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Conserved domains on  [gi|2462596344|ref|XP_054205591|]
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cyclin-G-associated kinase isoform X42 [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 ...
 176-338 3.41e-123

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: 374.62  E-value: 3.41e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  176 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 255
Cdd:cd14564      1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  256 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 335
Cdd:cd14564     81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                   ...
gi 2462596344  336 CDM 338
Cdd:cd14564    161 CDM 163
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 1-96 8.52e-62

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: 212.37  E-value: 8.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERL 80
Cdd:cd14036    187 MYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERL 266

                           90
                   ....*....|....*.
gi 2462596344   81 SIAEVVHQLQEIAAAR 96
Cdd:cd14036    267 SITEIVEQLQELAAAR 282
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 346-484 1.36e-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: 1.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  346 PHSKPILVRAVVMTPVPLFsKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARS 425
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596344  426 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 484
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 ...
 1080-1124 2.47e-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: 48.31  E-value: 2.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462596344 1080 PEQVKRHYRRAVLAVHPDKAAGQPYeqhAKMIFMELNDAWSEFEN 1124
Cdd:cd06257     14 DEEIKKAYRKLALKYHPDKNPDDPE---AEEKFKEINEAYEVLSD 55
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 584-965 9.07e-07

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 9.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  584 ENASSKESESALMEDRDESEVSDEG----GSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQ-----E 654
Cdd:pfam03154  140 DNRSTSPSIPSPQDNESDSDSSAQQqilqTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAtsqppN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  655 DGVDLLGLHSEVGAGPAVPPQACKAPSSntdllscllgPPEAASQGPPEDLLSEDPL---LLASPAPPL--SVQSTPRGG 729
Cdd:pfam03154  220 QTQSTAAPHTLIQQTPTLHPQRLPSPHP----------PLQPMTQPPPPSQVSPQPLpqpSLHGQMPPMphSLQTGPSHM 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  730 P-PAAADPFGPLLPSSGNNSQPCSNPDLFGEflNSDSVTVPPSFPSAHSAPPPS------CSADFLHLGDLPGEP-SKMT 801
Cdd:pfam03154  290 QhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ--SQQRIHTPPSQSQLQSQQPPReqplppAPLSMPHIKPPPTTPiPQLP 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  802 ASSSN--PDLLGGWAAWTetAASAVAPTPATEgPLFSPGGQPAPcgsqaswtkSQNPDPFaDLGDLSSGLQDPQAQSTVS 879
Cdd:pfam03154  368 NPQSHkhPPHLSGPSPFQ--MNSNLPPPPALK-PLSSLSTHHPP---------SAHPPPL-QLMPQSQQLPPPPAQPPVL 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  880 PRGQRVCTCSRRLPTgklkPGVADTGTAASPhrhcgspagFPPGGFIPKTATT--------PKGSSSWQTSRPPAQGASW 951
Cdd:pfam03154  435 TQSQSLPPPAASHPP----TSGLHQVPSQSP---------FPQHPFVPGGPPPitppsgppTSTSSAMPGIQPPSSASVS 501

                          410
                   ....*....|....
gi 2462596344  952 PPQAKPPPKACTQP 965
Cdd:pfam03154  502 SSGPVPAAVSCPLP 515
 
Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 176-338 3.41e-123

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: 374.62  E-value: 3.41e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  176 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 255
Cdd:cd14564      1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  256 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 335
Cdd:cd14564     81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                   ...
gi 2462596344  336 CDM 338
Cdd:cd14564    161 CDM 163
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 1-96 8.52e-62

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: 212.37  E-value: 8.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERL 80
Cdd:cd14036    187 MYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERL 266

                           90
                   ....*....|....*.
gi 2462596344   81 SIAEVVHQLQEIAAAR 96
Cdd:cd14036    267 SITEIVEQLQELAAAR 282
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 346-484 1.36e-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: 1.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  346 PHSKPILVRAVVMTPVPLFsKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARS 425
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596344  426 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 484
Cdd:pfam10409   80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 2-85 2.42e-15

