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Conserved domains on  [gi|1034639258|ref|XP_016863481|]
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cyclin-G-associated kinase isoform X17 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 291-453 1.66e-122

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein 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 a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with 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.


:

Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 375.01  E-value: 1.66e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  291 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 370
Cdd:cd14564      1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  371 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 450
Cdd:cd14564     81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                   ...
gi 1034639258  451 CDM 453
Cdd:cd14564    161 CDM 163
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 46-211 1.00e-104

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14036:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 282  Bit Score: 332.17  E-value: 1.00e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd14036     87 LCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDY 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  126 SWSAQRRALVEEE------------------------------ALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQ 175
Cdd:cd14036    167 SWSAQKRSLVEDEitrnttpmyrtpemidlysnypigekqdiwALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQ 246

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034639258  176 YTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAAR 211
Cdd:cd14036    247 YTVFHDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 461-599 1.51e-35

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 131.63  E-value: 1.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  461 PHSKPILVRAVVMTPVPLFsKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARS 540
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  541 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 599
Cdd:pfam10409   80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1195-1239 1.10e-07

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


:

Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 49.47  E-value: 1.10e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258 1195 PEQVKKHYRRAVLAVHPDKAAGQPYeqhAKMIFMELNDAWSEFEN 1239
Cdd:cd06257     14 DEEIKKAYRKLALKYHPDKNPDDPE---AEEKFKEINEAYEVLSD 55
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 730-1060 1.07e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  730 EGQEPRADPEPPGLAAGLVQQdlvfevETPAVLPEPVPqedgvdllglHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPP 809
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP------PPPPPTPEPAP----------HALVSATPLPPGPAAARQASPALPAAPAPPAV 2744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  810 EAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPS 889
Cdd:PHA03247  2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  890 AHSAPPPSCSAdflhlgdlPGEPSKMTASSSNPDLLGGWAAwtetAASAVAPTPATEGPLFSPGGQPAPCGSQ-ASWTKS 968
Cdd:PHA03247  2825 AGPLPPPTSAQ--------PTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS 2892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  969 QNPDPFADLGDLSSGLQDPQAQS----TVSPRGQRVCTCSRRLPTGKLKPGVADTGTAASPHRHCGSPA----GFPPGGF 1040
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgALVPGRV 2972

                          330       340
                   ....*....|....*....|
gi 1034639258 1041 IPKTATTPKGSSSWQTSRPP 1060
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAPASS 2992
PHA03321 super family cl33724
tegument protein VP11/12; Provisional
 600-854 8.94e-03

tegument protein VP11/12; Provisional


The actual alignment was detected with superfamily member PHA03321:

Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 40.33  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  600 VEPRDRPSREAPPWENSSMRGLNPKILFSSReeqqdilskfgkPELPRQPGSTAQY--DAGAGSPEAEPTDSDSPPSSSa 677
Cdd:PHA03321   458 RRARAQRARDAGPEYVDPLGALRRLPAGAAP------------PPEPAAAPSPATYytRMGGGPPRLPPRNRATETLRP- 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  678 dasrflhtlDWQEEKEAEtgaenaSSKESESALMEDRDESEVSDEGGSPISSEGQE-PRADPEPPGLAAGLVQQDLVFEV 756
Cdd:PHA03321   525 ---------DWGPPAAAP------PEQMEDPYLEPDDDRFDRRDGAAAAATSHPREaPAPDDDPIYEGVSDSEEPVYEEI 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  757 ETPAVLPEPVPQedgvdllglhSEVGAGPAVPPQACKAPSSNTDLL------SCLLGPPEAASQGPPEdllsedplLLAS 830
Cdd:PHA03321   590 PTPRVYQNPLPR----------PMEGAGEPPDLDAPTSPWVEEENPiygwgdSPLFSPPPAARFPPPD--------PALS 651

                          250       260
                   ....*....|....*....|....
gi 1034639258  831 PAPPLSVQSTPRggpPAAADPFGP 854
Cdd:PHA03321   652 PEPPALPAHRPR---PGALAPDGP 672
 
Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 291-453 1.66e-122

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein 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 a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with 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.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 375.01  E-value: 1.66e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  291 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 370
Cdd:cd14564      1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  371 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 450
Cdd:cd14564     81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                   ...
gi 1034639258  451 CDM 453
Cdd:cd14564    161 CDM 163
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 46-211 1.00e-104

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: 332.17  E-value: 1.00e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd14036     87 LCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDY 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  126 SWSAQRRALVEEE------------------------------ALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQ 175
Cdd:cd14036    167 SWSAQKRSLVEDEitrnttpmyrtpemidlysnypigekqdiwALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQ 246

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034639258  176 YTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAAR 211
Cdd:cd14036    247 YTVFHDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 461-599 1.51e-35

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 131.63  E-value: 1.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  461 PHSKPILVRAVVMTPVPLFsKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARS 540
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  541 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 599
Cdd:pfam10409   80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 53-200 1.68e-33

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 130.34  E-value: 1.68e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258    53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY---------P 123
Cdd:smart00220   83 DLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLADFGLARQLDPGeklttfvgtP 160

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   124 DYswsaqrRA---LVEEE--------ALGCILYLLCFRQHPFEDGAKL-----RIVNGKYSIPPHDTQYTV-FHSLIRAM 186
Cdd:smart00220  161 EY------MApevLLGKGygkavdiwSLGVILYELLTGKPPFPGDDQLlelfkKIGKPKPPFPPPEWDISPeAKDLIRKL 234

                           170
                    ....*....|....
gi 1034639258   187 LQVNPEERLSIAEV 200
Cdd:smart00220  235 LVKDPEKRLTAEEA 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
58-256 3.52e-19

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 92.38  E-value: 3.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSAT-----------TISHYPDYS 126
Cdd:COG0515     98 LRRRGPLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPDGRVKLIDFGIARalggatltqtgTVVGTPGYM 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 --WSAQRRALVEEE---ALGCILYLLCFRQHPFE---DGAKLRIVNGKYSIPPHDTQYTV---FHSLIRAMLQVNPEERL 195
Cdd:COG0515    176 apEQARGEPVDPRSdvySLGVTLYELLTGRPPFDgdsPAELLRAHLREPPPPPSELRPDLppaLDAIVLRALAKDPEERY 255

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  196 -SIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALA 256
Cdd:COG0515    256 qSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 317
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
59-155 3.34e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.51  E-value: 3.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   59 ESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-----SATTIS---------HY-- 122
Cdd:NF033483    99 REHGPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILITKDGRVKVTDFGiaralSSTTMTqtnsvlgtvHYls 176

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034639258  123 PDyswsaQ-RRALVEEE----ALGCILY-LLCFRQhPFE 155
Cdd:NF033483   177 PE-----QaRGGTVDARsdiySLGIVLYeMLTGRP-PFD 209
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 49-125 2.05e-10

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: 62.90  E-value: 2.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKmeSRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:pfam07714   86 GDLLDFLRK--HKRKLTLKDLLSMALQIAKGMEYLESKN--FVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYY 158
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 56-231 4.46e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 57.33  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   56 KKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------------SATTISHYP 123
Cdd:PTZ00267   158 QRLKEHLPFQEYEVGLLFYQIVLALDEVHSRK--MMHRDLKSANIFLMPTGIIKLGDFGfskqysdsvsldVASSFCGTP 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 DY----SWSAQRRA-LVEEEALGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPPHDTQYTVfHSLIRAMLQVNPEER 194
Cdd:PTZ00267   236 YYlapeLWERKRYSkKADMWSLGVILYELLTLHRPFKGPSQREIMQqvlyGKYDPFPCPVSSGM-KALLDPLLSKNPALR 314

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034639258  195 LSIAEVVHQ---------LQEIAAARNVNPKSPITELLEQNGGYGS 231
Cdd:PTZ00267   315 PTTQQLLHTeflkyvanlFQDIVRHSETISPHDREEILRQLQESGE 360
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1195-1239 1.10e-07

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 49.47  E-value: 1.10e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258 1195 PEQVKKHYRRAVLAVHPDKAAGQPYeqhAKMIFMELNDAWSEFEN 1239
Cdd:cd06257     14 DEEIKKAYRKLALKYHPDKNPDDPE---AEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1195-1240 1.85e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 46.07  E-value: 1.85e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1034639258  1195 PEQVKKHYRRAVLAVHPDKAAGQPYEqhAKMIFMELNDAWSEFENQ 1240
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
 730-1060 1.07e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  730 EGQEPRADPEPPGLAAGLVQQdlvfevETPAVLPEPVPqedgvdllglHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPP 809
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP------PPPPPTPEPAP----------HALVSATPLPPGPAAARQASPALPAAPAPPAV 2744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  810 EAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPS 889
Cdd:PHA03247  2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  890 AHSAPPPSCSAdflhlgdlPGEPSKMTASSSNPDLLGGWAAwtetAASAVAPTPATEGPLFSPGGQPAPCGSQ-ASWTKS 968
Cdd:PHA03247  2825 AGPLPPPTSAQ--------PTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS 2892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  969 QNPDPFADLGDLSSGLQDPQAQS----TVSPRGQRVCTCSRRLPTGKLKPGVADTGTAASPHRHCGSPA----GFPPGGF 1040
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgALVPGRV 2972

                          330       340
                   ....*....|....*....|
gi 1034639258 1041 IPKTATTPKGSSSWQTSRPP 1060
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAPASS 2992
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 699-1082 3.62e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 48.22  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  699 ENASSKESESALMEDRDESEVSDEG----GSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQ-----E 769
Cdd:pfam03154  140 DNRSTSPSIPSPQDNESDSDSSAQQqilqTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAtsqppN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  770 DGVDLLGLHSEVGAGPAVPPQACKAPSSntdllscllgPPEAASQGPPEDLLSEDPL---LLASPAPPL--SVQSTPRGG 844
Cdd:pfam03154  220 QTQSTAAPHTLIQQTPTLHPQRLPSPHP----------PLQPMTQPPPPSQVSPQPLpqpSLHGQMPPMphSLQTGPSHM 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  845 P-PAAADPFGPLLPSSGNNSQPCSNPDLFGEflNSDSVTVPPSFPSAHSAPPPS------CSADFLHLGDLPGEP-SKMT 916
Cdd:pfam03154  290 QhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ--SQQRIHTPPSQSQLQSQQPPReqplppAPLSMPHIKPPPTTPiPQLP 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  917 ASSSN--PDLLGGWAAWTetAASAVAPTPATEgPLFSPGGQPAPcgsqaswtkSQNPDPFaDLGDLSSGLQDPQAQSTVS 994
Cdd:pfam03154  368 NPQSHkhPPHLSGPSPFQ--MNSNLPPPPALK-PLSSLSTHHPP---------SAHPPPL-QLMPQSQQLPPPPAQPPVL 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  995 PRGQRV-CTCSRRLPTGKLKPGVADTGTAASPHRHCGSPAGFPPGGfiPKTATTPKGSsswqTSRPPAQGASWPPQAKPP 1073
Cdd:pfam03154  435 TQSQSLpPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSG--PPTSTSSAMP----GIQPPSSASVSSSGPVPA 508

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1034639258 1074 PKAC---------------------------TQPRP 1082
Cdd:pfam03154  509 AVSCplppvqikeealdeaeepesppppprsPSPEP 544
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1196-1235 6.73e-05

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 42.07  E-value: 6.73e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034639258 1196 EQVKKHYRRAVLAVHPDKAAGQPyeqHAKMIFMELNDAWS 1235
Cdd:pfam00226   15 EEIKKAYRKLALKYHPDKNPGDP---EAEEKFKEINEAYE 51
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1195-1234 3.44e-04

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 40.17  E-value: 3.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258 1195 PEQVKKHYRRAVLAVHPDK-AAGQPyeQHAKMIFME----LNDAW 1234
Cdd:COG1076     18 DAELKRAYRKLQREHHPDRlAAGLP--EEEQRLALQkaaaINEAY 60
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 600-854 8.94e-03

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 40.33  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  600 VEPRDRPSREAPPWENSSMRGLNPKILFSSReeqqdilskfgkPELPRQPGSTAQY--DAGAGSPEAEPTDSDSPPSSSa 677
Cdd:PHA03321   458 RRARAQRARDAGPEYVDPLGALRRLPAGAAP------------PPEPAAAPSPATYytRMGGGPPRLPPRNRATETLRP- 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  678 dasrflhtlDWQEEKEAEtgaenaSSKESESALMEDRDESEVSDEGGSPISSEGQE-PRADPEPPGLAAGLVQQDLVFEV 756
Cdd:PHA03321   525 ---------DWGPPAAAP------PEQMEDPYLEPDDDRFDRRDGAAAAATSHPREaPAPDDDPIYEGVSDSEEPVYEEI 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  757 ETPAVLPEPVPQedgvdllglhSEVGAGPAVPPQACKAPSSNTDLL------SCLLGPPEAASQGPPEdllsedplLLAS 830
Cdd:PHA03321   590 PTPRVYQNPLPR----------PMEGAGEPPDLDAPTSPWVEEENPiygwgdSPLFSPPPAARFPPPD--------PALS 651

                          250       260
                   ....*....|....*....|....
gi 1034639258  831 PAPPLSVQSTPRggpPAAADPFGP 854
Cdd:PHA03321   652 PEPPALPAHRPR---PGALAPDGP 672
 
Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 291-453 1.66e-122

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein 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 a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with 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.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 375.01  E-value: 1.66e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  291 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 370
Cdd:cd14564      1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  371 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 450
Cdd:cd14564     81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                   ...
gi 1034639258  451 CDM 453
Cdd:cd14564    161 CDM 163
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 46-211 1.00e-104

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: 332.17  E-value: 1.00e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd14036     87 LCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDY 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  126 SWSAQRRALVEEE------------------------------ALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQ 175
Cdd:cd14036    167 SWSAQKRSLVEDEitrnttpmyrtpemidlysnypigekqdiwALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQ 246

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034639258  176 YTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAAR 211
Cdd:cd14036    247 YTVFHDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 291-453 2.56e-103

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 323.53  E-value: 2.56e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  291 VANYAKGDLDISYITSRIAVMSFPAEGVESA-LKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARR 369
Cdd:cd14511      1 QQSYARNDLDISYITSRIIVMPFPAEGIESTyRKNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  370 APHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEY 449
Cdd:cd14511     81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYY 160


                   ....
gi 1034639258  450 MCDM 453
Cdd:cd14511    161 FSDI 164
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 291-453 5.32e-83

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 267.90  E-value: 5.32e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  291 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 370
Cdd:cd14563      1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  371 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 450
Cdd:cd14563     81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                   ...
gi 1034639258  451 CDM 453
Cdd:cd14563    161 CDL 163
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 48-209 1.59e-69

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: 234.54  E-value: 1.59e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   48 EGQLVEFLKKMEsRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIsHYPDYSW 127
Cdd:cd13985     85 PGSLVDILEKSP-PSPLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGRFKLCDFGSATTE-HYPLERA 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  128 saQRRALVEEE------------------------------ALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYT 177
Cdd:cd13985    163 --EEVNIIEEEiqknttpmyrapemidlyskkpigekadiwALGCLLYKLCFFKLPFDESSKLAIVAGKYSIPEQPRYSP 240

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034639258  178 VFHSLIRAMLQVNPEERLSIAEVVHQLQEIAA 209
Cdd:cd13985    241 ELHDLIRHMLTPDPAERPDIFQVINIITKDTK 272
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 300-452 2.05e-54

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 186.63  E-value: 2.05e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  300 DISYITSRIAVMSFPAEGV-ESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRP-SRFHNRVSECGWAARRAPHLHTLY 377
Cdd:cd14497      1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  378 NICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIW----PSHKRYIEYMCD 452
Cdd:cd14497     81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPgvtiPSQLRYLQYFER 159
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 300-449 3.04e-49

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 172.00  E-value: 3.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  300 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNL-SPRTYRPSRFHNRVSECGWAARRAPHLHTLYN 378
Cdd:cd14509      1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  379 ICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPG----IwPSHKRYIEY 449
Cdd:cd14509     81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKkgvtI-PSQRRYVYY 154
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 298-449 4.27e-43

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 154.83  E-value: 4.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  298 DLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNL-SPRTYRPSRFHNRVSECGWAARRAPHLHTL 376
Cdd:cd14510     13 DLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNVPTLDEM 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  377 YNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIW--------PSHKRYIE 448
Cdd:cd14510     93 LSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPSQSRYVG 172


                   .
gi 1034639258  449 Y 449
Cdd:cd14510    173 Y 173
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
 47-208 6.58e-42

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: 155.13  E-value: 6.58e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   47 AEGQLVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDys 126
Cdd:cd14037     89 KGGGVIDLMNQRLQTG-LTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLISDSGNYKLCDFGSATTKILPPQ-- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 wSAQRRALVEEE------------------------------ALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQY 176
Cdd:cd14037    166 -TKQGVTYVEEDikkyttlqyrapemidlyrgkpiteksdiwALGCLLYKLCFYTTPFEESGQLAILNGNFTFPDNSRYS 244

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034639258  177 TVFHSLIRAMLQVNPEERLSIAEVVHQLQEIA 208
Cdd:cd14037    245 KRLHKLIRYMLEEDPEKRPNIYQVSYEAFELA 276
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 300-453 5.42e-40

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 145.61  E-value: 5.42e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  300 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 379
Cdd:cd14508      1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  380 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKR-----CPPGIWPSHKRYIEYMCDM 453
Cdd:cd14508     81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRfyddkVGPLGQPSQKRYVGYFSGL 159
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 461-599 1.51e-35

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 131.63  E-value: 1.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  461 PHSKPILVRAVVMTPVPLFsKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARS 540
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  541 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 599
Cdd:pfam10409   80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 53-200 1.68e-33

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 130.34  E-value: 1.68e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258    53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY---------P 123
Cdd:smart00220   83 DLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLADFGLARQLDPGeklttfvgtP 160

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   124 DYswsaqrRA---LVEEE--------ALGCILYLLCFRQHPFEDGAKL-----RIVNGKYSIPPHDTQYTV-FHSLIRAM 186
Cdd:smart00220  161 EY------MApevLLGKGygkavdiwSLGVILYELLTGKPPFPGDDQLlelfkKIGKPKPPFPPPEWDISPeAKDLIRKL 234

                           170
                    ....*....|....
gi 1034639258   187 LQVNPEERLSIAEV 200
Cdd:smart00220  235 LVKDPEKRLTAEEA 248
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 300-450 7.69e-30

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 116.58  E-value: 7.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  300 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 379
Cdd:cd14561      1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  380 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMK-----RCPPGIWPSHKRYIEYM 450
Cdd:cd14561     81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKkfyddKVSALMQPSQKRYVQFL 156
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 53-200 8.42e-30

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: 119.54  E-value: 8.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY---------P 123
Cdd:cd14003     85 ELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNG--IVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGsllktfcgtP 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 DYS-----------------WSaqrralveeeaLGCILYLLCFRQHPFEDG--AKLR--IVNGKYSIPPHDTqyTVFHSL 182
Cdd:cd14003    163 AYAapevllgrkydgpkadvWS-----------LGVILYAMLTGYLPFDDDndSKLFrkILKGKYPIPSHLS--PDARDL 229

                          170
                   ....*....|....*...
gi 1034639258  183 IRAMLQVNPEERLSIAEV 200
Cdd:cd14003    230 IRRMLVVDPSKRITIEEI 247
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 49-203 1.21e-29

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: 119.10  E-value: 1.21e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRG-PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH------ 121
Cdd:cd08215     84 GDLAQKIKKQKKKGqPFPEEQILDWFVQICLALKYLHSRK--ILHRDLKTQNIFLTKDGVVKLGDFGISKVLESttdlak 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 -------Y--PD------YS-----WsaqrralveeeALGCILYLLCFRQHPFeDGAKL-----RIVNGKYsiPPHDTQY 176
Cdd:cd08215    162 tvvgtpyYlsPElcenkpYNyksdiW-----------ALGCVLYELCTLKHPF-EANNLpalvyKIVKGQY--PPIPSQY 227

                          170       180
                   ....*....|....*....|....*...
gi 1034639258  177 TV-FHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd08215    228 SSeLRDLVNSMLQKDPEKRPSANEILSS 255
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 300-449 7.96e-29

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 113.54  E-value: 7.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  300 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 379
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  380 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKR------CPPGiWPSHKRYIEY 449
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRfyedkvVPVG-QPSQKRYVHY 155
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 53-200 2.03e-27

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: 112.57  E-value: 2.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSA--- 129
Cdd:cd14007     86 ELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKN--IIHRDIKPENILLGSNGELKLADFG------------WSVhap 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 -QRRA------------LVEEE---------ALGCILYLLCFRQHPFEDG----AKLRIVNGKYSIPPH---DTQytvfh 180
Cdd:cd14007    152 sNRRKtfcgtldylppeMVEGKeydykvdiwSLGVLCYELLVGKPPFESKshqeTYKRIQNVDIKFPSSvspEAK----- 226

                          170       180
                   ....*....|....*....|
gi 1034639258  181 SLIRAMLQVNPEERLSIAEV 200
Cdd:cd14007    227 DLISKLLQKDPSKRLSLEQV 246
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 46-204 9.38e-27

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: 109.28  E-value: 9.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKkmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH---- 121
Cdd:cd00180     73 CEGGSLKDLLK--ENKGPLSEEEALSILRQLLSALEYLHSNG--IIHRDLKPENILLDSDGTVKLADFGLAKDLDSddsl 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 YPDYSWSAQRRALVEEE-------------ALGCILYLLcfrqhpfedgaklrivngkysipphdtqyTVFHSLIRAMLQ 188
Cdd:cd00180    149 LKTTGGTTPPYYAPPELlggryygpkvdiwSLGVILYEL-----------------------------EELKDLIRRMLQ 199

                          170
                   ....*....|....*.
gi 1034639258  189 VNPEERLSIAEVVHQL 204
Cdd:cd00180    200 YDPKKRPSAKELLEHL 215
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
 49-201 8.47e-26

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 108.02  E-value: 8.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY------ 122
Cdd:cd14099     86 GSLMELLKR---RKALTEPEVRYFMRQILSGVKYLHSNR--IIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDgerkkt 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 ----PDY-----------------SWSaqrralveeeaLGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHDTQYT 177
Cdd:cd14099    161 lcgtPNYiapevlekkkghsfevdIWS-----------LGVILYTLLVGKPPFETSDVketyKRIKKNEYSFPSHLSISD 229

                          170       180
                   ....*....|....*....|....
gi 1034639258  178 VFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14099    230 EAKDLIRSMLQPDPTKRPSLDEIL 253
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 300-449 4.68e-25

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 102.72  E-value: 4.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  300 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 379
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  380 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKR-C----PPGIWPSHKRYIEY 449
Cdd:cd14562     81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfCedkvATSLQPSQRRYISY 155
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 63-206 1.34e-24

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: 105.07  E-value: 1.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHR-QKPPIIHRDLKVENLLLSNQGTIKLCDFGSAT-----------------------T 118
Cdd:cd13986    102 FFPEDRILHIFLGICRGLKAMHEpELVPYAHRDIKPGNVLLSEDDEPILMDLGSMNparieiegrrealalqdwaaehcT 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  119 ISHYPDYSWSAQRRALVEEEA----LGCILYLLCFRQHPFE------DGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQ 188
Cdd:cd13986    182 MPYRAPELFDVKSHCTIDEKTdiwsLGCTLYALMYGESPFErifqkgDSLALAVLSGNYSFPDNSRYSEELHQLVKSMLV 261

                          170
                   ....*....|....*...
gi 1034639258  189 VNPEERLSIAEVVHQLQE 206
Cdd:cd13986    262 VNPAERPSIDDLLSRVHD 279
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 53-200 1.53e-23

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: 101.40  E-value: 1.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGSATTIS--------- 120
Cdd:cd05117     85 ELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQG--IVHRDLKPENILLASKdpdSPIKIIDFGLAKIFEegeklktvc 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 ---HY--PD------YS-----WSaqrralveeeaLGCILY-LLCFRqHPF--EDGAKL--RIVNGKYSIPPhdtqyTVF 179
Cdd:cd05117    163 gtpYYvaPEvlkgkgYGkkcdiWS-----------LGVILYiLLCGY-PPFygETEQELfeKILKGKYSFDS-----PEW 225

                          170       180
                   ....*....|....*....|....*...
gi 1034639258  180 HS-------LIRAMLQVNPEERLSIAEV 200
Cdd:cd05117    226 KNvseeakdLIKRLLVVDPKKRLTAAEA 253
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 49-199 4.20e-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: 100.31  E-value: 4.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMesRGPLSCDTVLKIFYQTCRAVQHMHR---QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISH---- 121
Cdd:cd08217     89 AQLIKKCKKE--NQYIPEEFIWKIFTQLLLALYECHNrsvGGGKILHRDLKPANIFLDSDNNVKLGDFGLARVLSHdssf 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 ---Y---PdYSWSAQrraLVEEE---------ALGCILYLLCFRQHPFE----DGAKLRIVNGKYS-IPPHdtqYTV-FH 180
Cdd:cd08217    167 aktYvgtP-YYMSPE---LLNEQsydeksdiwSLGCLIYELCALHPPFQaanqLELAKKIKEGKFPrIPSR---YSSeLN 239

                          170
                   ....*....|....*....
gi 1034639258  181 SLIRAMLQVNPEERLSIAE 199
Cdd:cd08217    240 EVIKSMLNVDPDKRPSVEE 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
 49-200 2.02e-22

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: 98.09  E-value: 2.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS-------- 120
Cdd:cd14081     86 GELFDYLVK---KGRLTEKEARKFFRQIISALDYCHSHS--ICHRDLKPENLLLDEKNNIKIADFGMASLQPegsllets 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 ----HY--PD------YS------WSaqrralveeeaLGCILYLLCFRQHPFeDGAKLR-----IVNGKYSIPPH---DT 174
Cdd:cd14081    161 cgspHYacPEvikgekYDgrkadiWS-----------CGVILYALLVGALPF-DDDNLRqllekVKRGVFHIPHFispDA 228

                          170       180
                   ....*....|....*....|....*.
gi 1034639258  175 QytvfhSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14081    229 Q-----DLLRRMLEVNPEKRITIEEI 249
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 53-200 1.30e-21

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 95.87  E-value: 1.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT---------TISHYP 123
Cdd:cd14075     87 ELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENN--IIHRDLKAENVFYASNNCVKVGDFGFSThakrgetlnTFCGSP 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 DYSWSAQRR------ALVEEEALGCILYLLCFRQHPF--EDGAKLR--IVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEE 193
Cdd:cd14075    165 PYAAPELFKdehyigIYVDIWALGVLLYFMVTGVMPFraETVAKLKkcILEGTYTIPSYVSEPC--QELIRGILQPVPSD 242


                   ....*..
gi 1034639258  194 RLSIAEV 200
Cdd:cd14075    243 RYSIDEI 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
 49-203 1.79e-21

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: 95.17  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD---- 124
Cdd:cd08529     84 GDLHSLIKSQRGR-PLPEDQIWKFFIQTLLGLSHLHSKK--ILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNfaqt 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  125 -----YSWSAQrraLVEEE---------ALGCILYLLCFRQHPFE---DGAK-LRIVNGKYsiPPHDTQYT-VFHSLIRA 185
Cdd:cd08529    161 ivgtpYYLSPE---LCEDKpyneksdvwALGCVLYELCTGKHPFEaqnQGALiLKIVRGKY--PPISASYSqDLSQLIDS 235

                          170
                   ....*....|....*...
gi 1034639258  186 MLQVNPEERLSIAEVVHQ 203
Cdd:cd08529    236 CLTKDYRQRPDTTELLRN 253
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 46-206 4.22e-21

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: 94.19  E-value: 4.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQ-LVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSATTISH--- 121
Cdd:cd14014     81 YVEGGsLADLLRE---RGPLPPREALRILAQIADALAAAHRA--GIVHRDIKPANILLTEDGRVKLTDFGIARALGDsgl 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 --------YPDYSWSAQ-RRALVEEE----ALGCILYLLCFRQHPFEDGAKLRIVNGK--YSIPPHDTQYTVFHS----L 182
Cdd:cd14014    156 tqtgsvlgTPAYMAPEQaRGGPVDPRsdiySLGVVLYELLTGRPPFDGDSPAAVLAKHlqEAPPPPSPLNPDVPPaldaI 235

                          170       180
                   ....*....|....*....|....*
gi 1034639258  183 IRAMLQVNPEERL-SIAEVVHQLQE 206
Cdd:cd14014    236 ILRALAKDPEERPqSAAELLAALRA 260
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 46-200 7.55e-21

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: 93.77  E-value: 7.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd14008     87 YCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENG--IVHRDIKPENLLLTADGTVKISDFGVSEMFEDGNDT 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  126 swsAQRRA-----------LVEEE----------ALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTVFH 180
Cdd:cd14008    165 ---LQKTAgtpaflapelcDGDSKtysgkaadiwALGVTLYCLVFGRLPFNGDNILelyeAIQNQNDEFPIPPELSPELK 241

                          170       180
                   ....*....|....*....|
gi 1034639258  181 SLIRAMLQVNPEERLSIAEV 200
Cdd:cd14008    242 DLLRRMLEKDPEKRITLKEI 261
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 49-196 1.08e-20

