIINLLGACEHRGYL 751
Cdd:cd14662    8 IGSGNFGVARLMRNKETkelvavkyierGLKIDENVQR-----EIINHRSL-----------RHPNIIRFKEVVLTPTHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDflrksRVletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA 831
Cdd:cd14662   72 AIVMEYAAGGELFE-----RI-----------CNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAP 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 832 --KIADFGLSRGQEVYV--KKTMGRlPVrWMAIESLNYSVYTTN-SDVWSYGVLLWeIVSLGGTPY 892
Cdd:cd14662  136 rlKICDFGYSKSSVLHSqpKSTVGT-PA-YIAPEVLSRKEYDGKvADVWSCGVTLY-VMLVGAYPF 198
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
682-885 3.58e-07

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: 53.19  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKAriKKDGLRMDAAIKRMKE-----YASKDDHRDFageleVLCKLGHHPNIINLLGAcehrgylylaie 756
Cdd:cd07850    7 PIGSGAQGIVCAA--YDTVTGQNVAIKKLSRpfqnvTHAKRAYREL-----VLMKLVNHKNIIGLLNV------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRKSRVLEtdpaFAIANSTastlssqQLLHFAADVAR----------GMDYLSQKQFIHRDLAARNILVG 826
Cdd:cd07850   68 FTPQKSLEEFQDVYLVME----LMDANLC-------QVIQMDLDHERmsyllyqmlcGIKHLHSAGIIHRDLKPSNIVVK 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 827 ENYVAKIADFGLSRGQEV------YVKKTMGRLPvrwMAIESLNYSvytTNSDVWSYGVLLWEIV 885
Cdd:cd07850  137 SDCTLKILDFGLARTAGTsfmmtpYVVTRYYRAP---EVILGMGYK---ENVDIWSVGCIMGEMI 195
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
672-894 3.79e-07

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: 52.59  E-value: 3.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 672 LDWNDIkfQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDfagELEVLCKLgHHPNIINLLGACEHRGYL 751
Cdd:cd14114    1 YDHYDI--LEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRK---EIQIMNQL-HHPKLINLHDAFEDDNEM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEYAPHGNLLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL--VGENY 829
Cdd:cd14114   75 VLILEFLSGGELFE-----RIAAEH----------YKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMctTKRSN 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 830 VAKIADFGLSRG---QEVyVKKTMGrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 894
Cdd:cd14114  140 EVKLIDFGLATHldpKES-VKVTTG--TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLS-GLSPFAG 203
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
639-892 4.64e-07

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 53.15  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 639 FQNREEPTVQFNSGtLALNRKaknnpdptiypvlDWNDIKfqdVIGEGNFGQVLKARIKKDglRMDAAIKRMK--EYASK 716
Cdd:cd05596    7 FLNRYEKPVNEITK-LRMNAE-------------DFDVIK---VIGRGAFGEVQLVRHKST--KKVYAMKLLSkfEMIKR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 717 DDHRDFAGELEVLCklghHPN---IINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqq 793
Cdd:cd05596   68 SDSAFFWEERDIMA----HANsewIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARF-------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 794 llhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG---------LSR-----GQEVY----VKKTMGRlpv 855
Cdd:cd05596  130 ---YTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGtcmkmdkdgLVRsdtavGTPDYispeVLKSQGG--- 203
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 759191595 856 rwmaieslnYSVYTTNSDVWSYGVLLWEIVsLGGTPY 892
Cdd:cd05596  204 ---------DGVYGRECDWWSVGVFLYEML-VGDTPF 230
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
126-171 4.74e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 47.35  E-value: 4.74e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 759191595 126 NGVCHEDTGECICPPGFMGRTCEKaCELHTFGRTckercSGPEGCK 171
Cdd:cd00055   11 SGQCDPGTGQCECKPNTTGRRCDR-CAPGYYGLP-----SQGGGCQ 50
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
683-886 4.99e-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: 52.76  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARiKKDGlrmdaaiKRMKEYASKDDH-----RDFAGELEVLCKLgHHPNIINL----LGACEHRgyLYL 753
Cdd:cd07867   10 VGRGTYGHVYKAK-RKDG-------KDEKEYALKQIEgtgisMSACREIALLREL-KHPNVIALqkvfLSHSDRK--VWL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 754 AIEYAPHG--NLLDFLRKSRvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV----GE 827
Cdd:cd07867   79 LFDYAEHDlwHIIKFHRASK----------ANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 828 NYVAKIADFGLSRGQEVYVKKTMGRLPVR---WMAIESLNYSV--YTTNSDVWSYGVLLWEIVS 886
Cdd:cd07867  149 RGRVKIADMGFARLFNSPLKPLADLDPVVvtfWYRAPELLLGArhYTKAIDIWAIGCIFAELLT 212
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
793-899 6.43e-07