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 77.18  E-value: 2.42e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344     2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKL-----RIVNGKYSIPPHDTQYTV-FHSLIRAMLQVN 75
Cdd:smart00220  162 YMAPEVL---LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlelfkKIGKPKPPFPPPEWDISPeAKDLIRKLLVKD 238

                            90
                    ....*....|
gi 2462596344    76 PEERLSIAEV 85
Cdd:smart00220  239 PEKRLTAEEA 248
Pkinase pfam00069
Protein kinase domain;
2-87 8.04e-13

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 68.81  E-value: 8.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPPHDtqYTV---FHSLIRAMLQV 74
Cdd:pfam00069  126 YMAPEVL---GGNPYGPKVDVWSLGCILYELLTGKPPFpginGNEIYELIIDQPYAFPELP--SNLseeAKDLLKKLLKK 200

                           90
                   ....*....|...
gi 2462596344   75 NPEERLSIAEVVH 87
Cdd:pfam00069  201 DPSKRLTATQALQ 213
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1080-1124 2.47e-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: 48.31  E-value: 2.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462596344 1080 PEQVKRHYRRAVLAVHPDKAAGQPYeqhAKMIFMELNDAWSEFEN 1124
Cdd:cd06257     14 DEEIKKAYRKLALKYHPDKNPDDPE---AEEKFKEINEAYEVLSD 55
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 584-965 9.07e-07

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: 53.23  E-value: 9.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  584 ENASSKESESALMEDRDESEVSDEG----GSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQ-----E 654
Cdd:pfam03154  140 DNRSTSPSIPSPQDNESDSDSSAQQqilqTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAtsqppN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  655 DGVDLLGLHSEVGAGPAVPPQACKAPSSntdllscllgPPEAASQGPPEDLLSEDPL---LLASPAPPL--SVQSTPRGG 729
Cdd:pfam03154  220 QTQSTAAPHTLIQQTPTLHPQRLPSPHP----------PLQPMTQPPPPSQVSPQPLpqpSLHGQMPPMphSLQTGPSHM 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  730 P-PAAADPFGPLLPSSGNNSQPCSNPDLFGEflNSDSVTVPPSFPSAHSAPPPS------CSADFLHLGDLPGEP-SKMT 801
Cdd:pfam03154  290 QhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ--SQQRIHTPPSQSQLQSQQPPReqplppAPLSMPHIKPPPTTPiPQLP 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  802 ASSSN--PDLLGGWAAWTetAASAVAPTPATEgPLFSPGGQPAPcgsqaswtkSQNPDPFaDLGDLSSGLQDPQAQSTVS 879
Cdd:pfam03154  368 NPQSHkhPPHLSGPSPFQ--MNSNLPPPPALK-PLSSLSTHHPP---------SAHPPPL-QLMPQSQQLPPPPAQPPVL 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  880 PRGQRVCTCSRRLPTgklkPGVADTGTAASPhrhcgspagFPPGGFIPKTATT--------PKGSSSWQTSRPPAQGASW 951
Cdd:pfam03154  435 TQSQSLPPPAASHPP----TSGLHQVPSQSP---------FPQHPFVPGGPPPitppsgppTSTSSAMPGIQPPSSASVS 501