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: 93.11  E-value: 1.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKkmESRGPL-SCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSW 127
Cdd:cd08219     83 GDLMQKIK--LQRGKLfPEDTILQWFVQMCLGVQHIHEKR--VLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYAC 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  128 S-AQRRALVEEE--------------ALGCILYLLCFRQHPFEDGA----KLRIVNGKYSIPPHDTQYTVfHSLIRAMLQ 188
Cdd:cd08219    159 TyVGTPYYVPPEiwenmpynnksdiwSLGCILYELCTLKHPFQANSwknlILKVCQGSYKPLPSHYSYEL-RSLIKQMFK 237


                   ....*...
gi 1034639258  189 VNPEERLS 196
Cdd:cd08219    238 RNPRSRPS 245
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 46-202 9.12e-20

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: 90.32  E-value: 9.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAE-GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG---------- 114
Cdd:cd14080     83 YAEhGDLLEYIQK---RGALSESQARIWFRQLALAVQYLHSLD--IAHRDLKCENILLDSNNNVKLSDFGfarlcpdddg 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 ---SAT--------------TISHYPDYS--WSaqrralveeeaLGCILYLLCFRQHPFEDG--AKL--RIVNGKYSIPP 171
Cdd:cd14080    158 dvlSKTfcgsaayaapeilqGIPYDPKKYdiWS-----------LGVILYIMLCGSMPFDDSniKKMlkDQQNRKVRFPS 226

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034639258  172 HDTQYTV-FHSLIRAMLQVNPEERLSIAEVVH 202
Cdd:cd14080    227 SVKKLSPeCKDLIDQLLEPDPTKRATIEEILN 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 46-200 1.95e-19

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: 89.64  E-value: 1.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAE-GQLVEFLKKMESRG-PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCD------FGSAT 117
Cdd:cd08224     81 LADaGDLSRLIKHFKKQKrLIPERTIWKYFVQLCSALEHMHSKR--IMHRDIKPANVFITANGVVKLGDlglgrfFSSKT 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 TISH----YPdYSWSAQRralVEEE---------ALGCILYLLCFRQHPFE-DGAKL-----RIVNGKYSIPPHDTQYTV 178
Cdd:cd08224    159 TAAHslvgTP-YYMSPER---IREQgydfksdiwSLGCLLYEMAALQSPFYgEKMNLyslckKIEKCEYPPLPADLYSQE 234

                          170       180
                   ....*....|....*....|..
gi 1034639258  179 FHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd08224    235 LRDLVAACIQPDPEKRPDISYV 256
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
58-256 3.52e-19

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 92.38  E-value: 3.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSAT-----------TISHYPDYS 126
Cdd:COG0515     98 LRRRGPLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPDGRVKLIDFGIARalggatltqtgTVVGTPGYM 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 --WSAQRRALVEEE---ALGCILYLLCFRQHPFE---DGAKLRIVNGKYSIPPHDTQYTV---FHSLIRAMLQVNPEERL 195
Cdd:COG0515    176 apEQARGEPVDPRSdvySLGVTLYELLTGRPPFDgdsPAELLRAHLREPPPPPSELRPDLppaLDAIVLRALAKDPEERY 255

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  196 -SIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALA 256
Cdd:COG0515    256 qSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 317
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 46-202 5.67e-19

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: 88.08  E-value: 5.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLkkmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH---- 121
Cdd:cd14002     81 YAQGELFQIL---EDDGTLPEEEVRSIAKQLVSALHYLHSNR--IIHRDMKPQNILIGKGGVVKLCDFGFARAMSCntlv 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 ------YPDYswsaQRRALVEEE---------ALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPphDTQYTVFHSL 182
Cdd:cd14002    156 ltsikgTPLY----MAPELVQEQpydhtadlwSLGCILYELFVGQPPFytNSIYQLvqMIVKDPVKWP--SNMSPEFKSF 229

                          170       180
                   ....*....|....*....|
gi 1034639258  183 IRAMLQVNPEERLSIAEVVH 202
Cdd:cd14002    230 LQGLLNKDPSKRLSWPDLLE 249
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 67-201 9.44e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 87.56  E-value: 9.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   67 DTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD---------YSWSAQrraLVEE 137
Cdd:cd08218    101 DQILDWFVQLCLALKHVHDRK--ILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVElartcigtpYYLSPE---ICEN 175

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258  138 E---------ALGCILYLLCFRQHPFEDGAK----LRIVNGKYsiPPHDTQYTV-FHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd08218    176 KpynnksdiwALGCVLYEMCTLKHAFEAGNMknlvLKIIRGSY--PPVPSRYSYdLRSLVSQLFKRNPRDRPSINSIL 251
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 53-196 1.48e-18

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: 86.80  E-value: 1.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLkiFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA----------TTIS 120
Cdd:cd05123     79 ELFSHLSKEGRFPEERAR--FYaaEIVLALEYLHSLG--IIYRDLKPENILLDSDGHIKLTDFGLAkelssdgdrtYTFC 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 HYPDYS----------------WSaqrralveeeaLGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQytVFH 180
Cdd:cd05123    155 GTPEYLapevllgkgygkavdwWS-----------LGVLLYEMLTGKPPFyaENRKEIyeKILKSPLKFPEYVSP--EAK 221

                          170
                   ....*....|....*.
gi 1034639258  181 SLIRAMLQVNPEERLS 196
Cdd:cd05123    222 SLISGLLQKDPTKRLG 237
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 49-204 4.36e-18

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: 85.28  E-value: 4.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMesRGPLSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD---- 124
Cdd:cd13999     75 GSLYDLLHKK--KIPLSWSLRLKIALDIARGMNYLH--SPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEkmtg 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  125 ----YSWSAqrralveEEAL--------------GCILYLLCFRQHPFEDGAKLRIVNGKY----------SIPPHdtqy 176
Cdd:cd13999    151 vvgtPRWMA-------PEVLrgepytekadvysfGIVLWELLTGEVPFKELSPIQIAAAVVqkglrppippDCPPE---- 219

                          170       180
                   ....*....|....*....|....*...
gi 1034639258  177 tvFHSLIRAMLQVNPEERLSIAEVVHQL 204
Cdd:cd13999    220 --LSKLIKRCWNEDPEKRPSFSEIVKRL 245
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 51-202 7.43e-18

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: 84.59  E-value: 7.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKMESrgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSAtTISHYPDYSWSA 129
Cdd:cd05118     87 LYELIKDYPR--GLPLDLIKSYLYQLLQALDFLHSNG--IIHRDLKPENILINLElGQLKLADFGLA-RSFTSPPYTPYV 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 QRRALVEEE---------------ALGCILYLLCFRQHPFEDG------AKLRIVNGKYSipphdtqytvFHSLIRAMLQ 188
Cdd:cd05118    162 ATRWYRAPEvllgakpygssidiwSLGCILAELLTGRPLFPGDsevdqlAKIVRLLGTPE----------ALDLLSKMLK 231

                          170
                   ....*....|....
gi 1034639258  189 VNPEERLSIAEVVH 202
Cdd:cd05118    232 YDPAKRITASQALA 245
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 51-200 8.50e-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: 84.60  E-value: 8.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTI--SHYPDYS- 126
Cdd:cd14005     94 LFDFITE---RGALSENLARIIFRQVVEAVRHCHQRG--VLHRDIKDENLLINlRTGEVKLIDFGCGALLkdSVYTDFDg 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 --------WSAQRRALVEEEA---LGCILYLLCFRQHPFEDgaKLRIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERL 195
Cdd:cd14005    169 trvysppeWIRHGRYHGRPATvwsLGILLYDMLCGDIPFEN--DEQILRGNVLFRPRLS--KECCDLISRCLQFDPSKRP 244


                   ....*
gi 1034639258  196 SIAEV 200
Cdd:cd14005    245 SLEQI 249
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 56-203 1.11e-17

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: 84.37  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   56 KKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT--------TISHYPDYS- 126
Cdd:cd08530     92 KRKKKRRLFPEDDIWRIFIQMLRGLKALHDQK--ILHRDLKSANILLSAGDLVKIGDLGISKvlkknlakTQIGTPLYAa 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 ---WsaQRRALVEEE---ALGCILYLLCFRQHPFE----DGAKLRIVNGKYSIPPH----DTQytvfhSLIRAMLQVNPE 192
Cdd:cd08530    170 pevW--KGRPYDYKSdiwSLGCLLYEMATFRPPFEartmQELRYKVCRGKFPPIPPvysqDLQ-----QIIRSLLQVNPK 242

                          170
                   ....*....|.
gi 1034639258  193 ERLSIAEVVHQ 203
Cdd:cd08530    243 KRPSCDKLLQS 253
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
 71-201 2.54e-17

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 83.49  E-value: 2.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSN---QGTIKLCDFGSA---------TTISHYPDYS------------ 126
Cdd:cd14089    104 EIMRQIGSAVAHLHSMN--IAHRDLKPENLLYSSkgpNAILKLTDFGFAketttkkslQTPCYTPYYVapevlgpekydk 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 ----WSaqrralveeeaLGCILY-LLC-----FRQH--PFEDGAKLRIVNGKYSIPphDTQYTVFHS----LIRAMLQVN 190
Cdd:cd14089    182 scdmWS-----------LGVIMYiLLCgyppfYSNHglAISPGMKKRIRNGQYEFP--NPEWSNVSEeakdLIRGLLKTD 248

                          170
                   ....*....|.
gi 1034639258  191 PEERLSIAEVV 201
Cdd:cd14089    249 PSERLTIEEVM 259
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 71-200 3.42e-17

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: 82.69  E-value: 3.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSW----------------SAQRRAL 134
Cdd:cd14119    101 GYFVQLIDGLEYLHSQG--IIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAEDDTcttsqgspafqppeiaNGQDSFS 178

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  135 ---VEEEALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPPH-DTQytvFHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14119    179 gfkVDIWSAGVTLYNMTTGKYPFEGDNIYKlfenIGKGEYTIPDDvDPD---LQDLLRGMLEKDPEKRFTIEQI 249
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 47-202 1.04e-16

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: 81.28  E-value: 1.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   47 AEGQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA---------T 117
Cdd:cd14073     84 SGGELYDYISE---RRRLPEREARRIFRQIVSAVHYCHKNG--VVHRDLKLENILLDQNGNAKIADFGLSnlyskdkllQ 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 TISHYPDY-----------------SWSaqrralveeeaLGCILYLLCFRQHPFE--DGAKLR--IVNGKYSIPPHDtqy 176
Cdd:cd14073    159 TFCGSPLYaspeivngtpyqgpevdCWS-----------LGVLLYTLVYGTMPFDgsDFKRLVkqISSGDYREPTQP--- 224

                          170       180
                   ....*....|....*....|....*.
gi 1034639258  177 TVFHSLIRAMLQVNPEERLSIAEVVH 202
Cdd:cd14073    225 SDASGLIRWMLTVNPKRRATIEDIAN 250
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 49-200 1.69e-16

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: 81.11  E-value: 1.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESrgpLSCDTVLkiFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA---------- 116
Cdd:cd05581     86 GDLLEYIRKYGS---LDEKCTR--FYtaEIVLALEYLHSKG--IIHRDLKPENILLDEDMHIKITDFGTAkvlgpdsspe 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 TTISHYPDYSWSAQRRA-------------LVEEE---------ALGCILYLLCFRQHPFEDGA----KLRIVNGKYSIP 170
Cdd:cd05581    159 STKGDADSQIAYNQARAasfvgtaeyvspeLLNEKpagkssdlwALGCIIYQMLTGKPPFRGSNeyltFQKIVKLEYEFP 238

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034639258  171 ---PHDTQytvfhSLIRAMLQVNPEERLSIAEV 200
Cdd:cd05581    239 enfPPDAK-----DLIQKLLVLDPSKRLGVNEN 266
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 72-201 2.16e-16

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: 80.51  E-value: 2.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWS-----------AQRRALVEEE-- 138
Cdd:cd14004    114 IFRQVADAVKHLHDQG--IVHRDIKDENVILDGNGTIKLIDFGSAAYIKSGPFDTFVgtidyaapevlRGNPYGGKEQdi 191

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  139 -ALGCILYLLCFRQHPFEDgaKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14004    192 wALGVLLYTLVFKENPFYN--IEEILEADLRIPYAVSEDLI--DLISRMLNRDVGDRPTIEELL 251
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 49-200 4.05e-16

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: 79.74  E-value: 4.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA---------TTI 119
Cdd:cd14071     84 GEIFDYLAQ---HGRMSEKEARKKFWQILSAVEYCHKRH--IVHRDLKAENLLLDANMNIKIADFGFSnffkpgellKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  120 SHYPDYS-----------------WSaqrralveeeaLGCILYLLCFRQHPFeDGAKL-----RIVNGKYSIPphdtqyt 177
Cdd:cd14071    159 CGSPPYAapevfegkeyegpqldiWS-----------LGVVLYVLVCGALPF-DGSTLqtlrdRVLSGRFRIP------- 219

                          170       180
                   ....*....|....*....|....*...
gi 1034639258  178 VFHS-----LIRAMLQVNPEERLSIAEV 200
Cdd:cd14071    220 FFMStdcehLIRRMLVLDPSKRLTIEQI 247
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
 49-200 8.43e-16

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: 78.85  E-value: 8.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG--SATTISHY---- 122
Cdd:cd14079     87 GELFDYIVQ---KGRLSEDEARRFFQQIISGVEYCHRHM--VVHRDLKPENLLLDSNMNVKIADFGlsNIMRDGEFlkts 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 ---PDYS-----------------WSAqrralveeealGCILY-LLCFRQhPFEDG--AKL--RIVNGKYSIPPHDTQYT 177
Cdd:cd14079    162 cgsPNYAapevisgklyagpevdvWSC-----------GVILYaLLCGSL-PFDDEhiPNLfkKIKSGIYTIPSHLSPGA 229

                          170       180
                   ....*....|....*....|...
gi 1034639258  178 VfhSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14079    230 R--DLIKRMLVVDPLKRITIPEI 250
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 54-199 1.57e-15

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: 78.29  E-value: 1.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   54 FLKKMesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH------------ 121
Cdd:cd07829     87 YLDKR--PGPLPPNLIKSIMYQLLRGLAYCHSHR--ILHRDLKPQNLLINRDGVLKLADFGLARAFGIplrtythevvtl 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 -Y---------PDYS-----WSAqrralveeealGCILYLLCfRQHPF-----EDGAKLRI------------------V 163
Cdd:cd07829    163 wYrapeillgsKHYStavdiWSV-----------GCIFAELI-TGKPLfpgdsEIDQLFKIfqilgtpteeswpgvtklP 230

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258  164 NGKYSIP--PHDTQYTVFHS-------LIRAMLQVNPEERLSIAE 199
Cdd:cd07829    231 DYKPTFPkwPKNDLEKVLPRldpegidLLSKMLQYNPAKRISAKE 275
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 61-203 1.75e-15

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: 77.69  E-value: 1.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   61 RGPL-SCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTI-KLCDFGSATTISHYPDYSWSA--------- 129
Cdd:cd08225     94 RGVLfSEDQILSWFVQISLGLKHIHDRK--ILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAYTCvgtpyylsp 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 ---QRRALVEEE---ALGCILYLLCFRQHPFEDGA----KLRIVNGKYS-IPPHDTQYtvFHSLIRAMLQVNPEERLSIA 198
Cdd:cd08225    172 eicQNRPYNNKTdiwSLGCVLYELCTLKHPFEGNNlhqlVLKICQGYFApISPNFSRD--LRSLISQLFKVSPRDRPSIT 249


                   ....*
gi 1034639258  199 EVVHQ 203
Cdd:cd08225    250 SILKR 254
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 53-200 2.94e-15

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: 77.40  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKK---ME--SRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------------S 115
Cdd:cd14118     96 ELVDKgavMEvpTDNPLSEETARSYFRDIVLGIEYLHYQK--IIHRDIKPSNLLLGDDGHVKIADFGvsnefegddallS 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  116 ATTISHY---PDyswsaqrrALVEEE-----------ALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPPHDTQYT 177
Cdd:cd14118    174 STAGTPAfmaPE--------ALSESRkkfsgkaldiwAMGVTLYCFVFGRCPFEDDHILGlhekIKTDPVVFPDDPVVSE 245

                          170       180
                   ....*....|....*....|...
gi 1034639258  178 VFHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14118    246 QLKDLILRMLDKNPSERITLPEI 268
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 11-201 3.48e-15

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: 77.28  E-value: 3.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   11 LAGPGSLGGASGRDQSDFVGQTVELGELRlrvrrvlaegQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppI 90
Cdd:cd14187     64 LAHQHVVGFHGFFEDNDFVYVVLELCRRR----------SLLELHKR---RKALTEPEARYYLRQIILGCQYLHRNR--V 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   91 IHRDLKVENLLLSNQGTIKLCDFGSATTISH----------YPDY----SWSAQRRAL-VEEEALGCILYLLCFRQHPFE 155
Cdd:cd14187    129 IHRDLKLGNLFLNDDMEVKIGDFGLATKVEYdgerkktlcgTPNYiapeVLSKKGHSFeVDIWSIGCIMYTLLVGKPPFE 208

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258  156 DG----AKLRIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14187    209 TSclkeTYLRIKKNEYSIPKHIN--PVAASLIQKMLQTDPTARPTINELL 256
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 47-200 5.28e-15

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: 76.53  E-value: 5.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   47 AEGQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT--------- 117
Cdd:cd14161     85 SRGDLYDYISE---RQRLSELEARHFFRQIVSAVHYCHANG--IVHRDLKLENILLDANGNIKIADFGLSNlynqdkflq 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 TISHYPDYS------WSAQRRALVEEEALGCILYLLCFRQHPFE--DGAKL--RIVNGKYSIPPHDTQYTvfhSLIRAML 187
Cdd:cd14161    160 TYCGSPLYAspeivnGRPYIGPEVDSWSLGVLLYILVHGTMPFDghDYKILvkQISSGAYREPTKPSDAC---GLIRWLL 236

                          170
                   ....*....|...
gi 1034639258  188 QVNPEERLSIAEV 200
Cdd:cd14161    237 MVNPERRATLEDV 249
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 64-202 7.62e-15

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: 75.88  E-value: 7.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT-----------TISHYPDYSWSA--Q 130
Cdd:cd14078     98 LSEDEARVFFRQIVSAVAYVHSQG--YAHRDLKPENLLLDEDQNLKLIDFGLCAkpkggmdhhleTCCGSPAYAAPEliQ 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  131 RRALVEEEA----LGCILY-LLC-FRqhPFEDG--AKL--RIVNGKYSIPPHDTQYTVFhsLIRAMLQVNPEERLSIAEV 200
Cdd:cd14078    176 GKPYIGSEAdvwsMGVLLYaLLCgFL--PFDDDnvMALyrKIQSGKYEEPEWLSPSSKL--LLDQMLQVDPKKRITVKEL 251


                   ..
gi 1034639258  201 VH 202
Cdd:cd14078    252 LN 253
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
 33-144 9.17e-15

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: 76.20  E-value: 9.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   33 VELGELRLRVRRV-----LAEGQLVEFLKkmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT 107
Cdd:cd07833     63 VNLKEAFRRKGRLylvfeYVERTLLELLE--ASPGGLPPDAVRSYIWQLLQAIAYCHSHN--IIHRDIKPENILVSESGV 138

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  108 IKLCDFGSATTI-----SHYPDYSWSAQRRA---LVEEE---------ALGCIL 144
Cdd:cd07833    139 LKLCDFGFARALtarpaSPLTDYVATRWYRApelLVGDTnygkpvdvwAIGCIM 192
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 58-200 1.09e-14

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: 75.72  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPDYSWSAQRRALVE 136
Cdd:cd05579     84 LENVGALDEDVARIYIAEIVLALEYLHSHG--IIHRDLKPDNILIDANGHLKLTDFGlSKVGLVRRQIKLSIQKKSNGAP 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  137 EE-----------------------------ALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQYTVFHSLI 183
Cdd:cd05579    162 EKedrrivgtpdylapeillgqghgktvdwwSLGVILYEFLVGIPPFhaETPEEIfqNILNGKIEWPEDPEVSDEAKDLI 241

                          170       180
                   ....*....|....*....|
gi 1034639258  184 RAMLQVNPEERL---SIAEV 200
Cdd:cd05579    242 SKLLTPDPEKRLgakGIEEI 261
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
 49-201 2.19e-14

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: 74.76  E-value: 2.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMEsrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFG------------- 114
Cdd:cd14074     87 GDMYDYIMKHE--NGLNEDLARKYFRQIVSAISYCHKLH--VVHRDLKPENVVFFeKQGLVKLTDFGfsnkfqpgeklet 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 -------SATTISHYPDYSWSAqrralVEEEALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHDTQYTvfHSLI 183
Cdd:cd14074    163 scgslaySAPEILLGDEYDAPA-----VDIWSLGVILYMLVCGQPPFQEANDsetlTMIMDCKYTVPAHVSPEC--KDLI 235

                          170
                   ....*....|....*...
gi 1034639258  184 RAMLQVNPEERLSIAEVV 201
Cdd:cd14074    236 RRMLIRDPKKRASLEEIE 253
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 49-201 2.27e-14

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: 74.79  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKkmeSRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattISHYpdYSWS 128
Cdd:cd14077     98 GQLLDYII---SHGKLKEKQARKFARQIASALDYLHRNS--IVHRDLKIENILISKSGNIKIIDFG----LSNL--YDPR 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  129 AQRRAL---------------------VEEEALGCILYLLCFRQHPFED----GAKLRIVNGKYSIPPHDTQYTVfhSLI 183
Cdd:cd14077    167 RLLRTFcgslyfaapellqaqpytgpeVDVWSFGVVLYVLVCGKVPFDDenmpALHAKIKKGKVEYPSYLSSECK--SLI 244

                          170
                   ....*....|....*...
gi 1034639258  184 RAMLQVNPEERLSIAEVV 201
Cdd:cd14077    245 SRMLVVDPKKRATLEQVL 262
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 53-200 2.64e-14

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: 74.74  E-value: 2.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT---IKLCDFGSAT---------TIS 120
Cdd:cd14084     97 ELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNG--IIHRDLKPENVLLSSQEEeclIKITDFGLSKilgetslmkTLC 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 HYPDY---------SWSAQRRAlVEEEALGCILYLLCFRQHPFED-----GAKLRIVNGKYS-IPPHDTQYTV-FHSLIR 184
Cdd:cd14084    175 GTPTYlapevlrsfGTEGYTRA-VDCWSLGVILFICLSGYPPFSEeytqmSLKEQILSGKYTfIPKAWKNVSEeAKDLVK 253

                          170
                   ....*....|....*.
gi 1034639258  185 AMLQVNPEERLSIAEV 200
Cdd:cd14084    254 KMLVVDPSRRPSIEEA 269
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 53-200 2.69e-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: 74.36  E-value: 2.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPDYSWSAQ- 130
Cdd:cd14663     86 ELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRG--VFHRDLKPENLLLDEDGNLKISDFGlSALSEQFRQDGLLHTTc 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  131 -RRALVEEEAL---------------GCILYLLCFRQHPFEDG--AKL--RIVNGKYSIPPHDTQYTVfhSLIRAMLQVN 190
Cdd:cd14663    164 gTPNYVAPEVLarrgydgakadiwscGVILFVLLAGYLPFDDEnlMALyrKIMKGEFEYPRWFSPGAK--SLIKRILDPN 241

                          170
                   ....*....|
gi 1034639258  191 PEERLSIAEV 200
Cdd:cd14663    242 PSTRITVEQI 251
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 49-203 2.91e-14

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: 74.00  E-value: 2.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGP--LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTI-KLCDFG---------SA 116
Cdd:cd08220     84 GTLFEYIQQ---RKGslLSEEEILHFFVQILLALHHVHSKQ--ILHRDLKTQNILLNKKRTVvKIGDFGiskilssksKA 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 TTISHYPDYSWS--AQRRALVEEE---ALGCILYLLCFRQHPFEdGAKL-----RIVNGKYSiPPHDTQYTVFHSLIRAM 186
Cdd:cd08220    159 YTVVGTPCYISPelCEGKPYNQKSdiwALGCVLYELASLKRAFE-AANLpalvlKIMRGTFA-PISDRYSEELRHLILSM 236

                          170
                   ....*....|....*..
gi 1034639258  187 LQVNPEERLSIAEVVHQ 203
Cdd:cd08220    237 LHLDPNKRPTLSEIMAQ 253
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 48-200 4.99e-14

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: 73.66  E-value: 4.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   48 EGQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------------- 114
Cdd:cd14165     86 QGDLLEFIKL---RGALPEDVARKMFHQLSSAIKYCHELD--IVHRDLKCENLLLDKDFNIKLTDFGfskrclrdengri 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 --SAT-----------TISHYPdY------SWSaqrralveeeaLGCILYLLCFRQHPFEDG---AKLRI-VNGKYSIPP 171
Cdd:cd14165    161 vlSKTfcgsaayaapeVLQGIP-YdpriydIWS-----------LGVILYIMVCGSMPYDDSnvkKMLKIqKEHRVRFPR 228

                          170       180
                   ....*....|....*....|....*....
gi 1034639258  172 HDTQYTVFHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14165    229 SKNLTSECKDLIYRLLQPDVSQRLCIDEV 257
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
 75-207 5.61e-14

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: 73.24  E-value: 5.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKP-PIIHRDLKVENLLLSNQGT-IKLCDFGSATTIS-HYPDYSWSAqrrALVEEEAL----------- 140
Cdd:cd14058     97 QCAKGVAYLHSMKPkALIHRDLKPPNLLLTNGGTvLKICDFGTACDIStHMTNNKGSA---AWMAPEVFegskysekcdv 173

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  141 ---GCILYLLCFRQHPFED--GAKLRIV----NGKYsiPPHDTQY-TVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd14058    174 fswGIILWEVITRRKPFDHigGPAFRIMwavhNGER--PPLIKNCpKPIESLMTRCWSKDPEKRPSMKEIVKIMSHL 248
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 58-201 5.62e-14

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: 73.50  E-value: 5.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRA---- 133
Cdd:cd13994     89 IEKADSLSLEEKDCFFKQILRGVAYLHSHG--IAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEKESPMSAGLcgse 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  134 --LVEEE--------------ALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPPHdTQYTVFH-----SLIRAM 186
Cdd:cd13994    167 pyMAPEVftsgsydgravdvwSCGIVLFALFTGRFPWrsakksDSAYKAYEKSGDFTNGPY-EPIENLLpsecrRLIYRM 245

                          170
                   ....*....|....*
gi 1034639258  187 LQVNPEERLSIAEVV 201
Cdd:cd13994    246 LHPDPEKRITIDEAL 260
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 69-201 8.64e-14

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: 72.84  E-value: 8.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   69 VLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNqGTIKLCDFG----------SATTISHYPDYswsAQRRALVEEE 138
Cdd:cd08222    108 ILDWFIQLLLAVQYMHERR--ILHRDLKAKNIFLKN-NVIKVGDFGisrilmgtsdLATTFTGTPYY---MSPEVLKHEG 181

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  139 --------ALGCILYLLCFRQHPFeDGAKL-----RIVNGKY-SIPPHDTqyTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd08222    182 ynsksdiwSLGCILYEMCCLKHAF-DGQNLlsvmyKIVEGETpSLPDKYS--KELNAIYSRMLNKDPALRPSAAEIL 255
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 71-202 1.33e-13

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 72.88  E-value: 1.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLL---SNQGTIKLCDFGSAT------TISHYPDYSWS-----AQRRALVE 136
Cdd:cd14171    113 QYTKQIALAVQHCHSLN--IAHRDLKPENLLLkdnSEDAPIKLCDFGFAKvdqgdlMTPQFTPYYVApqvleAQRRHRKE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  137 EE------------------ALGCILY-LLC-----FRQHP---FEDGAKLRIVNGKYSIPPHDTQYT--VFHSLIRAML 187
Cdd:cd14171    191 RSgiptsptpytydkscdmwSLGVIIYiMLCgyppfYSEHPsrtITKDMKRKIMTGSYEFPEEEWSQIseMAKDIVRKLL 270

                          170
                   ....*....|....*
gi 1034639258  188 QVNPEERLSIAEVVH 202
Cdd:cd14171    271 CVDPEERMTIEEVLH 285
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 49-203 1.34e-13

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 72.08  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKkmESRG-PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SAT 117
Cdd:cd08223     85 GDLYTRLK--EQKGvLLEERQVVEWFVQIAMALQYMHERN--ILHRDLKTQNIFLTKSNIIKVGDLGiarvlesssdMAT 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 TISHYPDYS----------------WsaqrralveeeALGCILYLLCFRQHPF--EDGAKL--RIVNGKysIPPHDTQY- 176
Cdd:cd08223    161 TLIGTPYYMspelfsnkpynhksdvW-----------ALGCCVYEMATLKHAFnaKDMNSLvyKILEGK--LPPMPKQYs 227

                          170       180
                   ....*....|....*....|....*..
gi 1034639258  177 TVFHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd08223    228 PELGELIKAMLHQDPEKRPSVKRILRQ 254
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
 73-201 1.71e-13

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: 71.78  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT---------TISHYPDYSWSA--QRRAL----VEE 137
Cdd:cd14072    105 FRQIVSAVQYCHQKR--IVHRDLKAENLLLDADMNIKIADFGFSNeftpgnkldTFCGSPPYAAPElfQGKKYdgpeVDV 182

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  138 EALGCILYLLCFRQHPFeDGAKL-----RIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14072    183 WSLGVILYTLVSGSLPF-DGQNLkelreRVLRGKYRIPFYMS--TDCENLLKKFLVLNPSKRGTLEQIM 248
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
 46-126 3.79e-13