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 52.00  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 793 QLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIES--LNYSVYTT 870
Cdd:cd07844  106 QLL-------RGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYSNEVVTLWYRPPDvlLGSTEYST 178
                         90       100       110
                 ....*....|....*....|....*....|
gi 759191595 871 NSDVWSYGVLLWEIVSlgGTP-YCGMTCAE 899
Cdd:cd07844  179 SLDMWGVGCIFYEMAT--GRPlFPGSTDVE 206
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
680-951 8.58e-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: 51.74  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 680 QDVIGEGNFGQVLKARIKKDGLRmdAAIKRMKeyaskddHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd13991   11 QLRIGRGSFGEVHRMEDKQTGFQ--CAVKKVR-------LEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN-YVAKIADFGL 838
Cdd:cd13991   82 GGSLGQLIKEQGCLPEDRA----------------LHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGH 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 839 S-RGQEVYVKKTMGRLPV-----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL---PQGYR 909
Cdd:cd13991  146 AeCLDPDGLGKSLFTGDYipgteTHMAPEVVLGKPCDAKVDVWSSCCMMLHMLN-GCHPWTQYYSGPLCLKIanePPPLR 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 910 lEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEE 951
Cdd:cd13991  225 -EIPPSCAPLTAQAIQAGLRKEPVHRASAAELRRKTNRALQE 265
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
683-947 8.67e-07

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: 52.17  E-value: 8.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAgELEVLCKL-GHHPNIINLLGACEHRG------------ 749
Cdd:cd13977    8 VGRGSYGVVYEAVVRRTGARV--AVKKIRCNAPENVELALR-EFWALSSIqRQHPNVIQLEECVLQRDglaqrmshgssk 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 ------------------------YLYLAIEYAPHGNLLDFLrksrvLETDPAFAIANSTASTLSSqqllhfaadvarGM 805
Cdd:cd13977   85 sdlylllvetslkgercfdprsacYLWFVMEFCDGGDMNEYL-----LSRRPDRQTNTSFMLQLSS------------AL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 806 DYLSQKQFIHRDLAARNILVGENY---VAKIADFGLSRgqevyVKKTMGRLPVRWMAIESLNYSV--------------- 867
Cdd:cd13977  148 AFLHRNQIVHRDLKPDNILISHKRgepILKVADFGLSK-----VCSGSGLNPEEPANVNKHFLSSacgsdfymapevweg 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 868 -YTTNSDVWSYGVLLWEIVS-------------LGGTPYCGMTCAELYEKLPQGYRLE------KPLNCDDEVYDLMRQC 927
Cdd:cd13977  223 hYTAKADIFALGIIIWAMVEritfrdgetkkelLGTYIQQGKEIVPLGEALLENPKLElqiplkKKKSMNDDMKQLLRDM 302
                        330       340
                 ....*....|....*....|
gi 759191595 928 WREKPYERPSFAQILVSLNR 947
Cdd:cd13977  303 LAANPQERPDAFQLELRLRQ 322
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
735-891 9.99e-07

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: 51.50  E-value: 9.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEHRGYLYLAIEYaphgnlldflrksrvLETDPAFAIANSTAStLSSQQLLHFAADVARGMDYLSQKQFI 814
Cdd:cd07870   57 HANIVLLHDIIHTKETLTFVFEY---------------MHTDLAQYMIQHPGG-LHPYNVRLFMFQLLRGLAYIHGQHIL 120
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 815 HRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIES--LNYSVYTTNSDVWSYGVLLWEIVSlgGTP 891
Cdd:cd07870  121 HRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVVTLWYRPPDvlLGATDYSSALDIWGAGCIFIEMLQ--GQP 197
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
682-942 1.11e-06