                          410
                   ....*....|....
gi 2462596344  952 PPQAKPPPKACTQP 965
Cdd:pfam03154  502 SSGPVPAAVSCPLP 515
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1080-1125 4.29e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 44.92  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2462596344  1080 PEQVKRHYRRAVLAVHPDKAAGQPYEqhAKMIFMELNDAWSEFENQ 1125
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-141 1.58e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 48.86  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   21 DIWALGCILYLLCFRQHPFE---DGAKLRIVNGKYSIPPHDTQYTV---FHSLIRAMLQVNPEERL-SIAEVVHQLQEIA 93
Cdd:COG0515    190 DVYSLGVTLYELLTGRPPFDgdsPAELLRAHLREPPPPPSELRPDLppaLDAIVLRALAKDPEERYqSAAELAAALRAVL 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462596344   94 AARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALA 141
Cdd:COG0515    270 RSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 317
PHA03247 PHA03247
large tegument protein UL36; Provisional
 615-945 1.90e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  615 EGQEPRADPEPPGLAAGLVQQdlvfevETPAVLPEPVPqedgvdllglHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPP 694
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP------PPPPPTPEPAP----------HALVSATPLPPGPAAARQASPALPAAPAPPAV 2744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  695 EAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPS 774
Cdd:PHA03247  2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  775 AHSAPPPSCSAdflhlgdlPGEPSKMTASSSNPDLLGGWAAwtetAASAVAPTPATEGPLFSPGGQPAPCGSQ-ASWTKS 853
Cdd:PHA03247  2825 AGPLPPPTSAQ--------PTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS 2892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  854 QNPDPFADLGDLSSGLQDPQAQS----TVSPRGQRVCTCSRRLPTGKLKPGVADTGTAASPHRHCGSPA----GFPPGGF 925
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgALVPGRV 2972

                          330       340
                   ....*....|....*....|
gi 2462596344  926 IPKTATTPKGSSSWQTSRPP 945
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAPASS 2992
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1080-1119 1.75e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 40.94  E-value: 1.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462596344 1080 PEQVKRHYRRAVLAVHPDK-AAGQPyeQHAKMIFME----LNDAW 1119
Cdd:COG1076     18 DAELKRAYRKLQREHHPDRlAAGLP--EEEQRLALQkaaaINEAY 60
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1081-1120 1.91e-04

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: 40.53  E-value: 1.91e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462596344 1081 EQVKRHYRRAVLAVHPDKAAGQPyeqHAKMIFMELNDAWS 1120
Cdd:pfam00226   15 EEIKKAYRKLALKYHPDKNPGDP---EAEEKFKEINEAYE 51
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 2-116 5.03e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 40.77  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEiidLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPPHDTQYTVfHSLIRAMLQVNPE 77
Cdd:PTZ00267   237 YLAPE---LWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQqvlyGKYDPFPCPVSSGM-KALLDPLLSKNPA 312

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462596344   78 ERLSIAEVVHQ---------LQEIAAARNVNPKSPITELLEQNGGYGS 116
Cdd:PTZ00267   313 LRPTTQQLLHTeflkyvanlFQDIVRHSETISPHDREEILRQLQESGE 360
 
Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 176-338 3.41e-123

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: 374.62  E-value: 3.41e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  176 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 255
Cdd:cd14564      1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  256 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 335
Cdd:cd14564     81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                   ...
gi 2462596344  336 CDM 338
Cdd:cd14564    161 CDM 163
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 176-338 5.99e-104

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: 5.99e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  176 VANYAKGDLDISYITSRIAVMSFPAEGVESA-LKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARR 254
Cdd:cd14511      1 QQSYARNDLDISYITSRIIVMPFPAEGIESTyRKNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  255 APHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEY 334
Cdd:cd14511     81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYY 160


                   ....
gi 2462596344  335 MCDM 338
Cdd:cd14511    161 FSDI 164
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 176-338 4.42e-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: 267.13  E-value: 4.42e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  176 VANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRA 255
Cdd:cd14563      1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  256 PHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 335
Cdd:cd14563     81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                   ...
gi 2462596344  336 CDM 338
Cdd:cd14563    161 CDL 163
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 1-96 8.52e-62

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: 212.37  E-value: 8.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERL 80
Cdd:cd14036    187 MYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERL 266

                           90
                   ....*....|....*.
gi 2462596344   81 SIAEVVHQLQEIAAAR 96
Cdd:cd14036    267 SITEIVEQLQELAAAR 282
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 185-337 1.80e-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: 1.80e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  185 DISYITSRIAVMSFPAEGV-ESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRP-SRFHNRVSECGWAARRAPHLHTLY 262
Cdd:cd14497      1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596344  263 NICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIW----PSHKRYIEYMCD 337
Cdd:cd14497     81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPgvtiPSQLRYLQYFER 159
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 185-334 2.73e-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: 2.73e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  185 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNL-SPRTYRPSRFHNRVSECGWAARRAPHLHTLYN 263
Cdd:cd14509      1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596344  264 ICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPG----IwPSHKRYIEY 334
Cdd:cd14509     81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKkgvtI-PSQRRYVYY 154
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 1-94 5.80e-45