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: 71.53  E-value: 3.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKmeSRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLsNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd07831     81 LMDMNLYELIKG--RKRPLPEKRVKNYMYQLLKSLDHMHRNG--IFHRDIKPENILI-KDDILKLADFGSCRGIYSKPPY 155


                   .
gi 1034639258  126 S 126
Cdd:cd07831    156 T 156
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 74-199 4.01e-13

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 71.30  E-value: 4.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   74 YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGSATTIS----HY------PDY-SWSAQRR----ALV 135
Cdd:cd14086    107 QQILESVNHCHQNG--IVHRDLKPENLLLASKskgAAVKLADFGLAIEVQgdqqAWfgfagtPGYlSPEVLRKdpygKPV 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  136 EEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd14086    185 DIWACGVILYILLVGYPPFwdEDQHRLyaQIKAGAYDYPSPewDTVTPEAKDLINQMLTVNPAKRITAAE 254
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 73-195 4.47e-13

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: 70.72  E-value: 4.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FYQTC--RAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS------------HY--P--------DYS-- 126
Cdd:cd05572     97 FYTACvvLAFEYLHSRG--IIYRDLKPENLLLDSNGYVKLVDFGFAKKLGsgrktwtfcgtpEYvaPeiilnkgyDFSvd 174

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  127 -WSaqrralveeeaLGCILY-LLCFRQhPF----EDGAKL--RIVNGKYSI--PPHDTQytVFHSLIRAMLQVNPEERL 195
Cdd:cd05572    175 yWS-----------LGILLYeLLTGRP-PFggddEDPMKIynIILKGIDKIefPKYIDK--NAKNLIKQLLRRNPEERL 239
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 49-201 5.90e-13

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 70.10  E-value: 5.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWS 128
Cdd:cd13997     85 GSLQDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKG--IVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEG 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  129 AQR---RALVEEE----------ALGCILYLLCfRQHPFEDGAKL--RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEE 193
Cdd:cd13997    163 DSRylaPELLNENythlpkadifSLGVTVYEAA-TGEPLPRNGQQwqQLRQGKLPLPPGLVLSQELTRLLKVMLDPDPTR 241


                   ....*...
gi 1034639258  194 RLSIAEVV 201
Cdd:cd13997    242 RPTADQLL 249
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 49-201 7.40e-13

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: 70.20  E-value: 7.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRGPLSCDTVLKifyQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSATTISH----- 121
Cdd:cd14098     86 GDLMDFIMAWGAIPEQHARELTK---QILEAMAYTHSMG--ITHRDLKPENILITQDDPviVKISDFGLAKVIHTgtflv 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 -------Y--PDYSWSAQRRA------LVEEEALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPhDTQYTVFH-- 180
Cdd:cd14098    161 tfcgtmaYlaPEILMSKEQNLqggysnLVDMWSVGCLVYVMLTGALPFDGSSQLpvekRIRKGRYTQPP-LVDFNISEea 239

                          170       180
                   ....*....|....*....|..
gi 1034639258  181 -SLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14098    240 iDFILRLLDVDPEKRMTAAQAL 261
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 61-199 8.08e-13

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: 70.07  E-value: 8.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   61 RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSATTISHYPDYSWSAQRR------- 132
Cdd:cd13993    101 IYVGKTELIKNVFLQLIDAVKHCHSLG--IYHRDIKPENILLSQDeGTVKLCDFGLATTEKISMDFGVGSEFYmapecfd 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  133 -----------ALVEEEALGCILYLLCFRQHPFEDGAKLRIVNGKY---------SIPPhDTQytVFHSLIRAMLQVNPE 192
Cdd:cd13993    179 evgrslkgypcAAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYylnspnlfdVILP-MSD--DFYNLLRQIFTVNPN 255


                   ....*..
gi 1034639258  193 ERLSIAE 199
Cdd:cd13993    256 NRILLPE 262
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 71-200 8.90e-13

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: 70.08  E-value: 8.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI-----------------------SHYPDYSW 127
Cdd:cd14093    113 RIMRQLFEAVEFLHSLN--IVHRDLKPENILLDDNLNVKISDFGFATRLdegeklrelcgtpgylapevlkcSMYDNAPG 190

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  128 SAQRralVEEEALGCILYLLCFRQHPFEDGAKL----RIVNGKYSI--PPHDTQYTVFHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14093    191 YGKE---VDMWACGVIMYTLLAGCPPFWHRKQMvmlrNIMEGKYEFgsPEWDDISDTAKDLISKLLVVDPKKRLTAEEA 266
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 39-203 1.04e-12

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: 69.84  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   39 RLRVRRVLAEG-QLVEFLKKM-ESRGPLSCDTVLKIFYQTCRAVQHMHRQKPpIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd08528     83 RLYIVMELIEGaPLGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHKEKQ-IVHRDLKPNNIMLGEDDKVTITDFGLA 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 TTISHYPDYSWSAQRRAL------VEEE---------ALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYT 177
Cdd:cd08528    162 KQKGPESSKMTSVVGTILyscpeiVQNEpygekadiwALGCILYQMCTLQPPFYSTNMLtlatKIVEAEYEPLPEGMYSD 241

                          170       180
                   ....*....|....*....|....*.
gi 1034639258  178 VFHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd08528    242 DITFVIRSCLTPDPEARPDIVEVSSM 267
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 48-200 1.17e-12

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: 69.55  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   48 EGQLVEFLKKMESRgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNqGTIKLCDFGSATTIshyPDYSW 127
Cdd:cd14131     85 EIDLATILKKKRPK-PIDPNFIRYYWKQMLEAVHTIHEEG--IVHSDLKPANFLLVK-GRLKLIDFGIAKAI---QNDTT 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  128 SAQR------------RALVEEEA------------------LGCILYLLCFRQHPFED----GAKL-RIVNGKYSI--P 170
Cdd:cd14131    158 SIVRdsqvgtlnymspEAIKDTSAsgegkpkskigrpsdvwsLGCILYQMVYGKTPFQHitnpIAKLqAIIDPNHEIefP 237

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034639258  171 PHDTQytvfhSLIRAM---LQVNPEERLSIAEV 200
Cdd:cd14131    238 DIPNP-----DLIDVMkrcLQRDPKKRPSIPEL 265
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 48-200 1.31e-12

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: 69.87  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   48 EGQLVEFLKKMESRgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYS- 126
Cdd:cd07830     81 EGNLYQLMKDRKGK-PFSESVIRSIIYQILQGLAHIHKHG--FFHRDLKPENLLVSGPEVVKIADFGLAREIRSRPPYTd 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 -----W---------SAQRRALVEEEALGCI-------------------LYLLC-----FRQHPFEDGAKL-RIVNGKY 167
Cdd:cd07830    158 yvstrWyrapeillrSTSYSSPVDIWALGCImaelytlrplfpgsseidqLYKICsvlgtPTKQDWPEGYKLaSKLGFRF 237

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034639258  168 ----SIPPHD---TQYTVFHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd07830    238 pqfaPTSLHQlipNASPEAIDLIKDMLRWDPKKRPTASQA 277
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 67-203 4.23e-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: 67.84  E-value: 4.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   67 DTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPdYSWSAQrraLVE 136
Cdd:cd08221    101 EVVLWYLYQIVSAVSHIH--KAGILHRDIKTLNIFLTKADLVKLGDFGiskvldsessMAESIVGTP-YYMSPE---LVQ 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  137 EE---------ALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIppHDTQYTV-FHSLIRAMLQVNPEERLSIAEVVH 202
Cdd:cd08221    175 GVkynfksdiwAVGCVLYELLTLKRTFDATNPLRlavkIVQGEYED--IDEQYSEeIIQLVHDCLHQDPEDRPTAEELLE 252


                   .
gi 1034639258  203 Q 203
Cdd:cd08221    253 R 253
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 51-199 5.77e-12

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: 67.29  E-value: 5.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG--TIKLCDFGSATTIS-HYPDYSW 127
Cdd:cd14133     87 LYEFLKQNKFQY-LSLPRIRKIAQQILEALVFLHSLG--LIHCDLKPENILLASYSrcQIKIIDFGSSCFLTqRLYSYIQ 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  128 SAQRRA------LVEEEA-----LGCILYLLCFRqHPFEDGAKL-----RIVNGKYSIPPH-----DTQYTVFHSLIRAM 186
Cdd:cd14133    164 SRYYRApevilgLPYDEKidmwsLGCILAELYTG-EPLFPGASEvdqlaRIIGTIGIPPAHmldqgKADDELFVDFLKKL 242

                          170
                   ....*....|...
gi 1034639258  187 LQVNPEERLSIAE 199
Cdd:cd14133    243 LEIDPKERPTASQ 255
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
 71-200 6.78e-12

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: 67.91  E-value: 6.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSA-------TTIS-----HY---------PDYS- 126
Cdd:cd14137    109 KLYsYQLFRGLAYLHSLG--ICHRDIKPQNLLVDPEtGVLKLCDFGSAkrlvpgePNVSyicsrYYrapelifgaTDYTt 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 ----WSAqrralveeealGCILYLLcFRQHPF---EDGAK--LRIV--------------NGKYS------IPPHDTQyT 177
Cdd:cd14137    187 aidiWSA-----------GCVLAEL-LLGQPLfpgESSVDqlVEIIkvlgtptreqikamNPNYTefkfpqIKPHPWE-K 253

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034639258  178 VFHS--------LIRAMLQVNPEERLSIAEV 200
Cdd:cd14137    254 VFPKrtppdaidLLSKILVYNPSKRLTALEA 284
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
 58-199 1.76e-11

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: 66.00  E-value: 1.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLScDTVLKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQRRALV- 135
Cdd:cd06606     90 LKKFGKLP-EPVVRKYtRQILEGLEYLHSNG--IVHRDIKGANILVDSDGVVKLADFGCAKRLA---EIATGEGTKSLRg 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  136 -----------EEE--------ALGCILYLLCFRQHPFED-----GAKLRIVNGKYS--IPPHDTQytVFHSLIRAMLQV 189
Cdd:cd06606    164 tpywmapevirGEGygraadiwSLGCTVIEMATGKPPWSElgnpvAALFKIGSSGEPppIPEHLSE--EAKDFLRKCLQR 241

                          170
                   ....*....|
gi 1034639258  190 NPEERLSIAE 199
Cdd:cd06606    242 DPKKRPTADE 251
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 50-204 1.91e-11

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: 66.20  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   50 QLVEFLKKMESRGPLScdTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------SATTISHY- 122
Cdd:cd08228     91 QMIKYFKKQKRLIPER--TVWKYFVQLCSAVEHMHSRR--VMHRDIKPANVFITATGVVKLGDLGlgrffsSKTTAAHSl 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 --PDYSWSAQRralVEEE---------ALGCILYLLCFRQHPFEdGAKLRIVNGKYSI-----PPHDTQY--TVFHSLIR 184
Cdd:cd08228    167 vgTPYYMSPER---IHENgynfksdiwSLGCLLYEMAALQSPFY-GDKMNLFSLCQKIeqcdyPPLPTEHysEKLRELVS 242

                          170       180
                   ....*....|....*....|
gi 1034639258  185 AMLQVNPEERLSIAeVVHQL 204
Cdd:cd08228    243 MCIYPDPDQRPDIG-YVHQI 261
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
 58-116 2.04e-11

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: 66.48  E-value: 2.04e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MES-RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07843     96 METmKQPFLQSEVKCLMLQLLSGVAHLHDNW--ILHRDLKTSNLLLNNRGILKICDFGLA 153
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
 49-204 2.74e-11

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 65.24  E-value: 2.74e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258    49 GQLVEFLKKmeSRGPLSCDTVLKIFYQTCRAVQHMHRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYpDYSWS 128
Cdd:smart00219   86 GDLLSYLRK--NRPKLSLSDLLSFALQIARGMEYLESK--NFIHRDLAARNCLVGENLVVKISDFGLSRDLYDD-DYYRK 160

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   129 AQRR------ALveeEAL--------------GCILY-LLCFRQHPFED--GAKL--RIVNGKY-SIPPHDTQYtvFHSL 182
Cdd:smart00219  161 RGGKlpirwmAP---ESLkegkftsksdvwsfGVLLWeIFTLGEQPYPGmsNEEVleYLKNGYRlPQPPNCPPE--LYDL 235

                           170       180
                    ....*....|....*....|..
gi 1034639258   183 IRAMLQVNPEERLSIAEVVHQL 204
Cdd:smart00219  236 MLQCWAEDPEDRPTFSELVEIL 257
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
 67-125 3.23e-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: 65.47  E-value: 3.23e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   67 DTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd07847    100 HLIKKIIWQTLQAVNFCHKHN--CIHRDVKPENILITKQGQIKLCDFGFARILTGPGDD 156
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
 49-204 3.27e-11

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: 65.26  E-value: 3.27e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258    49 GQLVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwS 128
Cdd:smart00221   86 GDLLDYLRKNRPKE-LSLSDLLSFALQIARGMEYLESKN--FIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYK-V 161

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   129 AQRR------ALveeEAL--------------GCILY-LLCFRQHPFE--DGAKL--RIVNGKY-SIPPHDTQYtvFHSL 182
Cdd:smart00221  162 KGGKlpirwmAP---ESLkegkftsksdvwsfGVLLWeIFTLGEEPYPgmSNAEVleYLKKGYRlPKPPNCPPE--LYKL 236

                           170       180
                    ....*....|....*....|..
gi 1034639258   183 IRAMLQVNPEERLSIAEVVHQL 204
Cdd:smart00221  237 MLQCWAEDPEDRPTFSELVEIL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
59-155 3.34e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.51  E-value: 3.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   59 ESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-----SATTIS---------HY-- 122
Cdd:NF033483    99 REHGPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILITKDGRVKVTDFGiaralSSTTMTqtnsvlgtvHYls 176

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034639258  123 PDyswsaQ-RRALVEEE----ALGCILY-LLCFRQhPFE 155
Cdd:NF033483   177 PE-----QaRGGTVDARsdiySLGIVLYeMLTGRP-PFD 209
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
 70-200 3.35e-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: 65.37  E-value: 3.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   70 LKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-----NQGTIKLCDFG----------SATTISHYPD-YSWSA---- 129
Cdd:cd13982    102 VRLLRQIASGLAHLHSLN--IVHRDLKPQNILIStpnahGNVRAMISDFGlckkldvgrsSFSRRSGVAGtSGWIApeml 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 -------QRRAlVEEEALGCIL-YLLCFRQHPFedGAKLR----IVNGKYSIP---PHDTQYTVFHSLIRAMLQVNPEER 194
Cdd:cd13982    180 sgstkrrQTRA-VDIFSLGCVFyYVLSGGSHPF--GDKLEreanILKGKYSLDkllSLGEHGPEAQDLIERMIDFDPEKR 256


                   ....*.
gi 1034639258  195 LSIAEV 200
Cdd:cd13982    257 PSAEEV 262
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 49-201 4.01e-11

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: 64.88  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKkmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS-----HY- 122
Cdd:cd14186     86 GEMSRYLK--NRKKPFTEDEARHFMHQIVTGMLYLHSHG--ILHRDLTLSNLLLTRNMNIKIADFGLATQLKmphekHFt 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 ----PDY--SWSAQRRALVEEE---ALGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPPHDTQYTvfHSLIRAMLQV 189
Cdd:cd14186    162 mcgtPNYisPEIATRSAHGLESdvwSLGCMFYTLLVGRPPFDTDTVKNTLNkvvlADYEMPAFLSREA--QDLIHQLLRK 239

                          170
                   ....*....|..
gi 1034639258  190 NPEERLSIAEVV 201
Cdd:cd14186    240 NPADRLSLSSVL 251
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 46-207 6.16e-11

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: 64.60  E-value: 6.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHR-QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISH--- 121
Cdd:cd14066     72 MPNGSLEDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPses 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 ------------Y--PDYSWSaqRRALVEEE--ALGCILYLLCFRQHPFEDG----AKLRIV-----NGKYS----IPPH 172
Cdd:cd14066    152 vsktsavkgtigYlaPEYIRT--GRVSTKSDvySFGVVLLELLTGKPAVDENrenaSRKDLVewvesKGKEElediLDKR 229

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034639258  173 -DTQYTVFHSLIRAMLQV-------NPEERLSIAEVVHQLQEI 207
Cdd:cd14066    230 lVDDDGVEEEEVEALLRLallctrsDPSLRPSMKEVVQMLEKL 272
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 49-199 6.33e-11

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: 64.17  E-value: 6.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS---NQGTIKLCDFGSATTIS----- 120
Cdd:cd14009     77 GDLSQYIRK---RGRLPEAVARHFMQQLASGLKFLRSKN--IIHRDLKPQNLLLStsgDDPVLKIADFGFARSLQpasma 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 ---------------HYPDYS-----WSaqrralveeeaLGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQY 176
Cdd:cd14009    152 etlcgsplymapeilQFQKYDakadlWS-----------VGAILFEMLVGKPPFRGSNHVqllrNIERSDAVIPFPIAAQ 220

                          170       180
                   ....*....|....*....|....*
gi 1034639258  177 TVFH--SLIRAMLQVNPEERLSIAE 199
Cdd:cd14009    221 LSPDckDLLRRLLRRDPAERISFEE 245
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 58-204 7.40e-11

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: 64.24  E-value: 7.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLSC---DTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSATTISHYPDYSWSA---- 129
Cdd:cd13996     95 IDRRNSSSKndrKLALELFKQILKGVSYIHSKG--IVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQKRELNNLnnnn 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 --------------------QRRAL-----VEEEALGCILY-LLCFRQHPFEdgaKLRIVNG--KYSIPPH-DTQYTVFH 180
Cdd:cd13996    173 ngntsnnsvgigtplyaspeQLDGEnynekADIYSLGIILFeMLHPFKTAME---RSTILTDlrNGILPESfKAKHPKEA 249

                          170       180
                   ....*....|....*....|....
gi 1034639258  181 SLIRAMLQVNPEERLSIAEVVHQL 204
Cdd:cd13996    250 DLIQSLLSKNPEERPSAEQLLRSL 273
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
 63-205 8.10e-11

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: 64.60  E-value: 8.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA----------TTISHYPDY----SWS 128
Cdd:cd14199    122 PLSEDQARFYFQDLIKGIEYLHYQK--IIHRDVKPSNLLVGEDGHIKIADFGVSnefegsdallTNTVGTPAFmapeTLS 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  129 AQRRAL----VEEEALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEV 200
Cdd:cd14199    200 ETRKIFsgkaLDVWAMGVTLYCFVFGQCPFMDERILslhsKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEI 279


                   ....*.
gi 1034639258  201 -VHQLQ 205
Cdd:cd14199    280 kLHPWV 285
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 73-200 1.73e-10

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: 63.11  E-value: 1.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FYQTCRAVQHMHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGSAT-------TISHYPDYswsaqrralVEEE--- 138
Cdd:cd14095    104 VTDLAQALKYLHSLS--IVHRDIKPENLLVveheDGSKSLKLADFGLATevkeplfTVCGTPTY---------VAPEila 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  139 -----------ALGCILY-LLC----FRQhPFEDGAKL--RIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIA 198
Cdd:cd14095    173 etgyglkvdiwAAGVITYiLLCgfppFRS-PDRDQEELfdLILAGEFEFLSPywDNISDSAKDLISRMLVVDPEKRYSAG 251


                   ..
gi 1034639258  199 EV 200
Cdd:cd14095    252 QV 253
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 49-125 2.05e-10

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: 62.90  E-value: 2.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKmeSRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:pfam07714   86 GDLLDFLRK--HKRKLTLKDLLSMALQIAKGMEYLESKN--FVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYY 158
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
 42-207 2.16e-10

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: 63.01  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAT---- 117
Cdd:cd14026     75 VTEYMTNGSLNELLHEKDIYPDVAWPLRLRILYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKwrql 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 ---------------TISHYP--DYSWSAQRRALVEEE--ALGCILYLLCFRQHPFEDGAK-----------LRIVNGKY 167
Cdd:cd14026    155 sisqsrssksapeggTIIYMPpeEYEPSQKRRASVKHDiySYAIIMWEVLSRKIPFEEVTNplqimysvsqgHRPDTGED 234

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034639258  168 SIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd14026    235 SLPVDIPHRATLINLIESGWAQNPDERPSFLKCLIELEPV 274
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
 48-121 2.41e-10

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: 63.15  E-value: 2.41e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   48 EGQLVEFLKKMESrgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH 121
Cdd:cd07845     91 EQDLASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENF--IIHRDLKVSNLLLTDKGCLKIADFGLARTYGL 160
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 79-199 2.52e-10

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: 62.22  E-value: 2.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD--------------------YS-----WSaqrra 133
Cdd:cd05122    110 GLEYLHSHG--IIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTrntfvgtpywmapeviqgkpYGfkadiWS----- 182

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  134 lveeeaLGCILYLLCFRQHPFEDGAKLRI-----VNGKYSIpPHDTQYT-VFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd05122    183 ------LGITAIEMAEGKPPYSELPPMKAlfliaTNGPPGL-RNPKKWSkEFKDFLKKCLQKDPEKRPTAEQ 247
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 51-199 2.99e-10

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 62.95  E-value: 2.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSATTiSHYPDYSWS 128
Cdd:cd14210    101 LYELLKSNNFQG-LSLSLIRKFAKQILQALQFLHKLN--IIHCDLKPENILLKQPSKssIKVIDFGSSCF-EGEKVYTYI 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  129 AQR--RA---------------------LVE-------------EEALGCILYLL----------CFRQHPFEDG---AK 159
Cdd:cd14210    177 QSRfyRApevilglpydtaidmwslgciLAElytgyplfpgeneEEQLACIMEVLgvppkslidkASRRKKFFDSngkPR 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034639258  160 LRIVNGKYSIPP--------HDTQYTVFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd14210    257 PTTNSKGKKRRPgskslaqvLKCDDPSFLDFLKKCLRWDPSERMTPEE 304
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
 64-125 3.19e-10

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: 62.44  E-value: 3.19e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH----YPDY 125
Cdd:cd07846     97 LDESRVRKYLFQILRGIDFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFARTLAApgevYTDY 160
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
 49-206 5.25e-10

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: 61.45  E-value: 5.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKPpIIHRDLKVENLLLSNQGTIKLCDFGSATTISH--YPDYS 126
Cdd:cd06623     84 GSLADLLKK---VGKIPEPVLAYIARQILKGLDYLHTKRH-IIHRDIKPSNLLINSKGEVKIADFGISKVLENtlDQCNT 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 W-------SAQRraLVEEE--------ALGCILYLLCFRQHPFEDGAK------LRIVNGKYSIPPHDTQYTV-FHSLIR 184
Cdd:cd06623    160 FvgtvtymSPER--IQGESysyaadiwSLGLTLLECALGKFPFLPPGQpsffelMQAICDGPPPSLPAEEFSPeFRDFIS 237

                          170       180
                   ....*....|....*....|..
gi 1034639258  185 AMLQVNPEERLSiaevVHQLQE 206
Cdd:cd06623    238 ACLQKDPKKRPS----AAELLQ 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
 72-202 5.84e-10

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: 61.81  E-value: 5.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS--HYPDYS----------------------- 126
Cdd:cd07840    109 YMKQLLEGLQYLHSNG--ILHRDIKGSNILINNDGVLKLADFGLARPYTkeNNADYTnrvitlwyrppelllgatrygpe 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 ---WSA--------QRRALV----EEEALGCIlYLLC----------FRQHPFEDGAKL-----RIVNGKYS--IPPHdt 174
Cdd:cd07840    187 vdmWSVgcilaelfTGKPIFqgktELEQLEKI-FELCgspteenwpgVSDLPWFENLKPkkpykRRLREVFKnvIDPS-- 263

                          170       180
                   ....*....|....*....|....*...
gi 1034639258  175 qytvFHSLIRAMLQVNPEERLSIAEVVH 202
Cdd:cd07840    264 ----ALDLLDKLLTLDPKKRISADQALQ 287
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
 51-202 6.00e-10

Catalytic domain of the Dual-specificity protein kinases, CDC-like 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. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 62.20  E-value: 6.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKMESRG-PLSCdtVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSN-------------------QGTIKL 110
Cdd:cd14134    100 LYDFLKKNNYGPfPLEH--VQHIAKQLLEAVAFLHDLK--LTHTDLKPENILLVDsdyvkvynpkkkrqirvpkSTDIKL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  111 CDFGSAT--------TIS--HY--P--------DYS---WSaqrralveeeaLGCILYLLC-----FRQH---------- 152
Cdd:cd14134    176 IDFGSATfddeyhssIVStrHYraPevilglgwSYPcdvWS-----------IGCILVELYtgellFQTHdnlehlamme 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  153 ------P--------------FEDGAKLR----IVNGKY-------------SIPPHDTQytvFHSLIRAMLQVNPEERL 195
Cdd:cd14134    245 rilgplPkrmirrakkgakyfYFYHGRLDwpegSSSGRSikrvckplkrlmlLVDPEHRL---LFDLIRKMLEYDPSKRI 321


                   ....*..
gi 1034639258  196 SIAEVVH 202
Cdd:cd14134    322 TAKEALK 328
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
 49-114 9.51e-10

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: 61.16  E-value: 9.51e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKMESRG-PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06608     94 GSVTDLVKGLRKKGkRLKEEWIAYILRETLRGLAYLHENK--VIHRDIKGQNILLTEEAEVKLVDFG 158
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 46-121 9.97e-10

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: 61.11  E-value: 9.97e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   46 LAEGQLVEFLKkmesRGPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTISH 121
Cdd:cd06609     81 CGGGSVLDLLK----PGPLDETYIAFILREVLLGLEYLHSEGK--IHRDIKAANILLSEEGDVKLADFGVSGQLTS 150
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 49-214 1.09e-09

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: 60.57  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT---------I 119
Cdd:cd05611     82 GDCASLIKTL---GGLPEDWAKQYIAEVVLGVEDLHQRG--IIHRDIKPENLLIDQTGHLKLTDFGLSRNglekrhnkkF 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  120 SHYPDYS-----WSAQRRALVEEEALGCILYLLCFRQHPFE----DGAKLRIVNGKYSIPPHDTQY--TVFHSLIRAMLQ 188
Cdd:cd05611    157 VGTPDYLapetiLGVGDDKMSDWWSLGCVIFEFLFGYPPFHaetpDAVFDNILSRRINWPEEVKEFcsPEAVDLINRLLC 236

                          170       180
                   ....*....|....*....|....*.
gi 1034639258  189 VNPEERLSiAEVVHQLQEIAAARNVN 214
Cdd:cd05611    237 MDPAKRLG-ANGYQEIKSHPFFKSIN 261
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
 51-116 1.76e-09

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: 60.37  E-value: 1.76e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQ--HMHRqkppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07838     92 LATYLDKCPKPG-LPPETIKDLMRQLLRGLDflHSHR----IVHRDLKPQNILVTSDGQVKLADFGLA 154
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 49-205 1.90e-09

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: 59.86  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKM------ESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY 122
Cdd:cd00192     81 GDLLDFLRKSrpvfpsPEPSTLSLKDLLSFAIQIAKGMEYLASKK--FVHRDLAARNCLVGEDLVVKISDFGLSRDIYDD 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 PDYSWSAQRR---------ALVEEE--------ALGCILY-LLCFRQHPFE----DGAKLRIVNGKY-SIPPHDTQYtvF 179
Cdd:cd00192    159 DYYRKKTGGKlpirwmapeSLKDGIftsksdvwSFGVLLWeIFTLGATPYPglsnEEVLEYLRKGYRlPKPENCPDE--L 236

                          170       180
                   ....*....|....*....|....*.
gi 1034639258  180 HSLIRAMLQVNPEERLSIAEVVHQLQ 205
Cdd:cd00192    237 YELMLSCWQLDPEDRPTFSELVERLE 262
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
 73-195 2.07e-09

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: 60.29  E-value: 2.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT-------TISHYPDY------SWSAQRRAlVEE 137
Cdd:cd05580    105 FYaaEVVLALEYLHSLD--IVYRDLKPENLLLDSDGHIKITDFGFAKrvkdrtyTLCGTPEYlapeiiLSKGHGKA-VDW 181

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  138 EALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQytVFHSLIRAMLQVNPEERL 195
Cdd:cd05580    182 WALGILIYEMLAGYPPFFDENPMkiyeKILEGKIRFPSFFDP--DAKDLIKRLLVVDLTKRL 241
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
 53-195 2.13e-09

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 60.50  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVlkIFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------SATTISH--- 121
Cdd:cd05584     86 ELFMHLEREGIFMEDTA--CFYlaEITLALGHLHSLG--IIYRDLKPENILLDAQGHVKLTDFGlckesiHDGTVTHtfc 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 ----Y--PD-YSWSAQRRAlVEEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQYTVfhSLIRAMLQVN 190
Cdd:cd05584    162 gtieYmaPEiLTRSGHGKA-VDWWSLGALMYDMLTGAPPFtaENRKKTidKILKGKLNLPPYLTNEAR--DLLKKLLKRN 238


                   ....*
gi 1034639258  191 PEERL 195
Cdd:cd05584    239 VSSRL 243
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
 70-205 2.71e-09