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: 51.20  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDF-AGELEV-LCKLGHHPNIINLLGACEHRGYLYLAI--E 756
Cdd:cd06652    9 LLGQGAFGRVYLCYDADTGREL--AVKQVQfDPESPETSKEVnALECEIqLLKNLLHERIVQYYGCLRDPQERTLSIfmE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHGNLLDFLRksrvletdpAFAIANSTASTLSSQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 836
Cdd:cd06652   87 YMPGGSIKDQLK---------SYGALTENVTRKYTRQILE-------GVHYLHSNMIVHRDIKGANILRDSVGNVKLGDF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 837 GLSRGQEVYVKKTMGRLPVR----WMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC-AELYEKLPQGYRLE 911
Cdd:cd06652  151 GASKRLQTICLSGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT-EKPPWAEFEAmAAIFKIATQPTNPQ 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 759191595 912 KPLNCDDEVYDLMRQCWREKPyERPSFAQIL 942
Cdd:cd06652  230 LPAHVSDHCRDFLKRIFVEAK-LRPSADELL 259
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
735-886 1.29e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 51.80  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 735 HPNIINLLGACEHRGYLYLAIeyaPH--GNLLDFL-RKSRVLETDPAFAIanstastlsSQQLLhfaadvaRGMDYLSQK 811
Cdd:PHA03209 116 HPSVIRMKDTLVSGAITCMVL---PHysSDLYTYLtKRSRPLPIDQALII---------EKQIL-------EGLRYLHAQ 176
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 812 QFIHRDLAARNILVGENYVAKIADFGLSRGqEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 886
Cdd:PHA03209 177 RIIHRDVKTENIFINDVDQVCIGDLGAAQF-PVVAPAFLGLAgTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
682-891 1.72e-06

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; 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 DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 51.29  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKdgLRMDAAIKRMKEyaSKDDHRDFAGELEVLCKLGHHP-----NIINLLGACEHRGYLYLAIE 756
Cdd:cd14224   72 VIGKGSFGQVVKAYDHK--THQHVALKMVRN--EKRFHRQAAEEIRILEHLKKQDkdntmNVIHMLESFTFRNHICMTFE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHgNLLDFLRKSRVletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA--KIA 834
Cdd:cd14224  148 LLSM-NLYELIKKNKF--------------QGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSgiKVI 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 835 DFGLS--RGQEVY--VKKTMGRLPvrwmaiESLNYSVYTTNSDVWSYGVLLWEIvsLGGTP 891
Cdd:cd14224  213 DFGSScyEHQRIYtyIQSRFYRAP------EVILGARYGMPIDMWSFGCILAEL--LTGYP 265
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
682-892 1.76e-06

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 51.27  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDglRMDAAIKRMK-EYASKDDHRDFA-GELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd05588    2 VIGRGSYAKVLMVELKKT--KRIYAMKVIKkELVNDDEDIDWVqTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:cd05588   80 GGDLMFHMQRQRRLPEEHA----------------RFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMC 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759191595 840 R-----GQevyVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd05588  144 KeglrpGD---TTSTFCGTP-NYIAPEILRGEDYGFSVDWWALGVLMFEMLA-GRSPF 196
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
683-942 1.83e-06

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 50.27  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRdfagELEVLCKLGHhPNIINLLGACEHRGYLYLAIEYAPHGN 762
Cdd:cd14107   10 IGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQ----ERDILARLSH-RRLTCLLDQFETRKTLILILELCSSEE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 763 LLDFL-RKSRVLETDPAFAIanstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGLS 839
Cdd:cd14107   85 LLDRLfLKGVVTEAEVKLYI----------QQVLE-------GIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 840 rgQEVyvkkTMGRLPV------RWMAIESLNYSVYTTNSDVWSYGVLLWeiVSLG-GTPYCG-------MTCAE--LYEK 903
Cdd:cd14107  148 --QEI----TPSEHQFskygspEFVAPEIVHQEPVSAATDIWALGVIAY--LSLTcHSPFAGendratlLNVAEgvVSWD 219
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 759191595 904 LPQGYRLEkplncdDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14107  220 TPEITHLS------EDAKDFIKRVLQPDPEKRPSASECL 252
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
683-941 1.99e-06