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: 163.66  E-value: 5.80e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERL 80
Cdd:cd13985    179 MYRAPEMIDLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERP 258

                           90
                   ....*....|....
gi 2462596344   81 SIAEVVHQLQEIAA 94
Cdd:cd13985    259 DIFQVINIITKDTK 272
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 183-334 3.84e-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: 3.84e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  183 DLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNL-SPRTYRPSRFHNRVSECGWAARRAPHLHTL 261
Cdd:cd14510     13 DLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNVPTLDEM 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  262 YNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIW--------PSHKRYIE 333
Cdd:cd14510     93 LSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPSQSRYVG 172


                   .
gi 2462596344  334 Y 334
Cdd:cd14510    173 Y 173
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 185-338 3.90e-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: 3.90e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  185 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 264
Cdd:cd14508      1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596344  265 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKR-----CPPGIWPSHKRYIEYMCDM 338
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 ...
 346-484 1.36e-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: 1.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  346 PHSKPILVRAVVMTPVPLFsKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARS 425
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596344  426 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 484
Cdd:pfam10409   80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 185-335 6.92e-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: 6.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  185 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 264
Cdd:cd14561      1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596344  265 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMK-----RCPPGIWPSHKRYIEYM 335
Cdd:cd14561     81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKkfyddKVSALMQPSQKRYVQFL 156
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 185-334 7.16e-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: 7.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  185 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 264
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596344  265 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKR------CPPGiWPSHKRYIEY 334
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRfyedkvVPVG-QPSQKRYVHY 155
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
 2-93 7.80e-29

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: 117.38  E-value: 7.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLS 81
Cdd:cd14037    185 YRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPFEESGQLAILNGNFTFPDNSRYSKRLHKLIRYMLEEDPEKRPN 264

                           90
                   ....*....|..
gi 2462596344   82 IAEVVHQLQEIA 93
Cdd:cd14037    265 IYQVSYEAFELA 276
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 185-334 4.21e-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: 4.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  185 DISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNI 264
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596344  265 CRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKR-C----PPGIWPSHKRYIEY 334
Cdd:cd14562     81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfCedkvATSLQPSQRRYISY 155
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 1-91 6.32e-20

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: 91.20  E-value: 6.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFE------DGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQV 74
Cdd:cd13986    183 PYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFErifqkgDSLALAVLSGNYSFPDNSRYSEELHQLVKSMLVV 262

                           90
                   ....*....|....*..
gi 2462596344   75 NPEERLSIAEVVHQLQE 91
Cdd:cd13986    263 NPAERPSIDDLLSRVHD 279
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 2-88 3.79e-18

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: 85.59  E-value: 3.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFeDGAKL-----RIVNGKYsiPPHDTQYTV-FHSLIRAMLQVN 75
Cdd:cd08215    169 YLSPELC---ENKPYNYKSDIWALGCVLYELCTLKHPF-EANNLpalvyKIVKGQY--PPIPSQYSSeLRDLVNSMLQKD 242

                           90
                   ....*....|...
gi 2462596344   76 PEERLSIAEVVHQ 88
Cdd:cd08215    243 PEKRPSANEILSS 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 2-85 2.42e-15

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 77.18  E-value: 2.42e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344     2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKL-----RIVNGKYSIPPHDTQYTV-FHSLIRAMLQVN 75
Cdd:smart00220  162 YMAPEVL---LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlelfkKIGKPKPPFPPPEWDISPeAKDLIRKLLVKD 238

                            90
                    ....*....|
gi 2462596344    76 PEERLSIAEV 85
Cdd:smart00220  239 PEKRLTAEEA 248
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 2-85 1.88e-14