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 59.73  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   70 LKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLsNQGT--IKLCDF-----------------GSATTIShyPD-YSWSA 129
Cdd:cd13974    135 LVIFYDVVRVVEALH--KKNIVHRDLKLGNMVL-NKRTrkITITNFclgkhlvseddllkdqrGSPAYIS--PDvLSGKP 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 QRRALVEEEALGCILYLLCFRQHPFEDGA--KL--RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQ 205
Cdd:cd13974    210 YLGKPSDMWALGVVLFTMLYGQFPFYDSIpqELfrKIKAAEYTIPEDGRVSENTVCLIRKLLVLNPQKRLTASEVLDSLE 289
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
 53-202 2.96e-09

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: 59.58  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKK---ME--SRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------------S 115
Cdd:cd14200    105 DLLRKgpvMEvpSDKPFSEDQARLYFRDIVLGIEYLHYQK--IVHRDIKPSNLLLGDDGHVKIADFGvsnqfegndallS 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  116 AT----------TIShypDYSWSAQRRALvEEEALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTVFHS 181
Cdd:cd14200    183 STagtpafmapeTLS---DSGQSFSGKAL-DVWAMGVTLYCFVYGKCPFIDEFILalhnKIKNKPVEFPEEPEISEELKD 258

                          170       180
                   ....*....|....*....|..
gi 1034639258  182 LIRAMLQVNPEERLSIAEV-VH 202
Cdd:cd14200    259 LILKMLDKNPETRITVPEIkVH 280
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
 49-114 3.13e-09

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: 59.28  E-value: 3.13e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   49 GQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHrQKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06605     84 GSLDKILKEV---GRIPERILGKIAVAVVKGLIYLH-EKHKIIHRDVKPSNILVNSRGQVKLCDFG 145
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 61-201 4.02e-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: 58.71  E-value: 4.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   61 RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTI--SHYPDY---------SW- 127
Cdd:cd14101    102 RGALDESLARRFFKQVVEAVQHCHSKG--VVHRDIKDENILVDlRTGDIKLIDFGSGATLkdSMYTDFdgtrvysppEWi 179

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  128 -SAQRRAL-VEEEALGCILYLLCFRQHPFEDGAKlrIVNGKYSIPPH---DTQytvfhSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14101    180 lYHQYHALpATVWSLGILLYDMVCGDIPFERDTD--ILKAKPSFNKRvsnDCR-----SLIRSCLAYNPSDRPSLEQIL 251
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
 45-200 4.17e-09

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: 58.72  E-value: 4.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   45 VLAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG-TIKLCDFGSATTISHYP 123
Cdd:cd14164     78 IVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMN--IVHRDLKCENILLSADDrKIKIADFGFARFVEDYP 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 DYSWS-AQRRALVEEE---------------ALGCILYLLCFRQHPFEDGAKLRIVNGKYSI--PPHDTQYTVFHSLIRA 185
Cdd:cd14164    156 ELSTTfCGSRAYTPPEvilgtpydpkkydvwSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVlyPSGVALEEPCRALIRT 235

                          170
                   ....*....|....*
gi 1034639258  186 MLQVNPEERLSIAEV 200
Cdd:cd14164    236 LLQFNPSTRPSIQQV 250
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
 79-196 4.19e-09

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: 58.81  E-value: 4.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA---------TTISHYPDYS-----WSAQRRALVEEEALGCIL 144
Cdd:cd05578    112 ALDYLHSKN--IIHRDIKPDNILLDEQGHVHITDFNIAtkltdgtlaTSTSGTKPYMapevfMRAGYSFAVDWWSLGVTA 189

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  145 YLLCFRQHPFE-------DGAKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERLS 196
Cdd:cd05578    190 YEMLRGKRPYEihsrtsiEEIRAKFETASVLYPAGWSEEAI--DLINKLLERDPQKRLG 246
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
 75-120 4.22e-09

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: 58.76  E-value: 4.22e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06614    105 EVLQGLEYLHSQN--VIHRDIKSDNILLSKDGSVKLADFGFAAQLT 148
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 70-204 4.45e-09

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: 59.04  E-value: 4.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   70 LKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEE----------- 138
Cdd:cd14047    120 LEIFEQITKGVEYIHSKK--LIHRDLKPSNIFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEqissqdygkev 197

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  139 ---ALGCILYLLCfrqHPFEDG-------AKLRivNGKysIPPH-DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQL 204
Cdd:cd14047    198 diyALGLILFELL---HVCDSAfekskfwTDLR--NGI--LPDIfDKRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
 72-120 5.25e-09

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: 59.49  E-value: 5.25e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07852    112 IMYQLLKALKYLHSGG--VIHRDLKPSNILLNSDCRVKLADFGLARSLS 158
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 46-202 7.04e-09

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: 58.08  E-value: 7.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAE-GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD 124
Cdd:cd14162     81 LAEnGDLLDYIRK---NGALPEPQARRWFRQLVAGVEYCHSKG--VVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKD 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  125 YSWSAQRR-----ALVEEE---------------ALGCILYLLCFRQHPFEDG---AKLRIVNGKYSIPPHDTQYTVFHS 181
Cdd:cd14162    156 GKPKLSETycgsyAYASPEilrgipydpflsdiwSMGVVLYTMVYGRLPFDDSnlkVLLKQVQRRVVFPKNPTVSEECKD 235

                          170       180
                   ....*....|....*....|.
gi 1034639258  182 LIRAMLqVNPEERLSIAEVVH 202
Cdd:cd14162    236 LILRML-SPVKKRITIEEIKR 255
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
 73-195 8.10e-09

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: 58.77  E-value: 8.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATT-----------ISHYPDYSWSa 129
Cdd:cd05570    100 FYaaEICLALQFLHERG--IIYRDLKLDNVLLDAEGHIKIADFGmckegiwggnTTSTfcgtpdyiapeILREQDYGFS- 176

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 qrralVEEEALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERL 195
Cdd:cd05570    177 -----VDWWALGVLLYEMLAGQSPFegddEDELFEAILNDEVLYPRWLSREAV--SILKGLLTKDPARRL 239
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
 55-124 9.20e-09

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: 58.69  E-value: 9.20e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   55 LKKM-ESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD 124
Cdd:cd07834     90 LHKViKSPQPLTDDHIQYFLYQILRGLKYLHSAG--VIHRDLKPSNILVNSNCDLKICDFGLARGVDPDED 158
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
 55-116 1.27e-08

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: 57.69  E-value: 1.27e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   55 LKK-MES--RGPLSCDTVLKIFYQTCRAVQ--HMHRqkppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07835     84 LKKyMDSspLTGLDPPLIKSYLYQLLQGIAfcHSHR----VLHRDLKPQNLLIDTEGALKLADFGLA 146
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
 49-207 1.45e-08

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: 56.89  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRgPLSCDTVLKIFYQTCRAVQHMHRQKP-PIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYP---- 123
Cdd:cd14060     67 GSLFDYLNSNESE-EMDMDQIMTWATDIAKGMHYLHMEAPvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTThmsl 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 --DYSWSAQR-------RALVEEEALGCILYLLCFRQHPFEDGAKLRIV------NGKYSIPphDTQYTVFHSLIRAMLQ 188
Cdd:cd14060    146 vgTFPWMAPEviqslpvSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAwlvvekNERPTIP--SSCPRSFAELMRRCWE 223

                          170
                   ....*....|....*....
gi 1034639258  189 VNPEERLSIAEVVHQLQEI 207
Cdd:cd14060    224 ADVKERPSFKQIIGILESM 242
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 53-200 1.86e-08

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: 56.92  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL--SNQGTIKLCDFG-SATTISHYPDYSwSA 129
Cdd:cd14665     82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQ--ICHRDLKLENTLLdgSPAPRLKICDFGySKSSVLHSQPKS-TV 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 QRRALVEEEAL---------------GCILYLLCFRQHPFEDGAK--------LRIVNGKYSIPPHDTQYTVFHSLIRAM 186
Cdd:cd14665    159 GTPAYIAPEVLlkkeydgkiadvwscGVTLYVMLVGAYPFEDPEEprnfrktiQRILSVQYSIPDYVHISPECRHLISRI 238

                          170
                   ....*....|....
gi 1034639258  187 LQVNPEERLSIAEV 200
Cdd:cd14665    239 FVADPATRITIPEI 252
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
 47-116 1.96e-08

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: 57.39  E-value: 1.96e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   47 AEGQLVEFLKkmesRGPLSCDTVLKIFYQTCRAVQHMH-------RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14055     82 ENGSLQDYLT----RHILSWEDLCKMAGSLARGLAHLHsdrtpcgRPKIPIAHRDLKSSNILVKNDGTCVLADFGLA 154
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 45-201 2.43e-08

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: 56.85  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   45 VLAEGQLVEFLKKMESrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS---- 120
Cdd:cd14182     91 LMKKGELFDYLTEKVT---LSEKETRKIMRALLEVICALHKLN--IVHRDLKPENILLDDDMNIKLTDFGFSCQLDpgek 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 ----------------------HYPDYSwsaqrrALVEEEALGCILYLLCFRQHPF---EDGAKLR-IVNGKYSI--PPH 172
Cdd:cd14182    166 lrevcgtpgylapeiiecsmddNHPGYG------KEVDMWSTGVIMYTLLAGSPPFwhrKQMLMLRmIMSGNYQFgsPEW 239

                          170       180
                   ....*....|....*....|....*....
gi 1034639258  173 DTQYTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14182    240 DDRSDTVKDLISRFLVVQPQKRYTAEEAL 268
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
 39-215 2.54e-08

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: 56.80  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   39 RLRVRRVLAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATt 118
Cdd:cd14117     78 RKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKK--VIHRDIKPENLLMGYKGELKIADFGWSV- 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  119 isHYPdyswSAQRRAL--------------------VEEEALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDT 174
Cdd:cd14117    155 --HAP----SLRRRTMcgtldylppemiegrthdekVDLWCIGVLCYELLVGMPPFESASHTetyrRIVKVDLKFPPFLS 228

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034639258  175 QYTvfHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNP 215
Cdd:cd14117    229 DGS--RDLISKLLRYHPSERLPLKGVMEHPWVKANSRRVLP 267
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 71-200 3.05e-08

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: 56.92  E-value: 3.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG---TIKLCDFGSA------------------------TTISHYP 123
Cdd:cd14092    103 RIMRQLVSAVSFMHSKG--VVHRDLKPENLLFTDEDddaEIKIVDFGFArlkpenqplktpcftlpyaapevlKQALSTQ 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 DYS-----WSaqrralveeeaLGCILYLLCFRQHPFEDGAKL--------RIVNGKYSIppHDTQYTVF----HSLIRAM 186
Cdd:cd14092    181 GYDescdlWS-----------LGVILYTMLSGQVPFQSPSRNesaaeimkRIKSGDFSF--DGEEWKNVsseaKSLIQGL 247

                          170
                   ....*....|....
gi 1034639258  187 LQVNPEERLSIAEV 200
Cdd:cd14092    248 LTVDPSKRLTMSEL 261
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 45-196 3.97e-08

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 56.13  E-value: 3.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   45 VLAEGQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS---- 120
Cdd:cd14181     97 LMRRGELFDYLTE---KVTLSEKETRSIMRSLLEAVSYLHANN--IVHRDLKPENILLDDQLHIKLSDFGFSCHLEpgek 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 -----HYPDYSWSAQRRALVEEE-----------ALGCILYLLCFRQHPFEDGAKL----RIVNGKY--SIPPHDTQYTV 178
Cdd:cd14181    172 lrelcGTPGYLAPEILKCSMDEThpgygkevdlwACGVILFTLLAGSPPFWHRRQMlmlrMIMEGRYqfSSPEWDDRSST 251

                          170
                   ....*....|....*...
gi 1034639258  179 FHSLIRAMLQVNPEERLS 196
Cdd:cd14181    252 VKDLISRLLVVDPEIRLT 269
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
 33-128 4.06e-08

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: 56.16  E-value: 4.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   33 VELGE-LRLRVRRVLA----EGQLVEFLKKMESRGPlsCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT 107
Cdd:cd07848     63 VELKEaFRRRGKLYLVfeyvEKNMLELLEEMPNGVP--PEKVRSYIYQLIKAIHWCHKND--IVHRDIKPENLLISHNDV 138

                           90       100
                   ....*....|....*....|.
gi 1034639258  108 IKLCDFGSATTISHYPDYSWS 128
Cdd:cd07848    139 LKLCDFGFARNLSEGSNANYT 159
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 49-114 4.08e-08

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: 56.28  E-value: 4.08e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKMESRGPLSCDTVL-KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06621     86 GSLDSIYKKVKKKGGRIGEKVLgKIAESVLKGLSYLHSRK--IIHRDIKPSNILLTRKGQVKLCDFG 150
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 56-231 4.46e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 57.33  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   56 KKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------------SATTISHYP 123
Cdd:PTZ00267   158 QRLKEHLPFQEYEVGLLFYQIVLALDEVHSRK--MMHRDLKSANIFLMPTGIIKLGDFGfskqysdsvsldVASSFCGTP 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  124 DY----SWSAQRRA-LVEEEALGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPPHDTQYTVfHSLIRAMLQVNPEER 194
Cdd:PTZ00267   236 YYlapeLWERKRYSkKADMWSLGVILYELLTLHRPFKGPSQREIMQqvlyGKYDPFPCPVSSGM-KALLDPLLSKNPALR 314

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034639258  195 LSIAEVVHQ---------LQEIAAARNVNPKSPITELLEQNGGYGS 231
Cdd:PTZ00267   315 PTTQQLLHTeflkyvanlFQDIVRHSETISPHDREEILRQLQESGE 360
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 40-203 4.99e-08

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: 55.40  E-value: 4.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   40 LRVRRVLAEGQLVEFLKKMESrgplscdtvlkifyqtcrAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT-- 117
Cdd:cd14188     92 LKARKVLTEPEVRYYLRQIVS------------------GLKYLHEQE--ILHRDLKLGNFFINENMELKVGDFGLAArl 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 --------TISHYPDY----SWSAQRRALVEE-EALGCILYLLCFRQHPFEDgAKLR-----IVNGKYSIPphDTQYTVF 179
Cdd:cd14188    152 eplehrrrTICGTPNYlspeVLNKQGHGCESDiWALGCVMYTMLLGRPPFET-TNLKetyrcIREARYSLP--SSLLAPA 228

                          170       180
                   ....*....|....*....|....
gi 1034639258  180 HSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14188    229 KHLIASMLSKNPEDRPSLDEIIRH 252
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 50-200 5.27e-08

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: 55.81  E-value: 5.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   50 QLVEFLKKMESRGPLScdTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------SATTISHY- 122
Cdd:cd08229    113 RMIKHFKKQKRLIPEK--TVWKYFVQLCSALEHMHSRR--VMHRDIKPANVFITATGVVKLGDLGlgrffsSKTTAAHSl 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 --PDYSWSAQRralVEEE---------ALGCILYLLCFRQHPFEdGAKL-------RIVNGKYSIPPHDTQYTVFHSLIR 184
Cdd:cd08229    189 vgTPYYMSPER---IHENgynfksdiwSLGCLLYEMAALQSPFY-GDKMnlyslckKIEQCDYPPLPSDHYSEELRQLVN 264

                          170
                   ....*....|....*.
gi 1034639258  185 AMLQVNPEERLSIAEV 200
Cdd:cd08229    265 MCINPDPEKRPDITYV 280
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
 77-203 6.07e-08

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: 55.34  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   77 CRAVQHMHRQKppIIHRDLKVENLLLSNQG----TIKLCDFGSAT-------TISHYPDYS----WSAQRRAL-VEEEAL 140
Cdd:cd14185    108 CEALVYIHSKH--IVHRDLKPENLLVQHNPdkstTLKLADFGLAKyvtgpifTVCGTPTYVapeiLSEKGYGLeVDMWAA 185

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  141 GCILY-LLC----FRQHPFEDGAKLRIVN-GKYS-IPPH-DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14185    186 GVILYiLLCgfppFRSPERDQEELFQIIQlGHYEfLPPYwDNISEAAKDLISRLLVVDPEKRYTAKQVLQH 256
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
 63-125 6.13e-08

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: 56.16  E-value: 6.13e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd14207    176 PLTMEDLISYSFQVARGMEFLSSRK--CIHRDLAARNILLSENNVVKICDFGLARDIYKNPDY 236
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
 63-114 6.15e-08

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: 55.52  E-value: 6.15e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06611     99 GLTEPQIRYVCRQMLEALNFLHSHK--VIHRDLKAGNILLTLDGDVKLADFG 148
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
 36-199 6.42e-08

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: 54.97  E-value: 6.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   36 GEL--RLRVRRVLAEGQLVEFLKkmesrgplscdtvlkifyQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG--TIKLC 111
Cdd:cd14006     74 GELldRLAERGSLSEEEVRTYMR------------------QLLEGLQYLHNHH--ILHLDLKPENILLADRPspQIKII 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  112 DFGSATTISH---------YPDYswsaQRRALVEEE---------ALGCILYLLCFRQHPF-EDGA---KLRIVNGKYsi 169
Cdd:cd14006    134 DFGLARKLNPgeelkeifgTPEF----VAPEIVNGEpvslatdmwSIGVLTYVLLSGLSPFlGEDDqetLANISACRV-- 207

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034639258  170 pphDTQYTVFHSL-------IRAMLQVNPEERLSIAE 199
Cdd:cd14006    208 ---DFSEEYFSSVsqeakdfIRKLLVKEPRKRPTAQE 241
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 49-195 6.61e-08

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: 55.52  E-value: 6.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKkmeSRGPLSCDTVLkiFYQT---CrAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT-------T 118
Cdd:cd05612     86 GELFSYLR---NSGRFSNSTGL--FYASeivC-ALEYLHSKE--IVYRDLKPENILLDKEGHIKLTDFGFAKklrdrtwT 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  119 ISHYPDY------SWSAQRRAlVEEEALGCILYLLCFRQHPFED----GAKLRIVNGKYSIPPHDTQYTvfHSLIRAMLQ 188
Cdd:cd05612    158 LCGTPEYlapeviQSKGHNKA-VDWWALGILIYEMLVGYPPFFDdnpfGIYEKILAGKLEFPRHLDLYA--KDLIKKLLV 234


                   ....*..
gi 1034639258  189 VNPEERL 195
Cdd:cd05612    235 VDRTRRL 241
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
 49-116 7.11e-08

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: 55.36  E-value: 7.11e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   49 GQLVEFLkkmeSRGPLSCDTVLKIFYQTCRAVQHMH------RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14056     78 GSLYDYL----QRNTLDTEEALRLAYSAASGLAHLHteivgtQGKPAIAHRDLKSKNILVKRDGTCCIADLGLA 147
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
 62-199 7.12e-08

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: 55.00  E-value: 7.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH------------YpdysWSA 129
Cdd:cd06613     92 GPLSELQIAYVCRETLKGLAYLHSTG--KIHRDIKGANILLTEDGDVKLADFGVSAQLTAtiakrksfigtpY----WMA 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 QRRALVEEE----------ALGCILYLLCFRQHPFEDGAKLR---IVNGKYSIPPH----DTQYTVFHSLIRAMLQVNPE 192
Cdd:cd06613    166 PEVAAVERKggydgkcdiwALGITAIELAELQPPMFDLHPMRalfLIPKSNFDPPKlkdkEKWSPDFHDFIKKCLTKNPK 245


                   ....*..
gi 1034639258  193 ERLSIAE 199
Cdd:cd06613    246 KRPTATK 252
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
 49-117 7.25e-08

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: 54.92  E-value: 7.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   49 GQLVEFLKKMesrGPLScdtvLKIFYQTCR----AVQHMHRQKPPIIHRDLKVENLLL-SNQGTIKLCDFGSAT 117
Cdd:cd13983     87 GTLKQYLKRF---KRLK----LKVIKSWCRqileGLNYLHTRDPPIIHRDLKCDNIFInGNTGEVKIGDLGLAT 153
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
 62-114 7.46e-08

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: 55.52  E-value: 7.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKPpIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06620     99 GPFPEEVLGKIAVAVLEGLTYLYNVHR-IIHRDIKPSNILVNSKGQIKLCDFG 150
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
 49-114 7.46e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 55.49  E-value: 7.46e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   49 GQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05609     85 GDCATLLKNI---GPLPVDMARMYFAETVLALEYLHSYG--IVHRDLKPDNLLITSMGHIKLTDFG 145
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 53-202 9.11e-08

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 54.78  E-value: 9.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL--SNQGTIKLCDFG-SATTISHYPDYSwSA 129
Cdd:cd14662     82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQ--ICHRDLKLENTLLdgSPAPRLKICDFGySKSSVLHSQPKS-TV 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 QRRALVEEEAL---------------GCILYLLCFRQHPFEDGAK--------LRIVNGKYSIPPHDTQYTVFHSLIRAM 186
Cdd:cd14662    159 GTPAYIAPEVLsrkeydgkvadvwscGVTLYVMLVGAYPFEDPDDpknfrktiQRIMSVQYKIPDYVRVSQDCRHLLSRI 238

                          170
                   ....*....|....*.
gi 1034639258  187 LQVNPEERLSIAEVVH 202
Cdd:cd14662    239 FVANPAKRITIPEIKN 254
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
 40-201 9.97e-08

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 54.95  E-value: 9.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   40 LRVRRVLAEGQLV----------EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG--- 106
Cdd:cd14091     57 ITLRDVYDDGNSVylvtellrggELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQG--VVHRDLKPSNILYADESgdp 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  107 -TIKLCDFGSATTISH------YPDYS--------------------WSaqrralveeeaLGCILYLLCFRQHPF----E 155
Cdd:cd14091    135 eSLRICDFGFAKQLRAengllmTPCYTanfvapevlkkqgydaacdiWS-----------LGVLLYTMLAGYTPFasgpN 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  156 DGAK---LRIVNGKYSI--PPHDTQYTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14091    204 DTPEvilARIGSGKIDLsgGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVL 254
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 69-199 1.02e-07

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: 54.66  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   69 VLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS---NQGTIKLCDFGSATTISH---------YPDYS---------- 126
Cdd:cd14106    110 VRRLMRQILEGVQYLHERN--IVHLDLKPQNILLTsefPLGDIKLCDFGISRVIGEgeeireilgTPDYVapeilsyepi 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 ------WSaqrralveeeaLGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHdtqytVFHSL-------IRAMLQV 189
Cdd:cd14106    188 slatdmWS-----------IGVLTYVLLTGHSPFGGDDKqetfLNISQCNLDFPEE-----LFKDVsplaidfIKRLLVK 251

                          170
                   ....*....|
gi 1034639258  190 NPEERLSIAE 199
Cdd:cd14106    252 DPEKRLTAKE 261
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 73-199 1.05e-07

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: 55.37  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI--SHYPDYSWSAQRRALVEEE---------- 138
Cdd:cd05573    105 FYiaELVLALDSLHKLG--FIHRDIKPDNILLDADGHIKLADFGLCTKMnkSGDRESYLNDSVNTLFQDNvlarrrphkq 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  139 --------------------------------ALGCILYLLCFRQHPFED----GAKLRIVNGKYS--IPPHDTQYTVFH 180
Cdd:cd05573    183 rrvraysavgtpdyiapevlrgtgygpecdwwSLGVILYEMLYGFPPFYSdslvETYSKIMNWKESlvFPDDPDVSPEAI 262

                          170
                   ....*....|....*....
gi 1034639258  181 SLIRAMLqVNPEERLSIAE 199
Cdd:cd05573    263 DLIRRLL-CDPEDRLGSAE 280
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1195-1239 1.10e-07

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 49.47  E-value: 1.10e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258 1195 PEQVKKHYRRAVLAVHPDKAAGQPYeqhAKMIFMELNDAWSEFEN 1239
Cdd:cd06257     14 DEEIKKAYRKLALKYHPDKNPDDPE---AEEKFKEINEAYEVLSD 55
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 62-225 1.10e-07

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: 54.79  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdySWSAQRRALVEEE--- 138
Cdd:cd06917     96 GPIAERYIAVIMREVLVALKFIH--KDGIIHRDIKAANILVTNTGNVKLCDFGVAASLN-----QNSSKRSTFVGTPywm 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  139 ------------------ALGCILYLLCFRQHPFEDGAKLRIVN--GKYSIP--PHDTQYTVFHSLIRAMLQVNPEERLS 196
Cdd:cd06917    169 apevitegkyydtkadiwSLGITTYEMATGNPPYSDVDALRAVMliPKSKPPrlEGNGYSPLLKEFVAACLDEEPKDRLS 248

                          170       180
                   ....*....|....*....|....*....
gi 1034639258  197 iAEVVHQLQEIAAARNVnPKSPITELLEQ 225
Cdd:cd06917    249 -ADELLKSKWIKQHSKT-PTSVLKELISR 275
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 51-121 1.13e-07

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: 55.40  E-value: 1.13e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLL--SNQGTIKLCDFGSATTISH 121
Cdd:cd14226    101 LYDLLRNTNFRG-VSLNLTRKFAQQLCTALLFLSTPELSIIHCDLKPENILLcnPKRSAIKIIDFGSSCQLGQ 172
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
 72-203 1.26e-07

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 54.65  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGSATTIS------HYPDYSWSAQRRALVEEE--- 138
Cdd:cd14175    100 VLHTICKTVEYLHSQG--VVHRDLKPSNILYvdesGNPESLRICDFGFAKQLRaengllMTPCYTANFVAPEVLKRQgyd 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  139 ------ALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14175    178 egcdiwSLGILLYTMLAGYTPFANGPSdtpeeilTRIGSGKFTLSGGnwNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQH 257
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
 72-121 1.31e-07

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: 54.19  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH 121
Cdd:cd06612    104 ILYQTLKGLEYLHSNK--KIHRDIKAGNILLNEEGQAKLADFGVSGQLTD 151
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
 75-201 1.41e-07

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: 54.86  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLS---NQGTIKLCDFGSATTIshyPDYSWSAQRRA---------LVEEEALGC 142
Cdd:cd14094    117 QILEALRYCHDNN--IIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQL---GESGLVAGGRVgtphfmapeVVKREPYGK 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  143 ---------ILYLLCFRQHPFEdGAKLR----IVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14094    192 pvdvwgcgvILFILLSGCLPFY-GTKERlfegIIKGKYKMNPRqwSHISESAKDLVRRMLMLDPAERITVYEAL 264
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
 79-199 1.51e-07

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: 54.70  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYSWSAQRRAL-----VEEEALGCI 143
Cdd:cd05592    108 GLQFLHSRG--IIYRDLKLDNVLLDREGHIKIADFGmckeniygenKASTFCGTPDYIAPEILKGQkynqsVDWWSFGVL 185

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  144 LYLLCFRQHPF----EDGAKLRIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEERLSIAE 199
Cdd:cd05592    186 LYEMLIGQSPFhgedEDELFWSICNDTPHYPRWLTKEA--ASCLSLLLERNPEKRLGVPE 243
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
 59-144 1.56e-07

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: 54.26  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   59 ESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQ---RR--- 132
Cdd:cd07832     92 DEERPLTEAQVKRYMRMLLKGVAYMHANR--IMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYSHQvatRWyra 169

                           90       100
                   ....*....|....*....|...
gi 1034639258  133 -----------ALVEEEALGCIL 144
Cdd:cd07832    170 pellygsrkydEGVDLWAVGCIF 192
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
 49-203 1.56e-07

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: 54.25  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG---------TIKLCDFG----- 114
Cdd:cd14202     86 GDLADYLHTM---RTLSEDTIRLFLQQIAGAMKMLHSKG--IIHRDLKPQNILLSYSGgrksnpnniRIKIADFGfaryl 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 ----SATTISHYPDYS-----WSAQRRALVEEEALGCILYLLCFRQHPFEDGA--KLRIVNGK-YSIPPHDTQYTVFH-- 180
Cdd:cd14202    161 qnnmMAATLCGSPMYMapeviMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSpqDLRLFYEKnKSLSPNIPRETSSHlr 240

                          170       180
                   ....*....|....*....|...
gi 1034639258  181 SLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14202    241 QLLLGLLQRNQKDRMDFDEFFHH 263
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
 51-120 1.61e-07

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: 53.99  E-value: 1.61e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKmesrgPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06607     90 IVEVHKK-----PLQEVEIAAICHGALQGLAYLHSHNR--IHRDVKAGNILLTEPGTVKLADFGSASLVC 152
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 79-203 1.62e-07

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 54.23  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGSA--TTISH---YPDYS-WSAQRRALVEEE--------ALG 141
Cdd:cd14172    115 AIQYLHSMN--IAHRDVKPENLLYTSKekdAVLKLTDFGFAkeTTVQNalqTPCYTpYYVAPEVLGPEKydkscdmwSLG 192

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  142 CILYLLCFRQHPF--------EDGAKLRIVNGKYSIP-PHDTQYTV-FHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14172    193 VIMYILLCGFPPFysntgqaiSPGMKRRIRMGQYGFPnPEWAEVSEeAKQLIRHLLKTDPTERMTITQFMNH 264
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 78-201 1.67e-07

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: 54.22  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   78 RAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSA-----------TTISHYPDYSWSAQRRA-----------LV 135
Cdd:cd14010    105 RGLHYIH--SKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeilkelfGQFSDEGNVNKVSKKQAkrgtpyymapeLF 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  136 EEE---------ALGCILYLLCFRQHPF--EDGAKL--RIVNG--KYSIPPHDTQYTV-FHSLIRAMLQVNPEERLSIAE 199
Cdd:cd14010    183 QGGvhsfasdlwALGCVLYEMFTGKPPFvaESFTELveKILNEdpPPPPPKVSSKPSPdFKSLLKGLLEKDPAKRLSWDE 262