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 50.37  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDD--HRDFAGELEVLCKLGHHpNIINLLGACEHR-GYLYLAIEYAP 759
Cdd:cd14163    8 IGEGTYSKVKEAFSKKHQRKV--AIKIIDKSGGPEEfiQRFLPRELQIVERLDHK-NIIHVYEMLESAdGKIYLVMELAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFlrksrVLETDPafaIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVgENYVAKIADFG-- 837
Cdd:cd14163   85 DGDVFDC-----VLHGGP---LPEHRAKALFRQ--------LVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGfa 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 838 --LSRGQEVYVKKTMGRlpVRWMAIESLNYSVY-TTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 914
Cdd:cd14163  148 kqLPKGGRELSQTFCGS--TAYAAPEVLQGVPHdSRKGDIWSMGVVLY-VMLCAQLPFDDTDIPKMLCQQQKGVSLPGHL 224
                        250       260
                 ....*....|....*....|....*..
gi 759191595 915 NCDDEVYDLMRQCWREKPYERPSFAQI 941
Cdd:cd14163  225 GVSRTCQDLLKRLLEPDMVLRPSIEEV 251
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
679-906 2.18e-06

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: 50.21  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 679 FQDVIGEGNFGQVLKARIKKDGLRMDAAIKrmkEYASKDDHRDFAgELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 758
Cdd:cd14111    7 FLDEKARGRFGVIRRCRENATGKNFPAKIV---PYQAEEKQGVLQ-EYEILKSL-HHERIMALHEAYITPRYLVLIAEFC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 759 PHGNLL-DFLRKSRVLETDPAFAIAnstastlssqQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 837
Cdd:cd14111   82 SGKELLhSLIDRFRYSEDDVVGYLV----------QIL-------QGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759191595 838 LSRGQEVYVKKTMGRL--PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYcgmtcaelYEKLPQ 906
Cdd:cd14111  145 SAQSFNPLSLRQLGRRtgTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLS-GRSPF--------EDQDPQ 206
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
682-942 3.00e-06

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: 49.95  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGLRMdaAIK-----RMKEYASkddhrdFAG-----ELEVLCKLGH-HPNIINLLGACEH-RG 749
Cdd:cd14102    7 VLGSGGFGTVYAGSRIADGLPV--AVKhvvkeRVTEWGT------LNGvmvplEIVLLKKVGSgFRGVIKLLDWYERpDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 750 YLYLAIEYAPHGNLLDFLRKSRVLETDPAFAianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILV---- 825
Cdd:cd14102   79 FLIVMERPEPVKDLFDFITEKGALDEDTARG----------------FFRQVLEAVRHCYSCGVVHRDIKDENLLVdlrt 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 GEnyvAKIADFGLSR--GQEVYVKKTMGRL--PVRWmaiesLNYSVYTTNS-DVWSYGVLLWEIVslggtpyCGMTCAEL 900
Cdd:cd14102  143 GE---LKLIDFGSGAllKDTVYTDFDGTRVysPPEW-----IRYHRYHGRSaTVWSLGVLLYDMV-------CGDIPFEQ 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 759191595 901 YEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14102  208 DEEILRG-RLYFRRRVSPECQQLIKWCLSLRPSDRPTLEQIF 248
pknD PRK13184
serine/threonine-protein kinase PknD;
683-892 3.10e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 51.31  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 760
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRV--ALKKIREDLSENPllKKRFLREAKIAADL-IHPGIVPVYSICSDGDPVYYTMPYIEG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 761 GNLLDFLRKSRVLETDPA-FAIANSTASTLSsqqLLHfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 839
Cdd:PRK13184  87 YTLKSLLKSVWQKESLSKeLAEKTSVGAFLS---IFH---KICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759191595 840 RGQE----------------VYVKKT-MGRL--PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLgGTPY 892
Cdd:PRK13184 161 IFKKleeedlldidvderniCYSSMTiPGKIvgTPDYMAPERLLGVPASESTDIYALGVILYQMLTL-SFPY 231
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
682-942 3.24e-06

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 49.71  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKArIKkdglRMDA---AIKR-MKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 757
Cdd:cd14051    7 KIGSGEFGSVYKC-IN----RLDGcvyAIKKsKKPVAGSVDEQNALNEVYAHAVLGKHPHVVRYYSAWAEDDHMIIQNEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHGNLLDFLRksrvletdpafaiANSTASTLSS-----QQLLHfaadVARGMDYLSQKQFIHRDLAARNILV------- 825
Cdd:cd14051   82 CNGGSLADAIS-------------ENEKAGERFSeaelkDLLLQ----VAQGLKYIHSQNLVHMDIKPGNIFIsrtpnpv 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 826 -----------------GENYVAKIADFG-LSRGQEVYVKKTmgrlPVRWMAIESL--NYSvYTTNSDVWSYGVLLWEIV 885
Cdd:cd14051  145 sseeeeedfegeednpeSNEVTYKIGDLGhVTSISNPQVEEG----DCRFLANEILqeNYS-HLPKADIFALALTVYEAA 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 759191595 886 SLGGTPYCGmtcaELYEKLPQGYRLEKPlNCDDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:cd14051  220 GGGPLPKNG----DEWHEIRQGNLPPLP-QCSPEFNELLRSMIHPDPEKRPSAAALL 271
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
683-884 3.85e-06