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: 74.48  E-value: 1.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIID--LYsnfpIGEKQDIWALGCILYLLCFRQHPFEDG--AKLR--IVNGKYSIPPHDTqyTVFHSLIRAMLQVN 75
Cdd:cd14003    164 YAAPEVLLgrKY----DGPKADVWSLGVILYAMLTGYLPFDDDndSKLFrkILKGKYPIPSHLS--PDARDLIRRMLVVD 237

                           90
                   ....*....|
gi 2462596344   76 PEERLSIAEV 85
Cdd:cd14003    238 PSKRITIEEI 247
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 2-84 6.35e-13

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: 70.26  E-value: 6.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFE----DGAKLRIVNGKYS-IPPHdtqYTV-FHSLIRAMLQVN 75
Cdd:cd08217    176 YMSPELL---NEQSYDEKSDIWSLGCLIYELCALHPPFQaanqLELAKKIKEGKFPrIPSR---YSSeLNEVIKSMLNVD 249


                   ....*....
gi 2462596344   76 PEERLSIAE 84
Cdd:cd08217    250 PDKRPSVEE 258
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 1-88 6.52e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 70.22  E-value: 6.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNP 76
Cdd:cd08528    179 LYSCPEIV---QNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLtlatKIVEAEYEPLPEGMYSDDITFVIRSCLTPDP 255

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd08528    256 EARPDIVEVSSM 267
Pkinase pfam00069
Protein kinase domain;
2-87 8.04e-13

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 68.81  E-value: 8.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPPHDtqYTV---FHSLIRAMLQV 74
Cdd:pfam00069  126 YMAPEVL---GGNPYGPKVDVWSLGCILYELLTGKPPFpginGNEIYELIIDQPYAFPELP--SNLseeAKDLLKKLLKK 200

                           90
                   ....*....|...
gi 2462596344   75 NPEERLSIAEVVH 87
Cdd:pfam00069  201 DPSKRLTATQALQ 213
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-81 8.97e-13

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: 69.62  E-value: 8.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIidlYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGA----KLRIVNGKYSIPPHDTQYTVfHSLIRAMLQVNPE 77
Cdd:cd08219    166 YVPPEI---WENMPYNNKSDIWSLGCILYELCTLKHPFQANSwknlILKVCQGSYKPLPSHYSYEL-RSLIKQMFKRNPR 241


                   ....
gi 2462596344   78 ERLS 81
Cdd:cd08219    242 SRPS 245
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-86 1.34e-12

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 69.07  E-value: 1.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDlysNFPIGEKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYsiPPHDTQYTV-FHSLIRAMLQVNP 76
Cdd:cd08218    167 YLSPEICE---NKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMknlvLKIIRGSY--PPVPSRYSYdLRSLVSQLFKRNP 241

                           90
                   ....*....|
gi 2462596344   77 EERLSIAEVV 86
Cdd:cd08218    242 RDRPSINSIL 251
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 2-88 1.59e-12

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: 69.00  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEiidLYSNFPIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKysIPPHDTQY-TVFHSLIRAMLQVNP 76
Cdd:cd08223    168 YMSPE---LFSNKPYNHKSDVWALGCCVYEMATLKHAFnaKDMNSLvyKILEGK--LPPMPKQYsPELGELIKAMLHQDP 242

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd08223    243 EKRPSVKRILRQ 254
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
 21-86 2.57e-12

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: 68.35  E-value: 2.57e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   21 DIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14099    184 DIWSLGVILYTLLVGKPPFETSDVketyKRIKKNEYSFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEIL 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
 2-85 6.58e-12

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: 66.89  E-value: 6.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYSnfpiGEKQDIWALGCILYLLCFRQHPFeDGAKLR-----IVNGKYSIPPH---DTQytvfhSLIRAM 71
Cdd:cd14081    166 YACPEVIkgEKYD----GRKADIWSCGVILYALLVGALPF-DDDNLRqllekVKRGVFHIPHFispDAQ-----DLLRRM 235

                           90
                   ....*....|....
gi 2462596344   72 LQVNPEERLSIAEV 85
Cdd:cd14081    236 LEVNPEKRITIEEI 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
 2-88 1.40e-11