                   ..
gi 1034639258  200 VV 201
Cdd:cd14010    263 LV 264
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 48-120 1.77e-07

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: 53.77  E-value: 1.77e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   48 EGQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06627     83 NGSLASIIKKF---GKFPESLVAVYIYQVLEGLAYLHEQG--VIHRDIKGANILTTKDGLVKLADFGVATKLN 150
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
 72-196 1.80e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 55.26  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-----SAT-------TISHYPDYS----WsaqRRALV 135
Cdd:PTZ00283   148 LFIQVLLAVHHVHSKH--MIHRDIKSANILLCSNGLVKLGDFGfskmyAATvsddvgrTFCGTPYYVapeiW---RRKPY 222

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  136 EEEA----LGCILYLLCFRQHPFeDGAKLRIV-----NGKYSiPPHDTQYTVFHSLIRAMLQVNPEERLS 196
Cdd:PTZ00283   223 SKKAdmfsLGVLLYELLTLKRPF-DGENMEEVmhktlAGRYD-PLPPSISPEMQEIVTALLSSDPKRRPS 290
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
 36-125 1.90e-07

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: 54.35  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   36 GELR--LRVRRvlAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDF 113
Cdd:cd05053    102 GNLRefLRARR--PPGEEASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKK--CIHRDLAARNVLVTEDNVMKIADF 177

                           90
                   ....*....|..
gi 1034639258  114 GSATTIsHYPDY 125
Cdd:cd05053    178 GLARDI-HHIDY 188
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
 48-156 2.08e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 53.71  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   48 EGQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFG------------ 114
Cdd:PHA03390    93 DGDLFDLLKK---EGKLSEAEVKKIIRQLVEALNDLHKHN--IIHNDIKLENVLYDrAKDRIYLCDYGlckiigtpscyd 167

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034639258  115 ------SATTISHYP-DYS---WsaqrralveeeALGCILYLLCFRQHPFED 156
Cdd:PHA03390   168 gtldyfSPEKIKGHNyDVSfdwW-----------AVGVLTYELLTGKHPFKE 208
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
 72-195 2.13e-07

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: 53.87  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtisHYPDYSWSAQRRA--------LVEEE--- 138
Cdd:cd05630    105 VFYaaEICCGLEDLHRER--IVYRDLKPENILLDDHGHIRISDLGLAV---HVPEGQTIKGRVGtvgymapeVVKNEryt 179

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  139 ------ALGCILYLLCFRQHPFEDGAK----------LRIVNGKYS--IPPhDTQytvfhSLIRAMLQVNPEERL 195
Cdd:cd05630    180 fspdwwALGCLLYEMIAGQSPFQQRKKkikreeverlVKEVPEEYSekFSP-QAR-----SLCSMLLCKDPAERL 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
 75-157 2.15e-07

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: 54.11  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQ-----RRAL------------VEE 137
Cdd:cd07841    110 MTLRGLEYLHSNW--ILHRDLKPNNLLIASDGVLKLADFGLARSFG-SPNRKMTHQvvtrwYRAPellfgarhygvgVDM 186

                           90       100
                   ....*....|....*....|
gi 1034639258  138 EALGCILYLLCFRQhPFEDG 157
Cdd:cd07841    187 WSVGCIFAELLLRV-PFLPG 205
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 71-116 2.28e-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: 53.92  E-value: 2.28e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639258   71 KIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07844    101 RLFlFQLLRGLAYCHQRR--VLHRDLKPQNLLISERGELKLADFGLA 145
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
 74-119 2.32e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 54.66  E-value: 2.32e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639258   74 YQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTI 119
Cdd:PTZ00036   177 YQLCRALAYIHSKF--ICHRDLKPQNLLIDpNTHTLKLCDFGSAKNL 221
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
 47-120 2.38e-07

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: 53.98  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   47 AEGQLVEFLKkmesRGPLSCDTVLKIFYQTCRAVQHMH-------RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTI 119
Cdd:cd13998     76 PNGSL*DYLS----LHTIDWVSLCRLALSVARGLAHLHseipgctQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRL 151


                   .
gi 1034639258  120 S 120
Cdd:cd13998    152 S 152
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 67-202 2.51e-07

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: 53.53  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   67 DTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT----ISHYP---DYSWSA---------- 129
Cdd:cd14046    104 DRLWRLFRQILEGLAYIHSQG--IIHRDLKPVNIFLDSNGNVKIGDFGLATSnklnVELATqdiNKSTSAalgssgdltg 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 -------------QRRALVEEE-----ALGCILYLLCfrqHPFEDGAK----LRIV-NGKYSIPP--HDTQYTVFHSLIR 184
Cdd:cd14046    182 nvgtalyvapevqSGTKSTYNEkvdmySLGIIFFEMC---YPFSTGMErvqiLTALrSVSIEFPPdfDDNKHSKQAKLIR 258

                          170
                   ....*....|....*...
gi 1034639258  185 AMLQVNPEERLSIAEVVH 202
Cdd:cd14046    259 WLLNHDPAKRPSAQELLK 276
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
 72-195 2.58e-07

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: 53.68  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA------TTISHYPDYSWSAQRRALVEEE----- 138
Cdd:cd05577     98 IFYaaEIICGLEHLHNRF--IVYRDLKPENILLDDHGHVRISDLGLAvefkggKKIKGRVGTHGYMAPEVLQKEVaydfs 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  139 ----ALGCILYLLCFRQHPFEDGA--------KLRIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEERL 195
Cdd:cd05577    176 vdwfALGCMLYEMIAGRSPFRQRKekvdkeelKRRTLEMAVEYPDSFSPEA--RSLCEGLLQKDPERRL 242
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 79-195 3.08e-07

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 54.05  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT-------TISHYPDY-----SWSAQRRALVEEEALGCILYL 146
Cdd:PTZ00263   130 AFEYLHSKD--IIYRDLKPENLLLDNKGHVKVTDFGFAKkvpdrtfTLCGTPEYlapevIQSKGHGKAVDWWTMGVLLYE 207

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  147 LCFRQHPFEDGAKLR----IVNGKYSIPP-HDTQYtvfHSLIRAMLQVNPEERL 195
Cdd:PTZ00263   208 FIAGYPPFFDDTPFRiyekILAGRLKFPNwFDGRA---RDLVKGLLQTDHTKRL 258
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
 62-145 3.91e-07

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: 53.09  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQRRAL------ 134
Cdd:cd07871     97 GNLMSMHNVKIFmFQLLRGLSYCHKRK--ILHRDLKPQNLLINEKGELKLADFGLARAKS-VPTKTYSNEVVTLwyrppd 173

                           90       100
                   ....*....|....*....|..
gi 1034639258  135 -----------VEEEALGCILY 145
Cdd:cd07871    174 vllgsteystpIDMWGVGCILY 195
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
 21-215 4.63e-07

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: 53.10  E-value: 4.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   21 SGRDQSDFVGQTVELGELR--LRVRRVLAEGQLVEFLKKMESRGPLsCDTVLK-----------IFYQTCRAVQHMHRQK 87
Cdd:cd14177     40 SKRDPSEEIEILMRYGQHPniITLKDVYDDGRYVYLVTELMKGGEL-LDRILRqkffsereasaVLYTITKTVDYLHCQG 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   88 ppIIHRDLKVENLLL----SNQGTIKLCDFGSATTISH---------------YPDYSWSAQRRALVEEEALGCILYLLC 148
Cdd:cd14177    119 --VVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGengllltpcytanfvAPEVLMRQGYDAACDIWSLGVLLYTML 196

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  149 FRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVVHqlQEIAAARNVNP 215
Cdd:cd14177    197 AGYTPFANGPNdtpeeilLRIGSGKFSLSGGnwDTVSDAAKDLLSHMLHVDPHQRYTAEQVLK--HSWIACRDQLP 270
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 75-201 4.66e-07

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: 52.65  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA--------TTISHYPDYSWSAQRRALVEEE-----ALG 141
Cdd:cd14116    113 ELANALSYCHSKR--VIHRDIKPENLLLGSAGELKIADFGWSvhapssrrTTLCGTLDYLPPEMIEGRMHDEkvdlwSLG 190

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  142 CILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14116    191 VLCYEFLVGKPPFEANTYqetyKRISRVEFTFPDFVTEGA--RDLISRLLKHNPSQRPMLREVL 252
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 59-115 4.94e-07

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: 52.77  E-value: 4.94e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   59 ESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGS 115
Cdd:cd13979     95 EGSEPLPLAHRILISLDIARALRFCHSHG--IVHLDVKPANILISEQGVCKLCDFGC 149
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
 49-116 5.31e-07

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: 52.37  E-value: 5.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG---------TIKLCDFGSA 116
Cdd:cd14120     77 GDLADYLQAK---GTLSEDTIRVFLQQIAAAMKALHSKG--IVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFA 148
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 61-200 5.50e-07

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 52.26  E-value: 5.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   61 RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTISH--YPDY---------SWS 128
Cdd:cd14102     99 KGALDEDTARGFFRQVLEAVRHCYSCG--VVHRDIKDENLLVDlRTGELKLIDFGSGALLKDtvYTDFdgtrvysppEWI 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  129 AQRR-----ALVeeEALGCILYLLCFRQHPFEDGAKlrIVNGKY----SIPPHDTQytvfhsLIRAMLQVNPEERLSIAE 199
Cdd:cd14102    177 RYHRyhgrsATV--WSLGVLLYDMVCGDIPFEQDEE--ILRGRLyfrrRVSPECQQ------LIKWCLSLRPSDRPTLEQ 246


                   .
gi 1034639258  200 V 200
Cdd:cd14102    247 I 247
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
 60-199 5.85e-07

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: 53.21  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   60 SRGPLSCDTVlKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT-------------ISHY--- 122
Cdd:cd07853     96 SPQPLSSDHV-KVFlYQILRGLKYLHSAG--ILHRDIKPGNLLVNSNCVLKICDFGLARVeepdeskhmtqevVTQYyra 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 PDYSWSAQR-RALVEEEALGCILYLLCFRQHPFE---------------------------DGAKLRIVNGKYSIPPHDT 174
Cdd:cd07853    173 PEILMGSRHyTSAVDIWSVGCIFAELLGRRILFQaqspiqqldlitdllgtpsleamrsacEGARAHILRGPHKPPSLPV 252

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034639258  175 QYTV--------FHSLIRaMLQVNPEERLSIAE 199
Cdd:cd07853    253 LYTLssqatheaVHLLCR-MLVFDPDKRISAAD 284
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 48-120 6.10e-07

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: 52.30  E-value: 6.10e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   48 EGQLVEFLKKmesrGPLSCDTVLKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06626     83 EGTLEELLRH----GRILDEAVIRVYtLQLLEGLAYLHENG--IVHRDIKPANIFLDSNGLIKLGDFGSAVKLK 150
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 73-195 6.44e-07

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: 52.41  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSAT-------TISHYPDY-----SWSAQRRALVEEE 138
Cdd:cd14209    105 FYaaQIVLAFEYLH--SLDLIYRDLKPENLLIDQQGYIKVTDFGFAKrvkgrtwTLCGTPEYlapeiILSKGYNKAVDWW 182

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  139 ALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERL 195
Cdd:cd14209    183 ALGVLIYEMAAGYPPFFADQPIqiyeKIVSGKVRFPSHFS--SDLKDLLRNLLQVDLTKRF 241
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 75-175 7.19e-07

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: 52.15  E-value: 7.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYS----WSAQ---RRALVEE 137
Cdd:cd06628    114 QILKGLNYLHNRG--IIHRDIKGANILVDNKGGIKISDFGiskkleanslSTKNNGARPSLQgsvfWMAPevvKQTSYTR 191

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639258  138 EA----LGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPPHDTQ 175
Cdd:cd06628    192 KAdiwsLGCLVVEMLTGTHPFPDCTQMQAIfkigeNASPTIPSNISS 238
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
 27-116 7.48e-07

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: 52.52  E-value: 7.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   27 DFVGQTVELGELRLrVRRVLAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQG 106
Cdd:cd14159     56 DLAGYSAQQGNYCL-IYVYLPNGSLEDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAAL 134

                           90
                   ....*....|
gi 1034639258  107 TIKLCDFGSA 116
Cdd:cd14159    135 NPKLGDFGLA 144
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
 65-130 7.89e-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: 52.27  E-value: 7.89e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   65 SCDTVLKIFyQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQ 130
Cdd:cd07870     97 PYNVRLFMF-QLLRGLAYIHGQH--ILHRDLKPQNLLISYLGELKLADFGLARAKS-IPSQTYSSE 158
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 71-114 8.34e-07

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: 52.37  E-value: 8.34e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034639258   71 KIFYQTCRAVQHMhRQKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06616    113 KIAVATVKALNYL-KEELKIIHRDVKPSNILLDRNGNIKLCDFG 155
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
 79-195 8.43e-07

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: 52.32  E-value: 8.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDY------SWSAQRRAlVEEEALGC 142
Cdd:cd05575    108 ALGYLHSLN--IIYRDLKPENILLDSQGHVVLTDFGlckegiepsdTTSTFCGTPEYlapevlRKQPYDRT-VDWWCLGA 184

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  143 ILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEERL 195
Cdd:cd05575    185 VLYEMLYGLPPFysRDTAEMydNILHKPLRLRTNVSPSA--RDLLEGLLQKDRTKRL 239
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
 75-114 8.95e-07

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: 51.74  E-value: 8.95e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd14070    111 QLVSAVEHLHRAG--VVHRDLKIENLLLDENDNIKLIDFG 148
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
 75-207 9.03e-07

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: 51.63  E-value: 9.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKP-PIIHRDLKVENLLLSN--------QGTIKLCDFGSA------TTISHYPDYSWSAQR--RALVEE 137
Cdd:cd14061    100 QIARGMNYLHNEAPvPIIHRDLKSSNILILEaienedleNKTLKITDFGLArewhktTRMSAAGTYAWMAPEviKSSTFS 179

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  138 EA-----LGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd14061    180 KAsdvwsYGVLLWELLTGEVPYKGIDGLAVAYGvavnKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
 67-114 9.34e-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: 52.57  E-value: 9.34e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034639258   67 DTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05610    104 EMAVKYISEVALALDYLHRHG--IIHRDLKPDNMLISNEGHIKLTDFG 149
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
 72-116 9.96e-07

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: 52.32  E-value: 9.96e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07866    120 YMLQLLEGINYLHENH--ILHRDIKAANILIDNQGILKIADFGLA 162
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
 28-196 1.05e-06

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: 51.77  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   28 FVGQTVELGELRLRVRRVLAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT 107
Cdd:cd14087     58 NIIQLIEVFETKERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLG--ITHRDLKPENLLYYHPGP 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  108 ---IKLCDFGSA-----------TTISHYPDY---------SWSAQrralVEEEALGCILYLLCFRQHPFEDGAKLR--- 161
Cdd:cd14087    136 dskIMITDFGLAstrkkgpnclmKTTCGTPEYiapeillrkPYTQS----VDMWAVGVIAYILLSGTMPFDDDNRTRlyr 211

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034639258  162 -IVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLS 196
Cdd:cd14087    212 qILRAKYSYSGEpwPSVSNLAKDFIDRLLTVNPGERLS 249
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 73-195 1.06e-06

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 52.11  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYSWSAQRRAL-----V 135
Cdd:cd05591    100 FYaaEVTLALMFLHRHG--VIYRDLKLDNILLDAEGHCKLADFGmckegilngkTTTTFCGTPDYIAPEILQELeygpsV 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  136 EEEALGCILYLLCFRQHPFEDGAKLRIVNgkySIPPHDTQYTVFHS-----LIRAMLQVNPEERL 195
Cdd:cd05591    178 DWWALGVLMYEMMAGQPPFEADNEDDLFE---SILHDDVLYPVWLSkeavsILKAFMTKNPAKRL 239
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
 75-225 1.08e-06

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: 51.96  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTI-------SHYPDYSWSAQRRALVEEE-------- 138
Cdd:cd06644    118 QMLEALQYLHSMK--IIHRDLKAGNVLLTLDGDIKLADFGvSAKNVktlqrrdSFIGTPYWMAPEVVMCETMkdtpydyk 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  139 ----ALGCILYLLCFRQHPFEDGAKLRI-VNGKYSIPP---HDTQYTV-FHSLIRAMLQVNPEERLSIAevvhQLQEIAA 209
Cdd:cd06644    196 adiwSLGITLIEMAQIEPPHHELNPMRVlLKIAKSEPPtlsQPSKWSMeFRDFLKTALDKHPETRPSAA----QLLEHPF 271

                          170
                   ....*....|....*.
gi 1034639258  210 ARNVNPKSPITELLEQ 225
Cdd:cd06644    272 VSSVTSNRPLRELVAE 287
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
 79-214 1.17e-06

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 52.19  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG--------SATTISHYPDYSWSAQrRALVEEE---------ALG 141
Cdd:cd05586    108 ALEHLHKND--IVYRDLKPENILLDANGHIALCDFGlskadltdNKTTNTFCGTTEYLAP-EVLLDEKgytkmvdfwSLG 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  142 CILYLLCFRQHPF--EDGAKL--RIVNGKYSIpPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVN 214
Cdd:cd05586    185 VLVFEMCCGWSPFyaEDTQQMyrNIAFGKVRF-PKDVLSDEGRSFVKGLLNRNPKHRLGAHDDAVELKEHPFFADID 260
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
 53-201 1.29e-06

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: 51.33  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY---------- 122
Cdd:cd14076     92 ELFDYILARRRLKDSVACRLFAQLISGVAYLH--KKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFngdlmstscg 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 -PDY-------SWSAQRRALVEEEALGCILYLLCFRQHPFEDG---------AKL--RIVNGKYSIPPHDTQYTvfHSLI 183
Cdd:cd14076    170 sPCYaapelvvSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDphnpngdnvPRLyrYICNTPLIFPEYVTPKA--RDLL 247

                          170
                   ....*....|....*...
gi 1034639258  184 RAMLQVNPEERLSIAEVV 201
Cdd:cd14076    248 RRILVPNPRKRIRLSAIM 265
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
 55-116 1.37e-06

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: 51.33  E-value: 1.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   55 LKK-MES---RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07836     84 LKKyMDThgvRGALDPNTVKSFTYQLLKGIAFCHENR--VLHRDLKPQNLLINKRGELKLADFGLA 147
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
 51-121 1.41e-06

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 51.81  E-value: 1.41e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   51 LVEFLKKMESRG-PLSCdtVLKIFYQTCRAVQHMHRqKPPIIHRDLKVENLLLS-NQGTIKLCDFGSATTISH 121
Cdd:cd14136    104 LLKLIKRYNYRGiPLPL--VKKIARQVLQGLDYLHT-KCGIIHTDIKPENVLLCiSKIEVKIADLGNACWTDK 173
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
 53-201 1.43e-06

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: 51.94  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGSATTIS------HY 122
Cdd:cd14176     99 ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRaengllMT 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 PDYSWSAQRRALVEEE---------ALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIR 184
Cdd:cd14176    177 PCYTANFVAPEVLERQgydaacdiwSLGVLLYTMLTGYTPFANGPDdtpeeilARIGSGKFSLSGGywNSVSDTAKDLVS 256

                          170
                   ....*....|....*..
gi 1034639258  185 AMLQVNPEERLSIAEVV 201
Cdd:cd14176    257 KMLHVDPHQRLTAALVL 273
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
 75-207 1.46e-06

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: 51.19  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQK-PPIIHRDLKVENLLLSNQ--------GTIKLCDFGSA------TTISHYPDYSWSAQ---RRALVE 136
Cdd:cd14146    110 QIARGMLYLHEEAvVPILHRDLKSSNILLLEKiehddicnKTLKITDFGLArewhrtTKMSAAGTYAWMAPeviKSSLFS 189

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  137 EE----ALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd14146    190 KGsdiwSYGVLLWELLTGEVPYRGIDGLAVAYGvavnKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
 51-114 1.46e-06

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: 51.27  E-value: 1.46e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258   51 LVEFLKKMESRGPLSCDTVL-KIFYQTCRAVQHMHrQKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06617     86 LDKFYKKVYDKGLTIPEDILgKIAVSIVKALEYLH-SKLSVIHRDVKPSNVLINRNGQVKLCDFG 149
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
 70-116 1.54e-06

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: 51.54  E-value: 1.54e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034639258   70 LKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07873    102 VKLFlFQLLRGLAYCHRRK--VLHRDLKPQNLLINERGELKLADFGLA 147
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
 30-116 1.59e-06

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: 50.91  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   30 GQTVELGELRLrVRRVLAEGQLVEFLKkMESrGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIK 109
Cdd:cd13978     59 GVCVERRSLGL-VMEYMENGSLKSLLE-REI-QDVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFHVK 135


                   ....*..
gi 1034639258  110 LCDFGSA 116
Cdd:cd13978    136 ISDFGLS 142
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 79-195 1.61e-06

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 51.24  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPD--YSW---------------SAQRRALVEEEAL 140
Cdd:cd05583    111 ALEHLHKLG--IIYRDIKLENILLDSEGHVVLTDFGlSKEFLPGENDraYSFcgtieymapevvrggSDGHDKAVDWWSL 188

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258  141 GCILYLLCFRQHPFE-DGAK-------LRIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERL 195
Cdd:cd05583    189 GVLTYELLTGASPFTvDGERnsqseisKRILKSHPPIPKTFS--AEAKDFILKLLEKDPKKRL 249
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
 75-207 1.62e-06

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: 51.14  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKP-PIIHRDLKVENLL---------LSNQgTIKLCDFGSA------TTISHYPDYSWSAQ---RRALV 135
Cdd:cd14148    100 QIARGMNYLHNEAIvPIIHRDLKSSNILilepienddLSGK-TLKITDFGLArewhktTKMSAAGTYAWMAPeviRLSLF 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  136 EEE----ALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd14148    179 SKSsdvwSFGVLLWELLTGEVPYREIDALAVAYGvamnKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 91-196 1.73e-06

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 51.54  E-value: 1.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   91 IHRDLKVENLLLSNQGTIKLCDFGSA--------------------------TTISHYP--------DYsWSaqrralve 136
Cdd:cd05601    124 VHRDIKPENILIDRTGHIKLADFGSAaklssdktvtskmpvgtpdyiapevlTSMNGGSkgtygvecDW-WS-------- 194

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  137 eeaLGCILYLLCFRQHPFEDGAKL----RIVNGK--YSIPPHDTQYTVFHSLIRAMLQvNPEERLS 196
Cdd:cd05601    195 ---LGIVAYEMLYGKTPFTEDTVIktysNIMNFKkfLKFPEDPKVSESAVDLIKGLLT-DAKERLG 256
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
 63-125 1.81e-06

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: 51.34  E-value: 1.81e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05054    134 PLTLEDLICYSFQVARGMEFLASRK--CIHRDLAARNILLSENNVVKICDFGLARDIYKDPDY 194
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1195-1240 1.85e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 46.07  E-value: 1.85e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1034639258  1195 PEQVKKHYRRAVLAVHPDKAAGQPYEqhAKMIFMELNDAWSEFENQ 1240
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
 78-203 1.92e-06

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: 51.17  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   78 RAVQHMHRQKppIIHRDLKVENLLLSNQG----TIKLCDFGSATTIS------HYPDYSWSAQRRALVEEE--------- 138
Cdd:cd14178    108 KTVEYLHSQG--VVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRaengllMTPCYTANFVAPEVLKRQgydaacdiw 185

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  139 ALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14178    186 SLGILLYTMLAGFTPFANGPDdtpeeilARIGSGKYALSGGnwDSISDAAKDIVSKMLHVDPHQRLTAPQVLRH 259
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
 61-125 2.01e-06

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: 51.52  E-value: 2.01e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258   61 RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05103    173 KDFLTLEDLICYSFQVAKGMEFLASRK--CIHRDLAARNILLSENNVVKICDFGLARDIYKDPDY 235
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
 63-116 2.08e-06

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: 51.15  E-value: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07849    102 HLSNDHIQYFLYQILRGLKYIHSAN--VLHRDLKPSNLLLNTNCDLKICDFGLA 153
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
 60-199 2.27e-06

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: 51.21  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   60 SRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD------YSWSAQR-- 131
Cdd:cd07855    102 SDQPLTLEHIRYFLYQLLRGLKYIHSAN--VIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEehkyfmTEYVATRwy 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  132 RA----LVEEE--------ALGCILYLLCFRQHPFEdGA----KLRIVNGKYSIPPHD---------------------- 173
Cdd:cd07855    180 RApelmLSLPEytqaidmwSVGCIFAEMLGRRQLFP-GKnyvhQLQLILTVLGTPSQAvinaigadrvrryiqnlpnkqp 258

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034639258  174 ----------TQYTVfhSLIRAMLQVNPEERLSIAE 199
Cdd:cd07855    259 vpwetlypkaDQQAL--DLLSQMLRFDPSERITVAE 292
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
 37-207 2.45e-06

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: 50.57  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   37 ELRLRVRRVLAEGQLVEFLK-KMESRGPLSCDTVLKIFYQTCRAVQHMHRQ-KPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd14664     63 TTNLLVYEYMPNGSLGELLHsRPESQPPLDWETRQRIALGSARGLAYLHHDcSPLIIHRDVKSNNILLDEEFEAHVADFG 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 SATTI----SHY------------PDYSWSAQRRALVEEEALGCILYLLCFRQHPF-------------------EDGAK 159
Cdd:cd14664    143 LAKLMddkdSHVmssvagsygyiaPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFdeaflddgvdivdwvrgllEEKKV 222

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258  160 LRIVNGKYSIPPHDTQytVFHSLIRAML--QVNPEERLSIAEVVHQLQEI 207
Cdd:cd14664    223 EALVDPDLQGVYKLEE--VEQVFQVALLctQSSPMERPTMREVVRMLEGD 270
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 79-203 2.77e-06

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 50.80  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGSAT-TISH----YPDYS-WSAQRRALVEEE--------ALG 141
Cdd:cd14170    113 AIQYLHSIN--IAHRDVKPENLLYTSKrpnAILKLTDFGFAKeTTSHnsltTPCYTpYYVAPEVLGPEKydkscdmwSLG 190

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  142 CILYLLCFRQHPF--------EDGAKLRIVNGKYSIPphDTQYTVF----HSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14170    191 VIMYILLCGYPPFysnhglaiSPGMKTRIRMGQYEFP--NPEWSEVseevKMLIRNLLKTEPTQRMTITEFMNH 262
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
 63-125 2.88e-06

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: 50.75  E-value: 2.88e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05102    168 PLTMEDLICYSFQVARGMEFLASRK--CIHRDLAARNILLSENNVVKICDFGLARDIYKDPDY 228
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
 42-203 3.13e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 50.49  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGPlscdtvlKIFYQTCRAV----QHMHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSA 116
Cdd:cd14031     91 VTELMTSGTLKTYLKRFKVMKP-------KVLRSWCRQIlkglQFLHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLA 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 T--------TISHYPDY----SWSAQRRALVEEEALGCILYLLCFRQHPF---EDGAKL--RIVNGKYSIPPHDTQYTVF 179
Cdd:cd14031    164 TlmrtsfakSVIGTPEFmapeMYEEHYDESVDVYAFGMCMLEMATSEYPYsecQNAAQIyrKVTSGIKPASFNKVTDPEV 243

                          170       180
                   ....*....|....*....|....
gi 1034639258  180 HSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14031    244 KEIIEGCIRQNKSERLSIKDLLNH 267
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 61-203 3.27e-06

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 49.97  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   61 RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTISH--YPDY---------SWS 128
Cdd:cd14100    100 RGALPEELARSFFRQVLEAVRHCHNCG--VLHRDIKDENILIDlNTGELKLIDFGSGALLKDtvYTDFdgtrvysppEWI 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  129 AQRRALVEEEA---LGCILYLLCFRQHPFEDGAKlrIVNG----KYSIPPHDTQytvfhsLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14100    178 RFHRYHGRSAAvwsLGILLYDMVCGDIPFEHDEE--IIRGqvffRQRVSSECQH------LIKWCLALRPSDRPSFEDIQ 249


                   ..
gi 1034639258  202 HQ 203
Cdd:cd14100    250 NH 251
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
 49-120 3.70e-06

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: 50.38  E-value: 3.70e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   49 GQLVEFLKKMESRGPLSCDTVLK-IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06639    109 GSVTELVKGLLKCGQRLDEAMISyILYGALLGLQHLHNNR--IIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 179
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 72-201 3.78e-06

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: 50.03  E-value: 3.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSN--QGT--IKLCDFGSATTISHyPDYSWSAQRRALVEE---------- 137
Cdd:cd14184    104 MVYNLASALKYLHGLC--IVHRDIKPENLLVCEypDGTksLKLGDFGLATVVEG-PLYTVCGTPTYVAPEiiaetgyglk 180

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  138 ---EALGCILYLLCFRQHPFEDGAKL------RIVNGKYSIP-PH-DTQYTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14184    181 vdiWAAGVITYILLCGFPPFRSENNLqedlfdQILLGKLEFPsPYwDNITDSAKELISHMLQVNVEARYTAEQIL 255
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 51-116 3.84e-06

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: 50.11  E-value: 3.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   51 LVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07861     85 LKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRR--VLHRDLKPQNLLIDNKGVIKLADFGLA 148
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
 49-120 4.12e-06