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 49.91  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRmDAAIK--R----MKEYASKddhrdfagELEVLCKL-GHHPN----IINLLGACEHRGYL 751
Cdd:cd14135    8 LGKGVFSNVVRARDLARGNQ-EVAIKiiRnnelMHKAGLK--------ELEILKKLnDADPDdkkhCIRLLRHFEHKNHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 752 YLAIEyAPHGNLLDFLRKsrvLETDPAFAIansTASTLSSQQLlhFAAdvargMDYLSQKQFIHRDLAARNILVGENY-V 830
Cdd:cd14135   79 CLVFE-SLSMNLREVLKK---YGKNVGLNI---KAVRSYAQQL--FLA-----LKHLKKCNILHADIKPDNILVNEKKnT 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 759191595 831 AKIADFG---LSRGQEV--YVKKTMGRLPvrwMAIESLNYSvytTNSDVWSYGVLLWEI 884
Cdd:cd14135  145 LKLCDFGsasDIGENEItpYLVSRFYRAP---EIILGLPYD---YPIDMWSVGCTLYEL 197
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
683-886 4.17e-06

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: 50.06  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYA-SKDDHRDFAgelevLCKLGHHPNIINL----LGACEHRgyLYLAIEY 757
Cdd:cd07868   25 VGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGiSMSACREIA-----LLRELKHPNVISLqkvfLSHADRK--VWLLFDY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 758 APHG--NLLDFLRKSRvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV----GENYVA 831
Cdd:cd07868   98 AEHDlwHIIKFHRASK----------ANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRV 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 832 KIADFGLSRGQEVYVKKTMGRLPVR---WMAIESLNYSV--YTTNSDVWSYGVLLWEIVS 886
Cdd:cd07868  168 KIADMGFARLFNSPLKPLADLDPVVvtfWYRAPELLLGArhYTKAIDIWAIGCIFAELLT 227
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
126-170 5.21e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 44.22  E-value: 5.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 759191595   126 NGVCHEDTGECICPPGFMGRTCEKaCELHTFGRTckercsgPEGC 170
Cdd:smart00180  10 SGTCDPDTGQCECKPNVTGRRCDR-CAPGYYGDG-------PPGC 46
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
681-894 5.47e-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: 49.64  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 681 DVIGEGNFGQVLKARikKDGLRMDAAIKRMKEYASKddHRDFAGELEVLCKLGHHP----NIINLLGACEHRGYLYLAIE 756
Cdd:cd14229    6 DFLGRGTFGQVVKCW--KRGTNEIVAVKILKNHPSY--ARQGQIEVGILARLSNENadefNFVRAYECFQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPHgNLLDFLRKSRVletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL----VGENYVAK 832
Cdd:cd14229   82 MLEQ-NLYDFLKQNKF--------------SPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVK 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759191595 833 IADFGLSRgqevYVKKTMGR--LPVRWM-AIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCG 894
Cdd:cd14229  147 VIDFGSAS----HVSKTVCStyLQSRYYrAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 206
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
683-942 6.12e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 50.51  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  683 IGEGNFGQVLKARIKKDG---LRMDAAIKRMKEyaskDDHRDFAGELEVLCKLgHHPNIINLLGACEHRG--YLYLAIEY 757
Cdd:PTZ00266   21 IGNGRFGEVFLVKHKRTQeffCWKAISYRGLKE----REKSQLVIEVNVMREL-KHKNIVRYIDRFLNKAnqKLYILMEF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  758 APHGNLLDFLRKSRVLetdpaFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY-------- 829
Cdd:PTZ00266   96 CDAGDLSRNIQKCYKM-----FGKIEEHAIVDITRQLLHALAYCHNLKDGPNGERVLHRDLKPQNIFLSTGIrhigkita 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595  830 ---------VAKIADFGLSR--GQEVYVKKTMGRlPVRWmAIESLNYSV--YTTNSDVWSYGVLLWEIVSlGGTPYC-GM 895
Cdd:PTZ00266  171 qannlngrpIAKIGDFGLSKniGIESMAHSCVGT-PYYW-SPELLLHETksYDDKSDMWALGCIIYELCS-GKTPFHkAN 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 759191595  896 TCAELYEKLPQGYRLekPLNC-DDEVYDLMRQCWREKPYERPSFAQIL 942
Cdd:PTZ00266  248 NFSQLISELKRGPDL--PIKGkSKELNILIKNLLNLSAKERPSALQCL 293
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
678-886 7.00e-06