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: 65.90  E-value: 1.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEiidLYSNFPIGEKQDIWALGCILYLLCFRQHPFE---DGAK-LRIVNGKYsiPPHDTQYT-VFHSLIRAMLQVNP 76
Cdd:cd08529    167 YLSPE---LCEDKPYNEKSDVWALGCVLYELCTGKHPFEaqnQGALiLKIVRGKY--PPISASYSqDLSQLIDSCLTKDY 241

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd08529    242 RQRPDTTELLRN 253
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 2-88 1.43e-11

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: 66.13  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDlysNFPIGEKQDIWALGCILYLLCFRQHPFEDGA----KLRIVNGKYS-IPPHDTQYtvFHSLIRAMLQVNP 76
Cdd:cd08225    168 YLSPEICQ---NRPYNNKTDIWSLGCVLYELCTLKHPFEGNNlhqlVLKICQGYFApISPNFSRD--LRSLISQLFKVSP 242

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd08225    243 RDRPSITSILKR 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 5-85 8.68e-11

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: 63.65  E-value: 8.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    5 PEIIDlysNFPIGEKQDIWALGCILY-LLCFRqHPF--EDGAKL--RIVNGKYSIPPhdtqyTVFHS-------LIRAML 72
Cdd:cd05117    170 PEVLK---GKGYGKKCDIWSLGVILYiLLCGY-PPFygETEQELfeKILKGKYSFDS-----PEWKNvseeakdLIKRLL 240

                           90
                   ....*....|...
gi 2462596344   73 QVNPEERLSIAEV 85
Cdd:cd05117    241 VVDPKKRLTAAEA 253
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 1-88 1.48e-10

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: 63.18  E-value: 1.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIidlYSNFPIGEKQDIWALGCILYLLCFRQHPFE----DGAKLRIVNGKYSIPPH----DTQytvfhSLIRAML 72
Cdd:cd08530    166 LYAAPEV---WKGRPYDYKSDIWSLGCLLYEMATFRPPFEartmQELRYKVCRGKFPPIPPvysqDLQ-----QIIRSLL 237

                           90
                   ....*....|....*.
gi 2462596344   73 QVNPEERLSIAEVVHQ 88
Cdd:cd08530    238 QVNPKKRPSCDKLLQS 253
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 2-87 1.98e-10

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: 62.79  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYsnfpIGEKQDIWALGCILY-LLC-FRqhPFEDG--AKL--RIVNGKYSIPPHDTQYTVFhsLIRAMLQ 73
Cdd:cd14078    168 YAAPELIqgKPY----IGSEADVWSMGVLLYaLLCgFL--PFDDDnvMALyrKIQSGKYEEPEWLSPSSKL--LLDQMLQ 239

                           90
                   ....*....|....
gi 2462596344   74 VNPEERLSIAEVVH 87
Cdd:cd14078    240 VDPKKRITVKELLN 253
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 5-85 3.53e-10

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: 61.89  E-value: 3.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    5 PEIIDLYSNFPiGEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPPH-DTQytvFHSLIRAMLQVNPEER 79
Cdd:cd14119    168 PEIANGQDSFS-GFKVDIWSAGVTLYNMTTGKYPFEGDNIYKlfenIGKGEYTIPDDvDPD---LQDLLRGMLEKDPEKR 243


                   ....*.
gi 2462596344   80 LSIAEV 85
Cdd:cd14119    244 FTIEQI 249
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 2-85 9.31e-10

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 60.43  E-value: 9.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYsnfpIGEKQDIWALGCILYLLCFRQHPF--EDGAKLR--IVNGKYSIPPHDTQYTvfHSLIRAMLQVN 75
Cdd:cd14075    166 YAAPELFkdEHY----IGIYVDIWALGVLLYFMVTGVMPFraETVAKLKkcILEGTYTIPSYVSEPC--QELIRGILQPV 239