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: 50.01  E-value: 4.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   49 GQLVEFLKKMESRGPLSCDTVLK-IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06638    105 GSVTDLVKGFLKRGERMEEPIIAyILHEALMGLQHLHVNK--TIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 67-207 4.17e-06

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: 50.04  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   67 DTVLKIFYQTCRAVQHMHRQK-PPIIHRDLKVENLL---------LSNQgTIKLCDFGSA------TTISHYPDYSWSAQ 130
Cdd:cd14145    104 DILVNWAVQIARGMNYLHCEAiVPVIHRDLKSSNILilekvengdLSNK-ILKITDFGLArewhrtTKMSAAGTYAWMAP 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  131 ---RRALVEEE----ALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd14145    183 eviRSSMFSKGsdvwSYGVLLWELLTGEVPFRGIDGLAVAYGvamnKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTN 262


                   ....*...
gi 1034639258  200 VVHQLQEI 207
Cdd:cd14145    263 ILDQLTAI 270
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
 42-208 4.53e-06

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: 49.47  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKkmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------- 114
Cdd:cd05114     77 VTEFMENGCLLNYLR--QRRGKLSRDMLLSMCQDVCEGMEYLERNN--FIHRDLAARNCLVNDTGVVKVSDFGmtryvld 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 ---------------SATTISHYPDYS-----WSaqrralveeeaLGCILY-LLCFRQHPFEDGAKLRIVN----GKYSI 169
Cdd:cd05114    153 dqytsssgakfpvkwSPPEVFNYSKFSsksdvWS-----------FGVLMWeVFTEGKMPFESKSNYEVVEmvsrGHRLY 221

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034639258  170 PPHDTQYTVFHSLIRAMlQVNPEERLSIAEVVHQLQEIA 208
Cdd:cd05114    222 RPKLASKSVYEVMYSCW-HEKPEGRPTFADLLRTITEIA 259
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
 72-199 6.28e-06

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: 49.61  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTC--RAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDY------SWSAQRRA 133
Cdd:cd05589    104 VFYAACvvLGLQFLHEHK--IVYRDLKLDNLLLDTEGYVKIADFGlckegmgfgdRTSTFCGTPEFlapevlTDTSYTRA 181

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  134 lVEEEALGCILYLLCFRQHPF----EDGAKLRIVNgkysippHDTQYTVFHS-----LIRAMLQVNPEERLSIAE 199
Cdd:cd05589    182 -VDWWGLGVLIYEMLVGESPFpgddEEEVFDSIVN-------DEVRYPRFLSteaisIMRRLLRKNPERRLGASE 248
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
 49-117 6.38e-06

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: 49.63  E-value: 6.38e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKMEsrgpLSCDTVLKIFYQTCRAVQHMHRQ--------KPPIIHRDLKVENLLLSNQGTIKLCDFGSAT 117
Cdd:cd14053     78 GSLCDYLKGNV----ISWNELCKIAESMARGLAYLHEDipatngghKPSIAHRDFKSKNVLLKSDLTACIADFGLAL 150
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
 71-127 6.38e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 50.46  E-value: 6.38e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYP---DYSW 127
Cdd:PHA03210   271 AIMKQLLCAVEYIHDKK--LIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEReafDYGW 328
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 75-199 6.43e-06

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: 49.32  E-value: 6.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYS-------WSA-----QRRALVEEEA--- 139
Cdd:cd06632    110 QILSGLAYLHSRN--TVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKsfkgspyWMApevimQKNSGYGLAVdiw 187

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  140 -LGCILYLLCFRQHPFED----GAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd06632    188 sLGCTVLEMATGKPPWSQyegvAAIFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQ 252
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
 67-114 6.67e-06

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: 49.24  E-value: 6.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258   67 DTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL--SNQGTIKLCDFG 114
Cdd:cd13987     91 ERVKRCAAQLASALDFMHSKN--LVHRDIKPENVLLfdKDCRRVKLCDFG 138
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 75-201 7.29e-06

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: 49.16  E-value: 7.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT----------TISHYPDYSWSA--QRRALVEEE---A 139
Cdd:cd14189    109 QIISGLKYLHLKG--ILHRDLKLGNFFINENMELKVGDFGLAArleppeqrkkTICGTPNYLAPEvlLRQGHGPESdvwS 186

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  140 LGCILYLLCFRQHPFEDgAKLR-----IVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14189    187 LGCVMYTLLCGNPPFET-LDLKetyrcIKQVKYTLPASLSLPA--RHLLAGILKRNPGDRLTLDQIL 250
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
 46-226 8.13e-06

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: 48.90  E-value: 8.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKmesrGPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTISHY--- 122
Cdd:cd06642     84 LGGGSALDLLKP----GPLEETYIATILREILKGLDYLHSERK--IHRDIKAANVLLSEQGDVKLADFGVAGQLTDTqik 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 ------------PDYSWSAQRRALVEEEALGCILYLLCFRQHPFEDGAKLRIVN--GKYSIPPHDTQYTV-FHSLIRAML 187
Cdd:cd06642    158 rntfvgtpfwmaPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFliPKNSPPTLEGQHSKpFKEFVEACL 237

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034639258  188 QVNPEERLSIAEVvhqLQEIAAARNVNPKSPITELLEQN 226
Cdd:cd06642    238 NKDPRFRPTAKEL---LKHKFITRYTKKTSFLTELIDRY 273
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 55-114 8.24e-06

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: 49.29  E-value: 8.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   55 LKKMEsrGPLSCDTVLKIFYQTCRAVqHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06618    104 LKRIQ--GPIPEDILGKMTVSIVKAL-HYLKEKHGVIHRDVKPSNILLDESGNVKLCDFG 160
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
 75-116 8.31e-06

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: 48.76  E-value: 8.31e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSA 116
Cdd:cd14103     99 QICEGVQYMHKQG--ILHLDLKPENILCVSRTGnqIKIIDFGLA 140
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
 79-114 8.53e-06

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: 49.28  E-value: 8.53e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05571    107 ALGYLHSQG--IVYRDLKLENLLLDKDGHIKITDFG 140
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
 58-114 8.71e-06

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: 48.87  E-value: 8.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06643     94 LELERPLTEPQIRVVCKQTLEALVYLHENK--IIHRDLKAGNILFTLDGDIKLADFG 148
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
 51-120 8.74e-06

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: 49.19  E-value: 8.74e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07863     93 LRTYLDKVPPPG-LPAETIKDLMRQFLRGLDFLHANC--IVHRDLKPENILVTSGGQVKLADFGLARIYS 159
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 56-201 8.82e-06

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: 49.10  E-value: 8.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   56 KKMESRGPLSCdtvLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH----------YPDY 125
Cdd:cd14048    110 CTMESRELFVC---LNIFKQIASAVEYLHSKG--LIHRDLKPSNVFFSLDDVVKVGDFGLVTAMDQgepeqtvltpMPAY 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  126 SWSAQR---RALVEEE--------------ALGCILYLLCF-------RQHPFEDGAKLRivngkysIPPHDTQ-YTVFH 180
Cdd:cd14048    185 AKHTGQvgtRLYMSPEqihgnqysekvdifALGLILFELIYsfstqmeRIRTLTDVRKLK-------FPALFTNkYPEER 257

                          170       180
                   ....*....|....*....|.
gi 1034639258  181 SLIRAMLQVNPEERLSIAEVV 201
Cdd:cd14048    258 DMVQQMLSPSPSERPEAHEVI 278
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
 49-207 8.97e-06

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: 48.96  E-value: 8.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRGPLScdTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattISHYPDYS-- 126
Cdd:cd05056     91 GELRSYLQVNKYSLDLA--SLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSSPDCVKLGDFG----LSRYMEDEsy 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 WSAQRRAL----VEEEALG---------------CILYLLCFRQHPFEdGAK-----LRIVNGKySIPPHDTQYTVFHSL 182
Cdd:cd05056    163 YKASKGKLpikwMAPESINfrrftsasdvwmfgvCMWEILMLGVKPFQ-GVKnndviGRIENGE-RLPMPPNCPPTLYSL 240

                          170       180
                   ....*....|....*....|....*
gi 1034639258  183 IRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd05056    241 MTKCWAYDPSKRPRFTELKAQLSDI 265
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
 70-120 9.60e-06

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: 49.22  E-value: 9.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   70 LKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07872    106 VKIFlYQILRGLAYCHRRK--VLHRDLKPQNLLINERGELKLADFGLARAKS 155
PHA03247 PHA03247
large tegument protein UL36; Provisional
 730-1060 1.07e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  730 EGQEPRADPEPPGLAAGLVQQdlvfevETPAVLPEPVPqedgvdllglHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPP 809
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP------PPPPPTPEPAP----------HALVSATPLPPGPAAARQASPALPAAPAPPAV 2744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  810 EAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPS 889
Cdd:PHA03247  2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  890 AHSAPPPSCSAdflhlgdlPGEPSKMTASSSNPDLLGGWAAwtetAASAVAPTPATEGPLFSPGGQPAPCGSQ-ASWTKS 968
Cdd:PHA03247  2825 AGPLPPPTSAQ--------PTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS 2892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  969 QNPDPFADLGDLSSGLQDPQAQS----TVSPRGQRVCTCSRRLPTGKLKPGVADTGTAASPHRHCGSPA----GFPPGGF 1040
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgALVPGRV 2972

                          330       340
                   ....*....|....*....|
gi 1034639258 1041 IPKTATTPKGSSSWQTSRPP 1060
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAPASS 2992
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 77-201 1.08e-05

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: 48.38  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   77 CR----AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYS----------WSA----QRRAL---V 135
Cdd:cd06647    109 CReclqALEFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQSkrstmvgtpyWMApevvTRKAYgpkV 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  136 EEEALGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVV 201
Cdd:cd06647    185 DIWSLGIMAIEMVEGEPPYLNENPLRALyliatNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELL 255
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
 60-125 1.08e-05

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: 48.91  E-value: 1.08e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   60 SRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd07858    101 SSQTLSDDHCQYFLYQLLRGLKYIHSAN--VLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF 164
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
 72-154 1.21e-05

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: 48.51  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI--------------------------SHYP 123
Cdd:cd05605    105 VFYaaEITCGLEHLHSER--IVYRDLKPENILLDDHGHVRISDLGLAVEIpegetirgrvgtvgymapevvkneryTFSP 182

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034639258  124 DYsWSaqrralveeeaLGCILYLLCFRQHPF 154
Cdd:cd05605    183 DW-WG-----------LGCLIYEMIEGQAPF 201
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 50-201 1.23e-05

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 48.45  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   50 QLV---EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLL-----------LSNQGTIKLCDFGS 115
Cdd:cd14166     80 QLVsggELFDRILERGVYTEKDASRVINQVLSAVKYLHENG--IVHRDLKPENLLyltpdenskimITDFGLSKMEQNGI 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  116 ATTISHYPDYSWS---AQR--RALVEEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PPHDTQYTVFHSLIR 184
Cdd:cd14166    158 MSTACGTPGYVAPevlAQKpySKAVDCWSIGVITYILLCGYPPFyeETESRLfeKIKEGYYEFesPFWDDISESAKDFIR 237

                          170
                   ....*....|....*..
gi 1034639258  185 AMLQVNPEERLSIAEVV 201
Cdd:cd14166    238 HLLEKNPSKRYTCEKAL 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
 60-204 1.24e-05

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: 48.38  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   60 SRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL-----SNQGTIKLCDFG--------SATTISHYPDYS 126
Cdd:cd14000    105 SFASLGRTLQQRIALQVADGLRYLHSAM--IIYRDLKSHNVLVwtlypNSAIIIKIADYGisrqccrmGAKGSEGTPGFR 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 WSAQRRALVEEE------ALGCILYLLCFRQHPFEDGAKLRI-VNGKYSIPPHDTQY-----TVFHSLIRAMLQVNPEER 194
Cdd:cd14000    183 APEIARGNVIYNekvdvfSFGMLLYEILSGGAPMVGHLKFPNeFDIHGGLRPPLKQYecapwPEVEVLMKKCWKENPQQR 262

                          170
                   ....*....|
gi 1034639258  195 LSIAEVVHQL 204
Cdd:cd14000    263 PTAVTVVSIL 272
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
 62-130 1.26e-05

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: 48.54  E-value: 1.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQ 130
Cdd:cd07869     98 GGLHPENVKLFLFQLLRGLSYIHQRY--ILHRDLKPQNLLISDTGELKLADFGLARAKS-VPSHTYSNE 163
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
 42-207 1.32e-05

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: 48.05  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH 121
Cdd:cd05082     78 VTEYMAKGSLVDYLRS-RGRSVLGGDCLLKFSLDVCEAMEYLEGNN--FVHRDLAARNVLVSEDNVAKVSDFGLTKEASS 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 YPDYS-----WSAQrRALVEEE--------ALGCILY-LLCFRQHPF------------EDGAKLRIVNGkysIPPhdtq 175
Cdd:cd05082    155 TQDTGklpvkWTAP-EALREKKfstksdvwSFGILLWeIYSFGRVPYpriplkdvvprvEKGYKMDAPDG---CPP---- 226

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034639258  176 ytVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd05082    227 --AVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
 51-225 1.43e-05

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: 48.49  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKmesrgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYS---- 126
Cdd:cd06633    110 LLEVHKK-----PLQEVEIAAITHGALQGLAYLHSHN--MIHRDIKAGNILLTEPGQVKLADFGSASIAS--PANSfvgt 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 --WSAQRRALVEEE----------ALGCILYLLCFRQHPFEDgakLRIVNGKYSIPPHDT------QYT-VFHSLIRAML 187
Cdd:cd06633    181 pyWMAPEVILAMDEgqydgkvdiwSLGITCIELAERKPPLFN---MNAMSALYHIAQNDSptlqsnEWTdSFRGFVDYCL 257

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034639258  188 QVNPEERLSIAEVV-HQLqeiaaARNVNPKSPITELLEQ 225
Cdd:cd06633    258 QKIPQERPSSAELLrHDF-----VRRERPPRVLIDLIQR 291
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
 42-114 1.45e-05

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: 48.12  E-value: 1.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06610     77 VMPLLSGGSLLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNG--QIHRDVKAGNILLGEDGSVKIADFG 147
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
 61-116 1.46e-05

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: 48.20  E-value: 1.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   61 RGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07839     93 NGDIDPEIVKSFMFQLLKGLAFCHSHN--VLHRDLKPQNLLINKNGELKLADFGLA 146
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 79-196 1.46e-05

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 48.47  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTI--SHYPDYsWSAQrrALV------EEEAL---------- 140
Cdd:cd05598    113 AIESVH--KMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwTHDSKY-YLAH--SLVgtpnyiAPEVLlrtgytqlcd 187

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  141 ----GCILYLLCFRQHPF----EDGAKLRIVNGKYS--IPPHDTQYTVFHSLIRAMLqVNPEERLS 196
Cdd:cd05598    188 wwsvGVILYEMLVGQPPFlaqtPAETQLKVINWRTTlkIPHEANLSPEAKDLILRLC-CDAEDRLG 252
Pkinase pfam00069
Protein kinase domain;
49-202 1.47e-05

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 47.62  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKmesRGPLSCDTVLKIFYQTCRAvqhmhrqkppiihrdLKVENLLLSNQGT--------IKLCDFGSATTIs 120
Cdd:pfam00069   83 GSLFDLLSE---KGAFSEREAKFIMKQILEG---------------LESGSSLTTFVGTpwymapevLGGNPYGPKVDV- 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 hypdysWSaqrralveeeaLGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPPHDtqYTV---FHSLIRAMLQVNPEE 193
Cdd:pfam00069  144 ------WS-----------LGCILYELLTGKPPFpginGNEIYELIIDQPYAFPELP--SNLseeAKDLLKKLLKKDPSK 204


                   ....*....
gi 1034639258  194 RLSIAEVVH 202
Cdd:pfam00069  205 RLTATQALQ 213
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 58-114 1.56e-05

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: 48.59  E-value: 1.56e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   58 MESRGPLSCDTVLK------------IFYQTCRAVQHMhRQKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06615     78 MEHMDGGSLDQVLKkagripenilgkISIAVLRGLTYL-REKHKIMHRDVKPSNILVNSRGEIKLCDFG 145
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
 49-195 1.57e-05

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: 48.08  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLkkmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG---------TIKLCDFG----- 114
Cdd:cd14201     90 GDLADYL---QAKGTLSEDTIRVFLQQIAAAMRILHSKG--IIHRDLKPQNILLSYASrkkssvsgiRIKIADFGfaryl 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 ----SATTISHYPDYS-----WSAQRRALVEEEALGCILYLLCFRQHPFEDGA--KLRIVNGKY-----SIPPHDTQYtv 178
Cdd:cd14201    165 qsnmMAATLCGSPMYMapeviMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSpqDLRMFYEKNknlqpSIPRETSPY-- 242

                          170
                   ....*....|....*..
gi 1034639258  179 FHSLIRAMLQVNPEERL 195
Cdd:cd14201    243 LADLLLGLLQRNQKDRM 259
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
 51-120 1.59e-05

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: 48.37  E-value: 1.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   51 LVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTIS 120
Cdd:cd14135     89 LREVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCN--ILHADIKPDNILVNeKKNTLKLCDFGSASDIG 157
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 46-116 1.65e-05

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: 47.73  E-value: 1.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   46 LAEGQLVEFLKkmeSRGP--LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd05039     82 MAKGSLVDYLR---SRGRavITRKDQLGFALDVCEGMEYLESKK--FVHRDLAARNVLVSEDNVAKVSDFGLA 149
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
 49-223 1.68e-05

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 48.12  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESRGPLSCDTVLKIF--YQTCRAVQHMHRQKppIIHRDLKVENLLL----------------SNQGtIKL 110
Cdd:cd13981     86 GTLLDVVNKMKNKTGGGMDEPLAMFftIELLKVVEALHEVG--IIHGDIKPDNFLLrleicadwpgegengwLSKG-LKL 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  111 CDFGSATTISHYPDYswsAQRRALVEEEALGCI--------------------LYLLCFRQHpfedgAKLRIVNGKYSIP 170
Cdd:cd13981    163 IDFGRSIDMSLFPKN---QSFKADWHTDSFDCIemregrpwtyqidyfgiaatIHVMLFGKY-----MELTQESGRWKIN 234

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  171 PHDTQY---TVFHSLIRAMLqvNPEERLSIAEVVHQLQEI----------AAARNVNPKSPITELL 223
Cdd:cd13981    235 QNLKRYwqrDIWNKFFDTLL--NPEPSCNTLPLLEELRKIleemeawfeaSLCNNLVVLRKLREIL 298
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
 73-121 1.87e-05

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: 47.71  E-value: 1.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034639258   73 FYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH 121
Cdd:cd14069    106 FQQLMAGLKYLHSCG--ITHRDIKPENLLLDENDNLKISDFGLATVFRY 152
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 73-125 2.21e-05

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: 47.99  E-value: 2.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI--SHY-------PDY 125
Cdd:cd05599    105 FYiaETVLAIESIHKLG--YIHRDIKPDNLLLDARGHIKLSDFGLCTGLkkSHLaystvgtPDY 166
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
 72-195 2.39e-05

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: 47.68  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIshyPDYSWSAQRRALVEEEA---------- 139
Cdd:cd05631    105 IFYaaELCCGLEDLQRER--IVYRDLKPENILLDDRGHIRISDLGLAVQI---PEGETVRGRVGTVGYMApevinnekyt 179

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  140 -------LGCILYLLCFRQHPFE--------DGAKLRIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPEERL 195
Cdd:cd05631    180 fspdwwgLGCLIYEMIQGQSPFRkrkervkrEEVDRRVKEDQEEYSEKFSEDA--KSICRMLLTKNPKERL 248
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
 45-119 2.49e-05

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: 47.51  E-value: 2.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   45 VLAEGQLVEFLKKMesrGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT-IKLCDFGSATTI 119
Cdd:cd13991     79 LKEGGSLGQLIKEQ---GCLPEDRALHYLGQALEGLEYLHSRK--ILHGDVKADNVLLSSDGSdAFLCDFGHAECL 149
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 62-116 2.54e-05

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: 47.42  E-value: 2.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT-IKLCDFGSA 116
Cdd:cd06630     98 GAFSENVIINYTLQILRGLAYLHDNQ--IIHRDLKGANLLVDSTGQrLRIADFGAA 151
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
 58-128 2.70e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.92  E-value: 2.70e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD----YSWS 128
Cdd:PHA03207   176 VDRSGPLPLEQAITIQRRLLEALAYLHGRG--IIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDtpqcYGWS 248
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-226 2.85e-05

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 47.51  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT---IKLCDFG---------SATTISHYPDYSWSAQRRAL-----VEE 137
Cdd:cd14085    106 QILEAVAYLHENG--IVHRDLKPENLLYATPAPdapLKIADFGlskivdqqvTMKTVCGTPGYCAPEILRGCaygpeVDM 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  138 EALGCILYLLCFRQHPFEDGAK-----LRIVNGKYSI--PPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ--LQEIA 208
Cdd:cd14085    184 WSVGVITYILLCGFEPFYDERGdqymfKRILNCDYDFvsPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHpwVTGKA 263

                          170
                   ....*....|....*...
gi 1034639258  209 AARNvNPKSPITELLEQN 226
Cdd:cd14085    264 ANFA-HMDTAQKKLQEFN 280
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
 47-120 3.02e-05

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: 46.72  E-value: 3.02e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   47 AEGQLVEFLKkmeSRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd14059     64 PYGQLYEVLR---AGREITPSLLVDWSKQIASGMNYLHLHK--IIHRDLKSPNVLVTYNDVLKISDFGTSKELS 132
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
 45-199 3.07e-05

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: 47.32  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   45 VLAEGQLVEFLKKMESrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSATTIS 120
Cdd:cd14194     89 LVAGGELFDFLAEKES---LTEEEATEFLKQILNGVYYLHSLQ--IAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKID 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 HYPDYSWSAQRRALVEEE--------------ALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPPHDTQYTVFH 180
Cdd:cd14194    164 FGNEFKNIFGTPEFVAPEivnyeplgleadmwSIGVITYILLSGASPFlgdtkqETLANVSAVNYEFEDEYFSNTSALAK 243

                          170
                   ....*....|....*....
gi 1034639258  181 SLIRAMLQVNPEERLSIAE 199
Cdd:cd14194    244 DFIRRLLVKDPKKRMTIQD 262
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
 68-117 3.15e-05

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: 47.00  E-value: 3.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258   68 TVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT 117
Cdd:cd14062     90 QLIDIARQTAQGMDYLHAKN--IIHRDLKSNNIFLHEDLTVKIGDFGLAT 137
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
 42-117 3.22e-05

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 46.92  E-value: 3.22e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGPlscdTVLKIF-YQTCRAVQHMHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSAT 117
Cdd:cd14033     82 VTELMTSGTLKTYLKRFREMKL----KLLQRWsRQILKGLHFLHSRCPPILHRDLKCDNIFITGpTGSVKIGDLGLAT 155
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 53-197 3.24e-05

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: 47.12  E-value: 3.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAQRR 132
Cdd:cd14111     85 ELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRR--VLHLDIKPDNIMVTNLNAIKIVDFGSAQSFN--PLSLRQLGRR 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  133 A---------LVEEE---------ALGCILYLLCFRQHPFEDG----AKLRIVNGKY---SIPPHDTQYTVfhSLIRAML 187
Cdd:cd14111    161 TgtleymapeMVKGEpvgppadiwSIGVLTYIMLSGRSPFEDQdpqeTEAKILVAKFdafKLYPNVSQSAS--LFLKKVL 238

                          170
                   ....*....|
gi 1034639258  188 QVNPEERLSI 197
Cdd:cd14111    239 SSYPWSRPTT 248
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
 72-195 3.40e-05

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: 47.21  E-value: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIshyPDYSWSAQRRA---------LVEEE-- 138
Cdd:cd05607    107 IFYsaQITCGILHLHSLK--IVYRDMKPENVLLDDNGNCRLSDLGLAVEV---KEGKPITQRAGtngymapeiLKEESys 181

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  139 ------ALGCILYLLCFRQHPFED--------GAKLRIVNGKYSIpPHDTQYTVFHSLIRAMLQVNPEERL 195
Cdd:cd05607    182 ypvdwfAMGCSIYEMVAGRTPFRDhkekvskeELKRRTLEDEVKF-EHQNFTEEAKDICRLFLAKKPENRL 251
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
 66-128 3.40e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 47.68  E-value: 3.40e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   66 CDtVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA---TTISHYPDYSWS 128
Cdd:PHA03212   182 CD-ILAIERSVLRAIQYLHENR--IIHRDIKAENIFINHPGDVCLGDFGAAcfpVDINANKYYGWA 244
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 699-1082 3.62e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 48.22  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  699 ENASSKESESALMEDRDESEVSDEG----GSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQ-----E 769
Cdd:pfam03154  140 DNRSTSPSIPSPQDNESDSDSSAQQqilqTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAtsqppN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  770 DGVDLLGLHSEVGAGPAVPPQACKAPSSntdllscllgPPEAASQGPPEDLLSEDPL---LLASPAPPL--SVQSTPRGG 844
Cdd:pfam03154  220 QTQSTAAPHTLIQQTPTLHPQRLPSPHP----------PLQPMTQPPPPSQVSPQPLpqpSLHGQMPPMphSLQTGPSHM 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  845 P-PAAADPFGPLLPSSGNNSQPCSNPDLFGEflNSDSVTVPPSFPSAHSAPPPS------CSADFLHLGDLPGEP-SKMT 916
Cdd:pfam03154  290 QhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ--SQQRIHTPPSQSQLQSQQPPReqplppAPLSMPHIKPPPTTPiPQLP 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  917 ASSSN--PDLLGGWAAWTetAASAVAPTPATEgPLFSPGGQPAPcgsqaswtkSQNPDPFaDLGDLSSGLQDPQAQSTVS 994
Cdd:pfam03154  368 NPQSHkhPPHLSGPSPFQ--MNSNLPPPPALK-PLSSLSTHHPP---------SAHPPPL-QLMPQSQQLPPPPAQPPVL 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  995 PRGQRV-CTCSRRLPTGKLKPGVADTGTAASPHRHCGSPAGFPPGGfiPKTATTPKGSsswqTSRPPAQGASWPPQAKPP 1073
Cdd:pfam03154  435 TQSQSLpPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSG--PPTSTSSAMP----GIQPPSSASVSSSGPVPA 508

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1034639258 1074 PKAC---------------------------TQPRP 1082
Cdd:pfam03154  509 AVSCplppvqikeealdeaeepesppppprsPSPEP 544
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
 72-195 3.92e-05

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: 47.18  E-value: 3.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI----SHYPDYSWSAQRRA---LVEEE---- 138
Cdd:cd05608    108 CFYtaQIISGLEHLHQRR--IIYRDLKPENVLLDDDGNVRISDLGLAVELkdgqTKTKGYAGTPGFMApelLLGEEydys 185

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  139 ----ALGCILYLLCFRQHPFE-DGAKLRIVNGKYSIPPHDTQYTV-----FHSLIRAMLQVNPEERL 195
Cdd:cd05608    186 vdyfTLGVTLYEMIAARGPFRaRGEKVENKELKQRILNDSVTYSEkfspaSKSICEALLAKDPEKRL 252
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
 46-125 4.11e-05

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: 47.33  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05105    217 SNDSEVKNLLSDDGSEG-LTTLDLLSFTYQVARGMEFLASKN--CVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNY 293
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
 42-117 4.14e-05

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 46.61  E-value: 4.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGPlscdtvlKIFYQTCRAVQH----MHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSA 116
Cdd:cd14032     82 VTELMTSGTLKTYLKRFKVMKP-------KVLRSWCRQILKgllfLHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLA 154


                   .
gi 1034639258  117 T 117
Cdd:cd14032    155 T 155
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
 62-120 4.26e-05

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: 46.99  E-value: 4.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06641     96 GPLDETQIATILREILKGLDYLHSEKK--IHRDIKAANVLLSEHGEVKLADFGVAGQLT 152
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 42-200 4.34e-05

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: 47.17  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGPLSCDTVLKifyQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQG---TIKLCDFGSA-- 116
Cdd:cd14180     79 VMELLRGGELLDRIKKKARFSESEASQLMR---SLVSAVSFMH--EAGVVHRDLKPENILYADESdgaVLKVIDFGFArl 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 ----TTISHYPDYSWSAQRRALVEEE---------ALGCILYLLCFRQHPFEDGAKL-----------RIVNGKYSIPPH 172
Cdd:cd14180    154 rpqgSRPLQTPCFTLQYAAPELFSNQgydescdlwSLGVILYTMLSGQVPFQSKRGKmfhnhaadimhKIKEGDFSLEGE 233

                          170       180       190
                   ....*....|....*....|....*....|
gi 1034639258  173 DTQYTVFHS--LIRAMLQVNPEERLSIAEV 200
Cdd:cd14180    234 AWKGVSEEAkdLVRGLLTVDPAKRLKLSEL 263
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
 82-116 4.52e-05

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: 46.73  E-value: 4.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1034639258   82 HMHRqkppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07860    117 HSHR----VLHRDLKPQNLLINTEGAIKLADFGLA 147
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
 55-116 4.83e-05

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: 46.72  E-value: 4.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   55 LKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14025     80 LEKLLASEPLPWELRFRIIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGLA 141
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
 58-201 4.86e-05