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: 49.39  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 678 KFQDV--IGEGNFGQVLKARIKKDGLRMdaAIKRMkeyASKDDH--RDFAGELEVLCKLgHHPNIINL---LGACEHR-- 748
Cdd:cd07854    6 RYMDLrpLGCGSNGLVFSAVDSDCDKRV--AVKKI---VLTDPQsvKHALREIKIIRRL-DHDNIVKVyevLGPSGSDlt 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 749 ---------GYLYLAIEYaphgnlldflrksrvLETDPAFAIANSTastLSSQQLLHFAADVARGMDYLSQKQFIHRDLA 819
Cdd:cd07854   80 edvgsltelNSVYIVQEY---------------METDLANVLEQGP---LSEEHARLFMYQLLRGLKYIHSANVLHRDLK 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759191595 820 ARNILVG-ENYVAKIADFGLSRGQEV-YVKK---TMGrLPVRWMAIESLNYSV--YTTNSDVWSYGVLLWEIVS 886
Cdd:cd07854  142 PANVFINtEDLVLKIGDFGLARIVDPhYSHKgylSEG-LVTKWYRSPRLLLSPnnYTKAIDMWAAGCIFAEMLT 214
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
123-148 7.84e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 7.84e-06
                         10        20
                 ....*....|....*....|....*...
gi 759191595 123 CMNNGVCHEDTG--ECICPPGFMGRTCE 148
Cdd:cd00054   11 CQNGGTCVNTVGsyRCSCPPGYTGRNCE 38
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
223-294 8.40e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 8.40e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759191595   223 CKASGWPLPaneEMTLVKPDGTVLHPKD-FNHTGHLSVATFTIHRILPPDSGVWVCSVNTVAGMVEKPFNISV 294
Cdd:smart00410  16 CEASGSPPP---EVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
683-884 9.33e-06

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: 48.47  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 683 IGEGNFGQVLKARIKKDgLRMDAA-----IKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAI-E 756
Cdd:cd13990    8 LGKGGFSEVYKAFDLVE-QRYVACkihqlNKDWSEEKKQNYIKHALREYEIHKSL-DHPRIVKLYDVFEIDTDSFCTVlE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 757 YAPhGNLLDF-LRKSRVLETDPAFAIAnstastlssqqllhfaADVARGMDYLSQKQ--FIHRDLAARNILVGENYVA-- 831
Cdd:cd13990   86 YCD-GNDLDFyLKQHKSIPEREARSII----------------MQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVSge 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 832 -KIADFGLSR--GQEVYVKKTM--------------------GRLPVRwmaIESlnysvyttNSDVWSYGVLLWEI 884
Cdd:cd13990  149 iKITDFGLSKimDDESYNSDGMeltsqgagtywylppecfvvGKTPPK---ISS--------KVDVWSVGVIFYQM 213
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
682-892 1.05e-05

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 48.10  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 682 VIGEGNFGQVLKARIKKDGlrmdaAIKRMKEYASKDDH--RDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 759
Cdd:cd14088    8 VIKTEEFCEIFRAKDKTTG-----KLYTCKKFLKRDGRkvRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759191595 760 HGNLLDFLrksrvleTDPAFAIANSTASTLssQQLLHFAAdvargmdYLSQKQFIHRDLAARNILVG---ENYVAKIADF 836
Cdd:cd14088   83 GREVFDWI-------LDQGYYSERDTSNVI--RQVLEAVA-------YLHSLKIVHRNLKLENLVYYnrlKNSKIVISDF 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759191595 837 GLSRGQEVYVKKTMGRlPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 892
Cdd:cd14088  147 HLAKLENGLIKEPCGT-P-EYLAPEVVGRQRYGRPVDCWAIGVIMYILLS-GNPPF 199
 
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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