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 46.19  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   58 MESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKL-CDFGSATTISHYPDYSWSAQR--RAL 134
Cdd:cd14023     75 VRSCKRLREEEAARLFKQIVSAVAHCHQSA--IVLGDLKLRKFVFSDEERTQLrLESLEDTHIMKGEDDALSDKHgcPAY 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  135 VEEE----------------ALGCILYLLCFRQHPFEDG------AKLRivNGKYSIPPHDTQYTvfHSLIRAMLQVNPE 192
Cdd:cd14023    153 VSPEilnttgtysgksadvwSLGVMLYTLLVGRYPFHDSdpsalfSKIR--RGQFCIPDHVSPKA--RCLIRSLLRREPS 228


                   ....*....
gi 1034639258  193 ERLSIAEVV 201
Cdd:cd14023    229 ERLTAPEIL 237
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
 51-120 5.10e-05

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: 46.56  E-value: 5.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07862     95 LTTYLDKVPEPG-VPTETIKDMMFQLLRGLDFLHSHR--VVHRDLKPQNILVTSSGQIKLADFGLARIYS 161
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
 73-195 5.27e-05

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: 46.89  E-value: 5.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYSWSAQRRA-----LV 135
Cdd:cd05603    100 FYaaEVASAIGYLHSLN--IIYRDLKPENILLDCQGHVVLTDFGlckegmepeeTTSTFCGTPEYLAPEVLRKepydrTV 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  136 EEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERL 195
Cdd:cd05603    178 DWWCLGAVLYEMLYGLPPFysRDVSQMydNILHKPLHLPGGKTVAAC--DLLQGLLHKDQRRRL 239
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 62-194 5.33e-05

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 46.56  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTI--------SHYPDYSWSAQRRA 133
Cdd:cd06646    101 GPLSELQIAYVCRETLQGLAYLHSKGK--MHRDIKGANILLTDNGDVKLADFGVAAKItatiakrkSFIGTPYWMAPEVA 178

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258  134 LVEEE----------ALGCILYLLCFRQHPFEDGAKLR--IVNGKYSIPP----HDTQY-TVFHSLIRAMLQVNPEER 194
Cdd:cd06646    179 AVEKNggynqlcdiwAVGITAIELAELQPPMFDLHPMRalFLMSKSNFQPpklkDKTKWsSTFHNFVKISLTKNPKKR 256
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
 56-114 5.55e-05

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: 46.62  E-value: 5.55e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   56 KKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPpIIHRDLKVENLLLSNQ-GTIKLCDFG 114
Cdd:cd14001     99 RYEAGLGPFPAATILKVALSIARALEYLHNEKK-ILHGDIKSGNVLIKGDfESVKLCDFG 157
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 51-116 5.67e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; 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. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. 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. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 47.00  E-value: 5.67e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQG--TIKLCDFGSA 116
Cdd:cd14225    131 LYELIKKNNFQG-FSLSLIRRFAISLLQCLRLLYRER--IIHCDLKPENILLRQRGqsSIKVIDFGSS 195
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
 19-126 6.48e-05

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: 46.70  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   19 GASGRDQSDFVGQTVELgelrlrvRRVLAEGQLVEF-LKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKV 97
Cdd:cd07854     72 GPSGSDLTEDVGSLTEL-------NSVYIVQEYMETdLANVLEQGPLSEEHARLFMYQLLRGLKYIHSAN--VLHRDLKP 142

                           90       100       110
                   ....*....|....*....|....*....|
gi 1034639258   98 ENLLLSNQG-TIKLCDFGSATTIShyPDYS 126
Cdd:cd07854    143 ANVFINTEDlVLKIGDFGLARIVD--PHYS 170
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
 62-116 6.51e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 46.79  E-value: 6.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:PHA03209   152 RPLPIDQALIIEKQILEGLRYLHAQR--IIHRDVKTENIFINDVDQVCIGDLGAA 204
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1196-1235 6.73e-05

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 42.07  E-value: 6.73e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034639258 1196 EQVKKHYRRAVLAVHPDKAAGQPyeqHAKMIFMELNDAWS 1235
Cdd:pfam00226   15 EEIKKAYRKLALKYHPDKNPGDP---EAEEKFKEINEAYE 51
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
 49-208 7.06e-05

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: 46.28  E-value: 7.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLkkmeSRGPLSCDTVLKIFYQTCRAVQHMHRQ------KPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHY 122
Cdd:cd14142     88 GSLYDYL----QRTTLDHQEMLRLALSAASGLVHLHTEifgtqgKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTHSQE 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 PDY---------------------------SWSAQRRALVeeEALGCILYLLCFR----------QHP----------FE 155
Cdd:cd14142    164 TNQldvgnnprvgtkrymapevldetintdCFESYKRVDI--YAFGLVLWEVARRcvsggiveeyKPPfydvvpsdpsFE 241

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  156 DGAKLRIVNG-KYSIPPH---DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIA 208
Cdd:cd14142    242 DMRKVVCVDQqRPNIPNRwssDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 693-1065 7.74e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 7.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  693 EAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQdlvfEVETPAVLPEPVPQEDGV 772
Cdd:PHA03307    78 EAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLS----EMLRPVGSPGPPPAASPP 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  773 DLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPF 852
Cdd:PHA03307   154 AAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  853 GPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPppscsadflhlgdLPGEPSKMTASSSNPDllggwaawt 932
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW-------------NGPSSRPGPASSSSSP--------- 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  933 etAASAVAPTPAtegplfSPGGQPAPCGSQASWTKSQNPDpfadlGDLSSGLQDPQAQSTVSPRGQRVCTCSRRLPTGKL 1012
Cdd:PHA03307   292 --RERSPSPSPS------SPGSGPAPSSPRASSSSSSSRE-----SSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034639258 1013 KPGVADTGTAASPHRHCGSPAGFPPGGFIPKTATTPKGSSSWQtSRPPAQGAS 1065
Cdd:PHA03307   359 PADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRR-DATGRFPAG 410
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 695-1097 7.81e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 7.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  695 ETGAENASSKESESALMEDRDESEVSDEGGSPISSEGqePRADPePPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDL 774
Cdd:PHA03307    12 EAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSA--ELAAV-TVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  775 LGLHSEVGAGPAVPPQACKAPSSNTDllscllGPPEAASQgPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGP 854
Cdd:PHA03307    89 TWSLSTLAPASPAREGSPTPPGPSSP------DPPPPTPP-PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  855 LlPSSGNNSQPCSNPdlfgefLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTET 934
Cdd:PHA03307   162 V-ASDAASSRQAALP------LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  935 AASAVAPT--------PATEGPLFSPGGQPAP-CGSQASWTKSQNPDPfadlgdlssglqdpqaqSTVSPRGqrvctcSR 1005
Cdd:PHA03307   235 SSSDSSSSessgcgwgPENECPLPRPAPITLPtRIWEASGWNGPSSRP-----------------GPASSSS------SP 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258 1006 RLPTGKLKPGVADTGTAASPHRHCGSPAGFPPGGfIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKAC------TQ 1079
Cdd:PHA03307   292 RERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS-SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPssprkrPR 370

                          410
                   ....*....|....*...
gi 1034639258 1080 PRPNyASNFSVIGAREER 1097
Cdd:PHA03307   371 PSRA-PSSPAASAGRPTR 387
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
 51-116 8.95e-05

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 46.09  E-value: 8.95e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSA 116
Cdd:cd14212     88 LYELLKQNQFRG-LSLQLIRKFLQQLLDALSVLKDAR--IIHCDLKPENILLVNLDSpeIKLIDFGSA 152
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
 49-199 9.51e-05

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: 45.36  E-value: 9.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKkmeSRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSATTISH----- 121
Cdd:cd14121     80 GDLSRFIR---SRRTLPESTVRRFLQQLASALQFLREHN--ISHMDLKPQNLLLSSRYNpvLKLADFGFAQHLKPndeah 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 -------Y--PDYSWSAQRRALVEEEALGCILYLLCFRQHPF------EDGAKLRiVNGKYSIPPHDTQYTVFHSLIRAM 186
Cdd:cd14121    155 slrgsplYmaPEMILKKKYDARVDLWSVGVILYECLFGRAPFasrsfeELEEKIR-SSKPIEIPTRPELSADCRDLLLRL 233

                          170
                   ....*....|...
gi 1034639258  187 LQVNPEERLSIAE 199
Cdd:cd14121    234 LQRDPDRRISFEE 246
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
 46-126 9.77e-05

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: 45.65  E-value: 9.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKP-PIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD 124
Cdd:cd14160     74 MQNGTLFDRLQCHGVTKPLSWHERINILIGIAKAIHYLHNSQPcTVICGNISSANILLDDQMQPKLTDFALAHFRPHLED 153


                   ..
gi 1034639258  125 YS 126
Cdd:cd14160    154 QS 155
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
 80-197 1.03e-04

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: 45.71  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   80 VQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYSWSAQRRAL-----VEEEALGCIL 144
Cdd:cd05620    109 LQFLHSKG--IIYRDLKLDNVMLDRDGHIKIADFGmckenvfgdnRASTFCGTPDYIAPEILQGLkytfsVDWWSFGVLL 186

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  145 YLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHS--LIRAMLQVNPEERLSI 197
Cdd:cd05620    187 YEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESkdILEKLFERDPTRRLGV 241
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
 75-135 1.03e-04

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: 45.51  E-value: 1.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdySWSAQRRALV 135
Cdd:cd06648    111 AVLKALSFLHSQG--VIHRDIKSDSILLTSDGRVKLSDFGFCAQVS-----KEVPRRKSLV 164
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
 64-117 1.03e-04

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 45.53  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL---SNQGTIKLCDFGSAT 117
Cdd:cd14016     93 FSLKTVLMLADQMISRLEYLHSKG--YIHRDIKPENFLMglgKNSNKVYLIDFGLAK 147
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
 82-120 1.05e-04

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: 45.82  E-value: 1.05e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034639258   82 HMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07865    134 YIHRNK--ILHRDMKAANILITKDGVLKLADFGLARAFS 170
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
 42-117 1.07e-04

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 45.81  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRGplscdtvLKIFYQTCRAV----QHMHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSA 116
Cdd:cd14030    106 VTELMTSGTLKTYLKRFKVMK-------IKVLRSWCRQIlkglQFLHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLA 178


                   .
gi 1034639258  117 T 117
Cdd:cd14030    179 T 179
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 42-116 1.10e-04

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: 45.52  E-value: 1.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258   42 VRRVLAEGQLVEFLKKMesRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd05059     77 VTEYMANGCLLNYLRER--RGKFQTEQLLEMCKDVCEAMEYLESNG--FIHRDLAARNCLVGEQNVVKVSDFGLA 147
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
 72-155 1.12e-04

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: 45.76  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDY------SWSAQRRAlV 135
Cdd:cd05616    104 VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGmckeniwdgvTTKTFCGTPDYiapeiiAYQPYGKS-V 182

                           90       100
                   ....*....|....*....|
gi 1034639258  136 EEEALGCILYLLCFRQHPFE 155
Cdd:cd05616    183 DWWAFGVLLYEMLAGQAPFE 202
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
 62-119 1.12e-04

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: 45.42  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI 119
Cdd:cd06625     97 GALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANILRDSNGNVKLGDFGASKRL 152
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
 49-125 1.15e-04

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: 45.55  E-value: 1.15e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   49 GQLVEFLKKmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05055    124 GDLLNFLRR-KRESFLTLEDLLSFSYQVAKGMAFLASKN--CIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNY 197
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
 48-131 1.21e-04

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: 45.49  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   48 EGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySW 127
Cdd:cd14052     87 NGSLDVFLSELGLLGRLDEFRVWKILVELSLGLRFIHDHH--FVHLDLKPANVLITFEGTLKIGDFGMAT--------VW 156


                   ....
gi 1034639258  128 SAQR 131
Cdd:cd14052    157 PLIR 160
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 42-198 1.27e-04

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: 45.42  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESrgpLSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQG---TIKLCDFGSA-- 116
Cdd:cd14179     80 VMELLKGGELLERIKKKQH---FSETEASHIMRKLVSAVSHMH--DVGVVHRDLKPENLLFTDESdnsEIKIIDFGFArl 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 ----TTISHYPDYSWSAQRRALVEEE---------ALGCILYLLCFRQHPFEDGAKL-----------RIVNGKYSIPPH 172
Cdd:cd14179    155 kppdNQPLKTPCFTLHYAAPELLNYNgydescdlwSLGVILYTMLSGQVPFQCHDKSltctsaeeimkKIKQGDFSFEGE 234

                          170       180
                   ....*....|....*....|....*...
gi 1034639258  173 DTQYTVFHS--LIRAMLQVNPEERLSIA 198
Cdd:cd14179    235 AWKNVSQEAkdLIQGLLTVDPNKRIKMS 262
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
 36-125 1.37e-04

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: 45.34  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   36 GELR--LRVRRvlAEGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDF 113
Cdd:cd05099    103 GNLRefLRARR--PPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRR--CIHRDLAARNVLVTEDNVMKIADF 178

                           90
                   ....*....|..
gi 1034639258  114 GSATTIsHYPDY 125
Cdd:cd05099    179 GLARGV-HDIDY 189
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 85-175 1.37e-04

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: 45.43  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   85 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEALGCILYLlcfRQHPFEDGAKL-RIV 163
Cdd:cd06650    120 REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSV---QSDIWSMGLSLvEMA 196

                           90
                   ....*....|..
gi 1034639258  164 NGKYSIPPHDTQ 175
Cdd:cd06650    197 VGRYPIPPPDAK 208
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
 60-120 1.38e-04

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: 45.47  E-value: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   60 SRGPLScDTVLKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07857     98 SGQPLT-DAHFQSFiYQILCGLKYIHSAN--VLHRDLKPGNLLVNADCELKICDFGLARGFS 156
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 73-214 1.43e-04

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: 45.34  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYSWSAQRRA-----LV 135
Cdd:cd05604    101 FYaaEIASALGYLHSIN--IVYRDLKPENILLDSQGHIVLTDFGlckegisnsdTTTTFCGTPEYLAPEVIRKqpydnTV 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  136 EEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPhDTQYTVFhSLIRAMLQVNPEERLSIAEVVHQLQEIAAAR 211
Cdd:cd05604    179 DWWCLGSVLYEMLYGLPPFycRDTAEMyeNILHKPLVLRP-GISLTAW-SILEELLEKDRQLRLGAKEDFLEIKNHPFFE 256


                   ...
gi 1034639258  212 NVN 214
Cdd:cd05604    257 SIN 259
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 73-131 1.51e-04

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: 45.79  E-value: 1.51e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQR 131
Cdd:cd05600    115 FYiaEMFAAISSLHQLG--YIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKIESMKIR 173
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
 67-114 1.55e-04

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: 45.00  E-value: 1.55e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   67 DTVLK------------IFYQTCRAVQHMHRQKPPIIHRDLKVENLLL---SNQGTIKLCDFG 114
Cdd:cd13990     93 DFYLKqhksiperearsIIMQVVSALKYLNEIKPPIIHYDLKPGNILLhsgNVSGEIKITDFG 155
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
 64-114 1.59e-04

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: 44.61  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd14050     97 LPESEVWNILLDLLKGLKHLHDHG--LIHLDIKPANIFLSKDGVCKLGDFG 145
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
 72-162 1.60e-04

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: 45.35  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAT-------------TISHYPDYSWSAQRRALVE 136
Cdd:cd05632    107 LFYaaEILCGLEDLHREN--TVYRDLKPENILLDDYGHIRISDLGLAVkipegesirgrvgTVGYMAPEVLNNQRYTLSP 184

                           90       100
                   ....*....|....*....|....*..
gi 1034639258  137 EE-ALGCILYLLCFRQHPFEdGAKLRI 162
Cdd:cd05632    185 DYwGLGCLIYEMIEGQSPFR-GRKEKV 210
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 79-114 1.64e-04

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: 45.08  E-value: 1.64e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05582    109 ALDHLHSLG--IIYRDLKPENILLDEDGHIKLTDFG 142
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
 75-198 1.67e-04

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 44.71  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQG---TIKLCDFGSATTIshyPDYSWsaqRRALVEEEA------------ 139
Cdd:cd14082    111 QILVALRYLHSKN--IVHCDLKPENVLLASAEpfpQVKLCDFGFARII---GEKSF---RRSVVGTPAylapevlrnkgy 182

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258  140 --------LGCILYLLCFRQHPF--EDGAKLRIVNGKYSIPPHDTQYTVFHS--LIRAMLQVNPEERLSIA 198
Cdd:cd14082    183 nrsldmwsVGVIIYVSLSGTFPFneDEDINDQIQNAAFMYPPNPWKEISPDAidLINNLLQVKMRKRYSVD 253
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 73-195 1.73e-04

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: 45.38  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG--------SAT--TISHYPDY------SWSAQRRAl 134
Cdd:cd05595     99 FYgaEIVSALEYLHSRD--VVYRDIKLENLMLDKDGHIKITDFGlckegitdGATmkTFCGTPEYlapevlEDNDYGRA- 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  135 VEEEALGCILY-LLCFRQhPF--EDGAKL--RIVNGKYSIPphDTQYTVFHSLIRAMLQVNPEERL 195
Cdd:cd05595    176 VDWWGLGVVMYeMMCGRL-PFynQDHERLfeLILMEEIRFP--RTLSPEAKSLLAGLLKKDPKQRL 238
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
 64-199 1.73e-04

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: 44.88  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSATTIShyPDYS-----WSAQRRA--L 134
Cdd:cd14114     97 MSEAEVINYMRQVCEGLCHMHENN--IVHLDIKPENIMCTTKRSneVKLIDFGLATHLD--PKESvkvttGTAEFAApeI 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  135 VEEE---------ALGCILYLLCFRQHPF---EDGAKLRIV---------NGKYSIPPHDTQYtvfhslIRAMLQVNPEE 193
Cdd:cd14114    173 VEREpvgfytdmwAVGVLSYVLLSGLSPFageNDDETLRNVkscdwnfddSAFSGISEEAKDF------IRKLLLADPNK 246


                   ....*.
gi 1034639258  194 RLSIAE 199
Cdd:cd14114    247 RMTIHQ 252
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
 62-199 1.88e-04

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: 44.68  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------------SATTIS--------- 120
Cdd:cd06629    103 GKFEEDLVRFFTRQILDGLAYLHSKG--ILHRDLKADNILVDLEGICKISDFGiskksddiygnnGATSMQgsvfwmape 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 --HYPDYSWSAQrralVEEEALGCILYLLCFRQHPFED----GAKLRIVNGKYSIP-PHDTQYT-VFHSLIRAMLQVNPE 192
Cdd:cd06629    181 viHSQGQGYSAK----VDIWSLGCVVLEMLAGRRPWSDdeaiAAMFKLGNKRSAPPvPEDVNLSpEALDFLNACFAIDPR 256


                   ....*..
gi 1034639258  193 ERLSIAE 199
Cdd:cd06629    257 DRPTAAE 263
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 90-114 1.92e-04

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: 44.84  E-value: 1.92e-04
                           10        20
                   ....*....|....*....|....*
gi 1034639258   90 IIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06622    124 IIHRDVKPTNVLVNGNGQVKLCDFG 148
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
 46-114 1.98e-04

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: 44.64  E-value: 1.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   46 LAE-GQLVEFLKKMESRGPLS--CDTVLKIfyqtCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05040     78 LAPlGSLLDRLRKDQGHFLIStlCDYAVQI----ANGMAYLESKR--FIHRDLAARNILLASKDKVKIGDFG 143
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
 47-116 1.98e-04

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: 44.74  E-value: 1.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   47 AEGQLVEFLkkmeSRGPLSCDTVLKIFYQTCRAVQHMH------RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14143     76 EHGSLFDYL----NRYTVTVEGMIKLALSIASGLAHLHmeivgtQGKPAIAHRDLKSKNILVKKNGTCCIADLGLA 147
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 834-1047 2.14e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  834 PLSVQSTPRGGPPAAADPFGPL-LPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSAdflhlgdlpgEP 912
Cdd:pfam05109  425 PESTTTSPTLNTTGFAAPNTTTgLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSP----------SP 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  913 SKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPlfSPGGQPAPCGSQASWTKSQNPDPFADlgDLSSGLQDPQAQST 992
Cdd:pfam05109  495 RDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTP--TPNATSPTLGKTSPTSAVTTPTPNAT--SPTPAVTTPTPNAT 570

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  993 VSPRGQRVCTCSRRLPT-GKLKPGVADTGTAASPHRHC-GSPAGFPPGGFIPKTATT 1047
Cdd:pfam05109  571 IPTLGKTSPTSAVTTPTpNATSPTVGETSPQANTTNHTlGGTSSTPVVTSPPKNATS 627
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 78-223 2.15e-04

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: 44.72  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   78 RAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYS----------WSA----QRRAL---VEEEAL 140
Cdd:cd06654    127 QALEFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQSkrstmvgtpyWMApevvTRKAYgpkVDIWSL 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  141 GCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVV-HQLQEIAaarnvN 214
Cdd:cd06654    203 GIMAIEMIEGEPPYLNENPLRALyliatNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLqHQFLKIA-----K 277


                   ....*....
gi 1034639258  215 PKSPITELL 223
Cdd:cd06654    278 PLSSLTPLI 286
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 90-195 2.36e-04

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: 44.90  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   90 IIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYS-----WSAQRRALVEEEALGCILYLLCFRQHPF 154
Cdd:cd05590    117 IIYRDLKLDNVLLDHEGHCKLADFGmckegifngkTTSTFCGTPDYIapeilQEMLYGPSVDWWAMGVLLYEMLCGHAPF 196

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258  155 ----EDGAKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERL 195
Cdd:cd05590    197 eaenEDDLFEAILNDEVVYPTWLSQDAV--DILKAFMTKNPTMRL 239
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
 46-116 2.52e-04

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: 44.41  E-value: 2.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   46 LAEGQLVEFlkkmesrgplSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07864    105 LLESGLVHF----------SEDHIKSFMKQLLEGLNYCH--KKNFLHRDIKCSNILLNNKGQIKLADFGLA 163
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 50-196 2.57e-04

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: 44.25  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   50 QLV---EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLL---LSNQGTIKLCDFGSA------- 116
Cdd:cd14167     81 QLVsggELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMG--IVHRDLKPENLLyysLDEDSKIMISDFGLSkiegsgs 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  117 --TTISHYPDYSWS---AQR--RALVEEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PPHDTQYTVFHSLI 183
Cdd:cd14167    159 vmSTACGTPGYVAPevlAQKpySKAVDCWSIGVIAYILLCGYPPFydENDAKLfeQILKAEYEFdsPYWDDISDSAKDFI 238

                          170
                   ....*....|...
gi 1034639258  184 RAMLQVNPEERLS 196
Cdd:cd14167    239 QHLMEKDPEKRFT 251
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 53-120 2.68e-04

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: 44.14  E-value: 2.68e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd14110     85 ELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRR--ILHLDLRSENMIITEKNLLKIVDLGNAQPFN 150
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
 75-146 2.79e-04

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: 44.24  E-value: 2.79e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAQRRAlveEEALGCILYL 146
Cdd:cd14150    104 QTAQGMDYLHAKN--IIHRDLKSNNIFLHEGLTVKIGDFGLATVKTR-----WSGSQQV---EQPSGSILWM 165
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
 25-125 2.88e-04

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: 44.11  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   25 QSDFV----GQTVELGELRLR-VRRVLAEGQLVEFLKKMESRgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVEN 99
Cdd:cd05081     63 HSDFIvkyrGVSYGPGRRSLRlVMEYLPSGCLRDFLQRHRAR--LDASRLLLYSSQICKGMEYLGSRR--CVHRDLAARN 138

                           90       100
                   ....*....|....*....|....*.
gi 1034639258  100 LLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05081    139 ILVESEAHVKIADFGLAKLLPLDKDY 164
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
 72-195 3.14e-04

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: 44.60  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDY------SWSAQRRAlV 135
Cdd:cd05615    114 VFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGmckehmvegvTTRTFCGTPDYiapeiiAYQPYGRS-V 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  136 EEEALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERL 195
Cdd:cd05615    193 DWWAYGVLLYEMLAGQPPFdgedEDELFQSIMEHNVSYPKSLSKEAV--SICKGLMTKHPAKRL 254
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
 69-146 3.17e-04

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: 44.28  E-value: 3.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   69 VLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAQRRAlveEEALGCILYL 146
Cdd:cd14151    106 LIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR-----WSGSHQF---EQLSGSILWM 173
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1195-1234 3.44e-04

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 40.17  E-value: 3.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258 1195 PEQVKKHYRRAVLAVHPDK-AAGQPyeQHAKMIFME----LNDAW 1234
Cdd:COG1076     18 DAELKRAYRKLQREHHPDRlAAGLP--EEEQRLALQkaaaINEAY 60
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
 62-120 3.45e-04

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: 43.89  E-value: 3.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06640     96 GPFDEFQIATMLKEILKGLDYLHSEKK--IHRDIKAANVLLSEQGDVKLADFGVAGQLT 152
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 62-194 3.47e-04

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: 43.88  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTI--------SHYPDYSWSAQRRA 133
Cdd:cd06645    103 GPLSESQIAYVSRETLQGLYYLHSKGK--MHRDIKGANILLTDNGHVKLADFGVSAQItatiakrkSFIGTPYWMAPEVA 180

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258  134 LVEEE----------ALGCILYLLCFRQHPFEDGAKLR--IVNGKYSIPPHDTQYTV-----FHSLIRAMLQVNPEER 194
Cdd:cd06645    181 AVERKggynqlcdiwAVGITAIELAELQPPMFDLHPMRalFLMTKSNFQPPKLKDKMkwsnsFHHFVKMALTKNPKKR 258
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
 42-199 3.52e-04

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: 43.84  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSAT 117
Cdd:cd14195     86 ILELVSGGELFDFLAEKES---LTEEEATQFLKQILDGVHYLHSKR--IAHFDLKPENIMLLDKNVpnprIKLIDFGIAH 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  118 TISHYPDYSWSAQRRALVEEE--------------ALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPPHDTQYT 177
Cdd:cd14195    161 KIEAGNEFKNIFGTPEFVAPEivnyeplgleadmwSIGVITYILLSGASPFlgetkqETLTNISAVNYDFDEEYFSNTSE 240

                          170       180
                   ....*....|....*....|..
gi 1034639258  178 VFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd14195    241 LAKDFIRRLLVKDPKKRMTIAQ 262
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 49-115 3.91e-04

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: 44.23  E-value: 3.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   49 GQLVEFLKKMESRGPLScdtvLKIFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGS 115
Cdd:cd05624    157 GDLLTLLSKFEDKLPED----MARFYigEMVLAIHSIHQLH--YVHRDIKPDNVLLDMNGHIRLADFGS 219
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
 51-116 4.44e-04

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: 43.97  E-value: 4.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   51 LVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSA 116
Cdd:cd14224    153 LYELIKKNKFQG-FSLQLVRKFAHSILQCLDALHRNK--IIHCDLKPENILLKQQGRsgIKVIDFGSS 217
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
 72-195 4.53e-04

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: 43.92  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFG--------SATT-------------ISHYPDYSWSaq 130
Cdd:cd05587    100 VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGmckegifgGKTTrtfcgtpdyiapeIIAYQPYGKS-- 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  131 rralVEEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERL 195
Cdd:cd05587    178 ----VDWWAYGVLLYEMLAGQPPFdgEDEDELfqSIMEHNVSYPKSLSKEAV--SICKGLLTKHPAKRL 240
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
 78-120 4.86e-04

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: 43.50  E-value: 4.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258   78 RAVQHMHRQ-------KPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd14054    104 RGLAYLHTDlrrgdqyKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLR 153
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
 49-201 4.96e-04

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: 43.41  E-value: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   49 GQLVEFLKKMESrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSATTISHYPD 124
Cdd:cd14196     93 GELFDFLAQKES---LSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVE 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  125 YSWSAQRRALVEEE--------------ALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPPHDTQYTVFHSLIR 184
Cdd:cd14196    168 FKNIFGTPEFVAPEivnyeplgleadmwSIGVITYILLSGASPFlgdtkqETLANITAVSYDFDEEFFSHTSELAKDFIR 247

                          170
                   ....*....|....*..
gi 1034639258  185 AMLQVNPEERLSIAEVV 201
Cdd:cd14196    248 KLLVKETRKRLTIQEAL 264
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
 62-199 4.99e-04

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: 43.58  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   62 GPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS---------------HYPDYs 126
Cdd:cd06631     98 GALEEPVFCRYTKQILEGVAYLHNNN--VIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCinlssgsqsqllksmRGTPY- 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  127 WSAQRraLVEEE---------ALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPPHDTQYTV-FHSLIRAMLQVNPE 192
Cdd:cd06631    175 WMAPE--VINETghgrksdiwSIGCTVFEMATGKPPWADMNPMAaifaIGSGRKPVPRLPDKFSPeARDFVHACLTRDQD 252


                   ....*..
gi 1034639258  193 ERLSIAE 199
Cdd:cd06631    253 ERPSAEQ 259
pknD PRK13184
serine/threonine-protein kinase PknD;
65-205 5.02e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 44.38  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   65 SCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA-----------------TTISHY----- 122
Cdd:PRK13184   111 SVGAFLSIFHKICATIEYVHSKG--VLHRDLKPDNILLGLFGEVVILDWGAAifkkleeedlldidvdeRNICYSsmtip 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  123 ------PDYswSAQRRAL-------VEEEALGCILYLLCFRQHPF--EDGAKLRIVNGKYS---IPPHDTQYTVFHSLIR 184
Cdd:PRK13184   189 gkivgtPDY--MAPERLLgvpasesTDIYALGVILYQMLTLSFPYrrKKGRKISYRDVILSpieVAPYREIPPFLSQIAM 266

                          170       180
                   ....*....|....*....|..
gi 1034639258  185 AMLQVNPEERL-SIAEVVHQLQ 205
Cdd:PRK13184   267 KALAVDPAERYsSVQELKQDLE 288
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
 42-114 5.12e-04

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: 43.33  E-value: 5.12e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05113     77 ITEYMANGCLLNYLREMRKR--FQTQQLLEMCKDVCEAMEYLESKQ--FLHRDLAARNCLVNDQGVVKVSDFG 145
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 79-195 5.14e-04

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 43.45  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSAT---------------TISHY-PDY---SWSAQRRAlVEEEA 139
Cdd:cd05613    117 ALEHLH--KLGIIYRDIKLENILLDSSGHVVLTDFGLSKeflldeneraysfcgTIEYMaPEIvrgGDSGHDKA-VDWWS 193

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639258  140 LGCILYLLCFRQHPFE-DGAK-------LRIVNgkySIPPHDTQYTVF-HSLIRAMLQVNPEERL 195
Cdd:cd05613    194 LGVLMYELLTGASPFTvDGEKnsqaeisRRILK---SEPPYPQEMSALaKDIIQRLLMKDPKKRL 255
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
 55-114 5.86e-04

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: 43.29  E-value: 5.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   55 LKK-MESRG-----PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFG 114
Cdd:cd07837     91 LKKfIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCHSHG--VMHRDLKPQNLLVDKQkGLLKIADLG 155
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
 46-125 5.95e-04

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: 43.38  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKmeSRGPLSCDTVLKIFYQTCRAVQHM-HRQkppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD 124
Cdd:cd05079     90 LPSGSLKEYLPR--NKNKINLKQQLKYAVQICKGMDYLgSRQ---YVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 164


                   .
gi 1034639258  125 Y 125
Cdd:cd05079    165 Y 165
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
 49-114 6.27e-04

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: 43.07  E-value: 6.27e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   49 GQLVEFLKKMESRGpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd06636    104 GSVTDLVKNTKGNA-LKEDWIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENAEVKLVDFG 166
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 51-114 6.98e-04

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: 41.27  E-value: 6.98e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   51 LVEFLKKMESRGPLSCDT-----VLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd13968     70 LMELVKGGTLIAYTQEEEldekdVESIMYQLAECMRLLHSFH--LIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 53-196 7.38e-04

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: 42.96  E-value: 7.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   53 EFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLL-----------LSNQGTIKLCDFGSATTISH 121
Cdd:cd14169     87 ELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLG--IVHRDLKPENLLyatpfedskimISDFGLSKIEAQGMLSTACG 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  122 YPDYSWSA--QRRAL---VEEEALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PPHDTQYTVFHSLIRAMLQVN 190
Cdd:cd14169    165 TPGYVAPEllEQKPYgkaVDVWAIGVISYILLCGYPPFydENDSELfnQILKAEYEFdsPYWDDISESAKDFIRHLLERD 244


                   ....*.
gi 1034639258  191 PEERLS 196
Cdd:cd14169    245 PEKRFT 250
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 79-114 7.46e-04

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 43.37  E-value: 7.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034639258   79 AVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05614    117 ALEHLH--KLGIVYRDIKLENILLDSEGHVVLTDFG 150
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
 79-114 7.49e-04

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: 43.33  E-value: 7.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034639258   79 AVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05585    106 ALECLH--KFNVIYRDLKPENILLDYTGHIALCDFG 139
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 85-175 7.55e-04

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: 43.11  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   85 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEALGCILYLlcfRQHPFEDGAKL-RIV 163
Cdd:cd06649    120 REKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSV---QSDIWSMGLSLvELA 196

                           90
                   ....*....|..
gi 1034639258  164 NGKYSIPPHDTQ 175
Cdd:cd06649    197 IGRYPIPPPDAK 208
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
 29-117 7.70e-04

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: 42.87  E-value: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   29 VGQTVELGELRLrVRRVLAEGQLVEFLKKMESrgPLSCDTvlKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTI 108
Cdd:cd14027     57 LGVILEEGKYSL-VMEYMEKGNLMHVLKKVSV--PLSVKG--RIILEIIEGMAYLHGKG--VIHKDLKPENILVDNDFHI 129


                   ....*....
gi 1034639258  109 KLCDFGSAT 117
Cdd:cd14027    130 KIADLGLAS 138
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
 46-125 8.17e-04

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: 42.75  E-value: 8.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKMESRgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY 125
Cdd:cd05038     90 LPSGSLRDYLQRHRDQ--IDLKRLLLFASQICKGMEYLGSQR--YIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEY 165
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 53-116 8.50e-04

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: 42.58  E-value: 8.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   53 EFLKKMESRgPLSCDT-VLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSA 116
Cdd:cd14108     83 ELLERITKR-PTVCESeVRSYMRQLLEGIEYLHQND--VLHLDLKPENLLMADQKTdqVRICDFGNA 146
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 42-201 8.54e-04

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: 42.54  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKmesRGPLSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSN-------QGTIKLCDFG 114
Cdd:cd14097     78 VMELCEDGELKELLLR---KGFFSENETRHIIQSLASAVAYLH--KNDIVHRDLKLENILVKSsiidnndKLNIKVTDFG 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  115 SA----------------TTISHYP------DYS-----WSaqrralveeeaLGCILYLLCFRQHPFEDGAKLRIVNgky 167
Cdd:cd14097    153 LSvqkyglgedmlqetcgTPIYMAPevisahGYSqqcdiWS-----------IGVIMYMLLCGEPPFVAKSEEKLFE--- 218

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034639258  168 SIPPHDTQYT--VFHSL-------IRAMLQVNPEERLSIAEVV 201
Cdd:cd14097    219 EIRKGDLTFTqsVWQSVsdaaknvLQQLLKVDPAHRMTASELL 261
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
 51-120 8.61e-04

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: 43.12  E-value: 8.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKmesrgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06635    114 LLEVHKK-----PLQEIEIAAITHGALQGLAYLHSHN--MIHRDIKAGNILLTEPGQVKLADFGSASIAS 176
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
 47-125 8.63e-04

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: 43.09  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   47 AEGQLVEFLKKMESRG-------------PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDF 113
Cdd:cd05100    101 SKGNLREYLRARRPPGmdysfdtcklpeeQLTFKDLVSCAYQVARGMEYLASQK--CIHRDLAARNVLVTEDNVMKIADF 178

                           90
                   ....*....|..
gi 1034639258  114 GSATTIsHYPDY 125
Cdd:cd05100    179 GLARDV-HNIDY 189
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
 55-116 9.32e-04

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 42.63  E-value: 9.32e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258   55 LKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGSA 116
Cdd:cd14017     85 LRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVG--FLHRDVKPSNFAIgrgpSDERTVYILDFGLA 148
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 843-1038 1.08e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  843 GGPPAAADPFGPLLPSSGNNSQPCSNPDlfgeflnSDSVTVPPSFPSAHSAP-PPSCSADFLHLGDLPGEPSKMTASSSN 921
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPA-------APAAPAAPAAPAPAGAAaAPAEASAAPAPGVAAPEHHPKHVAVPD 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  922 P-DLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPdpfadlGDLSSGLQDPQAQSTVSPRgQRV 1000
Cdd:PRK07764   662 AsDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG------QADDPAAQPPQAAQGASAP-SPA 734

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034639258 1001 CTCSRRLPTGKLKPGVADTGTAASPHRHCGSPAGFPPG 1038
Cdd:PRK07764   735 ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
 67-116 1.09e-03

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: 42.21  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   67 DTVLKIfYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSA 116
Cdd:cd14193    103 DTILFI-KQICEGIQYMHQMY--ILHLDLKPENILCVSREAnqVKIIDFGLA 151
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
782-964 1.17e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  782 GAGPAVPPQACKAPSSNTdllscllGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPfgpllPSSGN 861
Cdd:PRK07003   370 GGVPARVAGAVPAPGARA-------AAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAP-----PATAD 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  862 NSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAP 941
Cdd:PRK07003   438 RGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517

                          170       180
                   ....*....|....*....|...
gi 1034639258  942 TPATEGPLFSPGGQPAPCGSQAS 964
Cdd:PRK07003   518 REDAPAAAAPPAPEARPPTPAAA 540
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
 63-116 1.29e-03

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: 42.67  E-value: 1.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07851    114 KLSDDHIQFLVYQILRGLKYIHSAG--IIHRDLKPSNLAVNEDCELKILDFGLA 165
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 49-115 1.30e-03

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: 42.33  E-value: 1.30e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258   49 GQLVEFLKKMESRGPLScdtvLKIFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGS 115
Cdd:cd05597     86 GDLLTLLSKFEDRLPEE----MARFYlaEMVLAIDSIHQLG--YVHRDIKPDNVLLDRNGHIRLADFGS 148
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
 74-199 1.38e-03

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 42.11  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   74 YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQgTIKLCDFGSATTISHYPDYSWSAQRRALVEEE--------------A 139
Cdd:cd14109    106 RQLLLALKHMHDLG--IAHLDLRPEDILLQDD-KLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEivnsypvtlatdmwS 182

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258  140 LGCILYLLCFRQHPF---EDGAKLR-IVNGKYSIppHDTQYTVFHS----LIRAMLQVNPEERLSIAE 199
Cdd:cd14109    183 VGVLTYVLLGGISPFlgdNDRETLTnVRSGKWSF--DSSPLGNISDdardFIKKLLVYIPESRLTVDE 248
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 75-207 1.45e-03

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: 41.94  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   75 QTCRAVQHMHRQK-PPIIHRDLKVENLLLSNQG--------TIKLCDFGSA------TTISHYPDYSWSAQR-------R 132
Cdd:cd14147    109 QIARGMHYLHCEAlVPVIHRDLKSNNILLLQPIenddmehkTLKITDFGLArewhktTQMSAAGTYAWMAPEvikastfS 188

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639258  133 ALVEEEALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEI 207
Cdd:cd14147    189 KGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGvavnKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
 49-116 1.46e-03

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: 42.34  E-value: 1.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   49 GQLVEFLKKMEsrgpLSCDTVLKIFYQTCRAVQHMHRQ------KPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14219     88 GSLYDYLKSTT----LDTKAMLKLAYSSVSGLCHLHTEifstqgKPAIAHRDLKSKNILVKKNGTCCIADLGLA 157
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
 42-129 1.48e-03

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: 41.78  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKmESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISH 121
Cdd:cd05083     76 VMELMSKGNLVNFLRS-RGRALVPVIQLLQFSLDVAEGMEYLESKK--LVHRDLAARNILVSEDGVAKISDFGLAKVGSM 152

                           90
                   ....*....|...
gi 1034639258  122 YPDYS-----WSA 129
Cdd:cd05083    153 GVDNSrlpvkWTA 165
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
 74-116 1.53e-03

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: 42.46  E-value: 1.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1034639258   74 YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07859    110 YQLLRALKYIHTAN--VFHRDLKPKNILANADCKLKICDFGLA 150
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 63-116 1.54e-03

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: 42.17  E-value: 1.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07856    104 PLEKQFIQYFLYQILRGLKYVHSAG--VIHRDLKPSNILVNENCDLKICDFGLA 155
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
 73-195 1.58e-03

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 42.36  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FYQT--CRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEE------------ 138
Cdd:cd05633    112 FYATeiILGLEHMHNRF--VVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVlqkgtaydssad 189

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258  139 --ALGCILYLLC-----FRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERL 195
Cdd:cd05633    190 wfSLGCMLFKLLrghspFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRL 253
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
 69-146 1.63e-03

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: 41.94  E-value: 1.63e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   69 VLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAQRRAlveEEALGCILYL 146
Cdd:cd14149    110 LIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR-----WSGSQQV---EQPTGSILWM 177
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
 42-133 1.63e-03

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: 41.80  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   42 VRRVLAEGQLVEFLKKMESRgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISh 121
Cdd:cd05067     79 ITEYMENGSLVDFLKTPSGI-KLTINKLLDMAAQIAEGMAFIEERN--YIHRDLRAANILVSDTLSCKIADFGLARLIE- 154

                           90
                   ....*....|..
gi 1034639258  122 ypDYSWSAQRRA 133
Cdd:cd05067    155 --DNEYTAREGA 164
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
 46-129 1.65e-03

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: 41.86  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   46 LAEGQLVEFLKKmeSRGPLSCDTVLKIFYQTCRAVQHMhrQKPPIIHRDLKVENLLLSNQGTIKLCDFG----------S 115
Cdd:cd05112     81 MEHGCLSDYLRT--QRGLFSAETLLGMCLDVCEGMAYL--EEASVIHRDLAARNCLVGENQVVKVSDFGmtrfvlddqyT 156

                           90
                   ....*....|....
gi 1034639258  116 ATTISHYPdYSWSA 129
Cdd:cd05112    157 SSTGTKFP-VKWSS 169
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
 74-118 1.73e-03

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: 42.02  E-value: 1.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258   74 YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT 118
Cdd:cd07850    109 YQMLCGIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLART 151
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
 72-203 1.75e-03

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: 41.90  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGSATTISHyPDYSWSAQRRALVEE---------- 137
Cdd:cd14183    109 MLYNLASAIKYLHSLN--IVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDG-PLYTVCGTPTYVAPEiiaetgyglk 185

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258  138 ---EALGCILYLLCFRQHPF----EDGAKL--RIVNGKYSIP-PH-DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ 203
Cdd:cd14183    186 vdiWAAGVITYILLCGFPPFrgsgDDQEVLfdQILMGQVDFPsPYwDNVSDSAKELITMMLQVDVDQRYSALQVLEH 262
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
 72-114 1.77e-03

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 41.97  E-value: 1.77e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034639258   72 IFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQ---GTIKLCDFG 114
Cdd:cd14041    116 IIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGtacGEIKITDFG 161
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
 36-136 1.82e-03

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: 41.92  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   36 GELR--LRVRRVLaeGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDF 113
Cdd:cd05101    115 GNLReyLRARRPP--GMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQK--CIHRDLAARNVLVTENNVMKIADF 190

                           90       100
                   ....*....|....*....|...
gi 1034639258  114 GSATTISHYPDYSWSAQRRALVE 136
Cdd:cd05101    191 GLARDINNIDYYKKTTNGRLPVK 213
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
 49-116 1.84e-03

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: 41.95  E-value: 1.84e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   49 GQLVEFLKKMEsrgpLSCDTVLKIFYQTCRAVQHMHRQ------KPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14220     78 GSLYDFLKCTT----LDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGTCCIADLGLA 147
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
 62-116 1.97e-03

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: 41.62  E-value: 1.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639258   62 GPLSCDTVLKIFY--QTCRAVQHMHRQKppIIHRDLKVENLLLSN-QGTIKLCDFGSA 116
Cdd:cd06624    101 GPLKDNENTIGYYtkQILEGLKYLHDNK--IVHRDIKGDNVLVNTySGVVKISDFGTS 156
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
 80-154 1.99e-03

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: 41.83  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   80 VQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYS-----WSAQRRALVEEEALGCIL 144
Cdd:cd05619    119 LQFLHSKG--IVYRDLKLDNILLDKDGHIKIADFGmckenmlgdaKTSTFCGTPDYIapeilLGQKYNTSVDWWSFGVLL 196

                           90
                   ....*....|
gi 1034639258  145 YLLCFRQHPF 154
Cdd:cd05619    197 YEMLIGQSPF 206
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
 78-119 1.99e-03

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: 41.63  E-value: 1.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034639258   78 RAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI 119
Cdd:cd06637    122 RGLSHLHQHK--VIHRDIKGQNVLLTENAEVKLVDFGVSAQL 161
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
 45-199 2.05e-03

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: 41.70  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   45 VLAEGQLVEFLKKMESrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSATTIS 120
Cdd:cd14105     89 LVAGGELFDFLAEKES---LSEEEATEFLKQILDGVNYLHTKN--IAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIE 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  121 HYPDYSWSAQRRALVEEE--------------ALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIpphDTQY-----T 177
Cdd:cd14105    164 DGNEFKNIFGTPEFVAPEivnyeplgleadmwSIGVITYILLSGASPFLGDTKqetlANITAVNYDF---DDEYfsntsE 240

                          170       180
                   ....*....|....*....|..
gi 1034639258  178 VFHSLIRAMLQVNPEERLSIAE 199
Cdd:cd14105    241 LAKDFIRQLLVKDPRKRMTIQE 262
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
 51-120 2.07e-03

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: 41.93  E-value: 2.07e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   51 LVEFLKKmesrgPLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06634    104 LLEVHKK-----PLQEVEIAAITHGALQGLAYLHSHN--MIHRDVKAGNILLTEPGLVKLGDFGSASIMA 166
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
 38-114 2.17e-03

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: 41.54  E-value: 2.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   38 LRLrVRRVLAEGQLVEFLKKMESRgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd14205     82 LRL-IMEYLPYGSLRDYLQKHKER--IDHIKLLQYTSQICKGMEYLGTKR--YIHRDLATRNILVENENRVKIGDFG 153
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
 73-195 2.24e-03

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: 41.64  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   73 FY--QTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGS---------------------ATTISHYPDYSWSa 129
Cdd:cd05588    100 FYsaEISLALNFLHEKG--IIYRDLKLDNVLLDSEGHIKLTDYGMckeglrpgdttstfcgtpnyiAPEILRGEDYGFS- 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  130 qrralVEEEALGCILYLLCFRQHPFEdgaklriVNGKYSIPPHDTQYTVFH------------------SLIRAMLQVNP 191
Cdd:cd05588    177 -----VDWWALGVLMFEMLAGRSPFD-------IVGSSDNPDQNTEDYLFQvilekpiriprslsvkaaSVLKGFLNKNP 244


                   ....
gi 1034639258  192 EERL 195
Cdd:cd05588    245 AERL 248
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
 64-136 2.35e-03

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: 41.54  E-value: 2.35e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVE 136
Cdd:cd05098    132 LSSKDLVSCAYQVARGMEYLASKK--CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVK 202
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 78-223 2.43e-03

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: 41.63  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   78 RAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYS----------WSA----QRRAL---VEEEAL 140
Cdd:cd06655    126 QALEFLHANQ--VIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT--PEQSkrstmvgtpyWMApevvTRKAYgpkVDIWSL 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  141 GCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVV-HQLQEIAaarnvN 214
Cdd:cd06655    202 GIMAIEMVEGEPPYLNENPLRALyliatNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLqHPFLKLA-----K 276


                   ....*....
gi 1034639258  215 PKSPITELL 223
Cdd:cd06655    277 PLSSLTPLI 285
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 90-119 2.47e-03

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: 41.40  E-value: 2.47e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034639258   90 IIHRDLKVENLLLSNQGTIKLCDFGSATTI 119
Cdd:cd06619    116 ILHRDVKPSNMLVNTRGQVKLCDFGVSTQL 145
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
 79-195 2.59e-03

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 41.57  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEE--------------ALGCIL 144
Cdd:cd14223    115 GLEHMHSRF--VVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVlqkgvaydssadwfSLGCML 192

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639258  145 YLLC-----FRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERL 195
Cdd:cd14223    193 FKLLrghspFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRL 248
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 71-127 2.60e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 39.94  E-value: 2.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639258   71 KIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGtIKLCDFGSATTISHYPDYSW 127
Cdd:COG3642     55 ELLRELGRLLARLHRAG--IVHGDLTTSNILVDDGG-VYLIDFGLARYSDPLEDKAV 108
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
 64-116 2.74e-03

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: 41.56  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034639258   64 LSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07877    117 LTDDHVQFLIYQILRGLKYIHSAD--IIHRDLKPSNLAVNEDCELKILDFGLA 167
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
 63-116 2.77e-03

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: 41.43  E-value: 2.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHrqKPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07879    113 PLSEDKVQYLVYQMLCGLKYIH--SAGIIHRDLKPGNLAVNEDCELKILDFGLA 164
PHA03247 PHA03247
large tegument protein UL36; Provisional
 694-1032 2.88e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  694 AETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPR-ADPEPPGLAAGLVQQDLvfeveTPAVLPEPVPQEDGV 772
Cdd:PHA03247  2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPP-----PPGPPPPSLPLGGSV 2856

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  773 DLLGLHSEVG------AGPAVPPQ------ACKAPSSNTDLLSclLGPPEAASQGPPEdlLSEDPLllasPAPPLSVQST 840
Cdd:PHA03247  2857 APGGDVRRRPpsrspaAKPAAPARppvrrlARPAVSRSTESFA--LPPDQPERPPQPQ--APPPPQ----PQPQPPPPPQ 2928

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  841 PRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSdsvTVPPSFPSAHSAPPPScsadflhlgdlpgEPSKMTASSS 920
Cdd:PHA03247  2929 PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA---LVPGRVAVPRFRVPQP-------------APSREAPASS 2992

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  921 NPDLLGGWAAWTETAASAVAPTPATEGPLFSPggqpapcgSQASWTKSQNPDP------FADLGDLSSGLQDPQAQSTVS 994
Cdd:PHA03247  2993 TPPLTGHSLSRVSSWASSLALHEETDPPPVSL--------KQTLWPPDDTEDSdadslfDSDSERSDLEALDPLPPEPHD 3064

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1034639258  995 PrgqrvctcsrrlPTGKLKPGVADTGTAASPHRHCGSP 1032
Cdd:PHA03247  3065 P------------FAHEPDPATPEAGARESPSSQFGPP 3090
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
 49-119 2.92e-03

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: 41.04  E-value: 2.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639258   49 GQLVEFLKKMEsrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTI 119
Cdd:cd05080     93 GSLRDYLPKHS----IGLAQLLLFAQQICEGMAYLHSQH--YIHRDLAARNVLLDNDRLVKIGDFGLAKAV 157
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
 73-116 3.08e-03

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 40.67  E-value: 3.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034639258   73 FYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSA 116
Cdd:cd14019    107 LRNLFKALKHVHSFG--IIHRDVKPGNFLYNREtGKGVLVDFGLA 149
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
 72-120 3.19e-03

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: 41.17  E-value: 3.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd07876    128 LLYQMLCGIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLARTAC 174
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
 75-116 3.28e-03

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: 40.72  E-value: 3.28e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034639258   75 QTCRAVQHMHRQKppIIHRDLKVENLLLSNQ--GTIKLCDFGSA 116
Cdd:cd14192    110 QICEGVHYLHQHY--ILHLDLKPENILCVNStgNQIKIIDFGLA 151
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
 63-116 3.33e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 41.42  E-value: 3.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   63 PLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:PHA03211   256 PLGLAQVTAVARQLLSAIDYIHGEG--IIHRDIKTENVLVNGPEDICLGDFGAA 307
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1195-1234 4.03e-03

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 37.78  E-value: 4.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034639258 1195 PEQVKKHYRRAVLAVHPDKAAGQPyeQHAKMIFMELNDAW 1234
Cdd:COG2214     19 LEEIRQAYRRLAKLLHPDRGGELK--ALAEELFQRLNEAY 56
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
 78-120 4.23e-03

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: 40.79  E-value: 4.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1034639258   78 RAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS 120
Cdd:cd06658    129 RALSYLHNQG--VIHRDIKSDSILLTSDGRIKLSDFGFCAQVS 169
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
 55-116 4.33e-03

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: 40.71  E-value: 4.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639258   55 LKKMESrgpLSCDTVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd07880    109 LMKHEK---LSEDRIQFLVYQMLKGLKYIHAAG--IIHRDLKPGNLAVNEDCELKILDFGLA 165
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
 19-114 5.38e-03

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: 40.21  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   19 GASGRDQSDF--VGQTVELGELrlrvrrvlaegqlveFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLK 96
Cdd:cd14064     58 GACLDDPSQFaiVTQYVSGGSL---------------FSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNLTQPIIHRDLN 122

                           90
                   ....*....|....*...
gi 1034639258   97 VENLLLSNQGTIKLCDFG 114
Cdd:cd14064    123 SHNILLYEDGHAVVADFG 140
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
 79-195 5.51e-03

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: 40.40  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258   79 AVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFG----------SATTISHYPDYSWSAQRRA-----LVEEEALGCI 143
Cdd:cd05618    133 ALNYLHERG--IIYRDLKLDNVLLDSEGHIKLTDYGmckeglrpgdTTSTFCGTPNYIAPEILRGedygfSVDWWALGVL 210

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  144 LYLLCFRQHPFEdgaklriVNGKYSIPPHDTQYTVFH------------------SLIRAMLQVNPEERL 195
Cdd:cd05618    211 MFEMMAGRSPFD-------IVGSSDNPDQNTEDYLFQvilekqiriprslsvkaaSVLKSFLNKDPKERL 273
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
 68-116 5.84e-03

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 40.50  E-value: 5.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034639258   68 TVLKIFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSA 116
Cdd:cd14013    121 IIKSIMRQILVALRKLHSTG--IVHRDVKPQNIIVSEGdGQFKIIDLGAA 168
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
 49-116 6.02e-03

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: 40.15  E-value: 6.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   49 GQLVEFLKKMEsrgpLSCDTVLKIFYQTCRAVQHMHRQ------KPPIIHRDLKVENLLLSNQGTIKLCDFGSA 116
Cdd:cd14144     78 GSLYDFLRGNT----LDTQSMLKLAYSAACGLAHLHTEifgtqgKPAIAHRDIKSKNILVKKNGTCCIADLGLA 147
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
 72-114 6.30e-03

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 40.04  E-value: 6.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034639258   72 IFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQ---GTIKLCDFG 114
Cdd:cd14040    116 IVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGtacGEIKITDFG 161
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 759-1103 6.42e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 6.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  759 PAVLPEPVPQEDGVDLLGLH-SEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSV 837
Cdd:PHA03307    24 PPATPGDAADDLLSGSQGQLvSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  838 QS------TPRGGPPAAADPFGPLlPSSGNNSQPcsnpdlfgeflnsDSVTVPPSFPSAHSAPPPScsadflhlGDLPGE 911
Cdd:PHA03307   104 GSptppgpSSPDPPPPTPPPASPP-PSPAPDLSE-------------MLRPVGSPGPPPAASPPAA--------GASPAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  912 PSKMTASSSNPDLLggwAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDlSSGLQDPQAQS 991
Cdd:PHA03307   162 VASDAASSRQAALP---LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR-SAADDAGASSS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  992 TVSPRGQRVCTCSRRLPTGKLKPGVADTGTA-ASPHRHCGSPAGFPPGgfiPKTATTPKGSSSWQTSRPpaqgaswppqa 1070
Cdd:PHA03307   238 DSSSSESSGCGWGPENECPLPRPAPITLPTRiWEASGWNGPSSRPGPA---SSSSSPRERSPSPSPSSP----------- 303

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1034639258 1071 kpppkaCTQPRPNYASNFSVIGAREERGVRAPS 1103
Cdd:PHA03307   304 ------GSGPAPSSPRASSSSSSSRESSSSSTS 330
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
 72-118 6.81e-03

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: 40.46  E-value: 6.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT 118
Cdd:cd07874    124 LLYQMLCGIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLART 168
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
 56-116 7.19e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 39.80  E-value: 7.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639258   56 KKMESRGPLSCD-TVLKIF-YQTCRAVQHMHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSA 116
Cdd:PLN00009    89 KHMDSSPDFAKNpRLIKTYlYQILRGIAYCHSHR--VLHRDLKPQNLLIDRRtNALKLADFGLA 150
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
 72-118 8.43e-03

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: 40.03  E-value: 8.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639258   72 IFYQTCRAVQHMHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT 118
Cdd:cd07875    131 LLYQMLCGIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLART 175
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
 73-114 8.68e-03

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: 40.01  E-value: 8.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034639258   73 FY--QTCRAVQHMHRQKPpIIHRDLKVENLLLSNQGTIKLCDFG 114
Cdd:cd05594    129 FYgaEIVSALDYLHSEKN-VVYRDLKLENLMLDKDGHIKITDFG 171
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 600-854 8.94e-03

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 40.33  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  600 VEPRDRPSREAPPWENSSMRGLNPKILFSSReeqqdilskfgkPELPRQPGSTAQY--DAGAGSPEAEPTDSDSPPSSSa 677
Cdd:PHA03321   458 RRARAQRARDAGPEYVDPLGALRRLPAGAAP------------PPEPAAAPSPATYytRMGGGPPRLPPRNRATETLRP- 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  678 dasrflhtlDWQEEKEAEtgaenaSSKESESALMEDRDESEVSDEGGSPISSEGQE-PRADPEPPGLAAGLVQQDLVFEV 756
Cdd:PHA03321   525 ---------DWGPPAAAP------PEQMEDPYLEPDDDRFDRRDGAAAAATSHPREaPAPDDDPIYEGVSDSEEPVYEEI 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639258  757 ETPAVLPEPVPQedgvdllglhSEVGAGPAVPPQACKAPSSNTDLL------SCLLGPPEAASQGPPEdllsedplLLAS 830
Cdd:PHA03321   590 PTPRVYQNPLPR----------PMEGAGEPPDLDAPTSPWVEEENPiygwgdSPLFSPPPAARFPPPD--------PALS 651

                          250       260
                   ....*....|....*....|....
gi 1034639258  831 PAPPLSVQSTPRggpPAAADPFGP 854
Cdd:PHA03321   652 PEPPALPAHRPR---PGALAPDGP 672
 
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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