                           90
                   ....*....|
gi 2462596344   76 PEERLSIAEV 85
Cdd:cd14075    240 PSDRYSIDEI 249
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 2-85 1.24e-09

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: 60.18  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDG----AKLRIVNGKYSIPPH---DTQytvfhSLIRAMLQV 74
Cdd:cd14007    164 YLPPEMV---EGKEYDYKVDIWSLGVLCYELLVGKPPFESKshqeTYKRIQNVDIKFPSSvspEAK-----DLISKLLQK 235

                           90
                   ....*....|.
gi 2462596344   75 NPEERLSIAEV 85
Cdd:cd14007    236 DPSKRLSLEQV 246
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
 2-86 2.18e-09

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: 59.35  E-value: 2.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYSnfpiGEKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHDTQYTvfHSLIRAMLQVN 75
Cdd:cd14074    169 YSAPEILlgDEYD----APAVDIWSLGVILYMLVCGQPPFQEANDsetlTMIMDCKYTVPAHVSPEC--KDLIRRMLIRD 242

                           90
                   ....*....|.
gi 2462596344   76 PEERLSIAEVV 86
Cdd:cd14074    243 PKKRASLEEIE 253
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 2-85 2.35e-09

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: 59.54  E-value: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPE-IIDL-YSNFP-----IGEKQDIWALGCILYLLCFRQHPFED----GAKL-RIVNGKYSI--PPHDTQytvfhSL 67
Cdd:cd14131    170 YMSPEaIKDTsASGEGkpkskIGRPSDVWSLGCILYQMVYGKTPFQHitnpIAKLqAIIDPNHEIefPDIPNP-----DL 244

                           90       100
                   ....*....|....*....|.
gi 2462596344   68 IRAM---LQVNPEERLSIAEV 85
Cdd:cd14131    245 IDVMkrcLQRDPKKRPSIPEL 265
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
 2-85 3.20e-09

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: 58.82  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIID--LYSnfpiGEKQDIWALGCILY-LLCFRQhPFEDG--AKL--RIVNGKYSIPPHDTQYTVfhSLIRAMLQV 74
Cdd:cd14079    167 YAAPEVISgkLYA----GPEVDVWSCGVILYaLLCGSL-PFDDEhiPNLfkKIKSGIYTIPSHLSPGAR--DLIKRMLVV 239

                           90
                   ....*....|.
gi 2462596344   75 NPEERLSIAEV 85
Cdd:cd14079    240 DPLKRITIPEI 250
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
 2-86 1.05e-08

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: 57.36  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPiGEKQDIWALGCILYLLCFRQHPFEDG------AKLRivNGKYSIPPHDTQYTvfHSLIRAMLQVN 75
Cdd:cd14023    152 YVSPEILNTTGTYS-GKSADVWSLGVMLYTLLVGRYPFHDSdpsalfSKIR--RGQFCIPDHVSPKA--RCLIRSLLRRE 226

                           90
                   ....*....|.
gi 2462596344   76 PEERLSIAEVV 86
Cdd:cd14023    227 PSERLTAPEIL 237
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-88 1.24e-08

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: 57.05  E-value: 1.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDlysNFPIGEKQDIWALGCILYLLCFRQHPFEdGAKL-----RIVNGKYSiPPHDTQYTVFHSLIRAMLQVNP 76
Cdd:cd08220    167 YISPELCE---GKPYNQKSDIWALGCVLYELASLKRAFE-AANLpalvlKIMRGTFA-PISDRYSEELRHLILSMLHLDP 241

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd08220    242 NKRPTLSEIMAQ 253
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 5-85 1.39e-08

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: 57.18  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    5 PEIID----LYSNFPIgekqDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNP 76
Cdd:cd14008    177 PELCDgdskTYSGKAA----DIWALGVTLYCLVFGRLPFNGDNILelyeAIQNQNDEFPIPPELSPELKDLLRRMLEKDP 252


                   ....*....
gi 2462596344   77 EERLSIAEV 85
Cdd:cd14008    253 EKRITLKEI 261
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 2-85 1.44e-08

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: 57.37  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPPHDTQYTVFHSLIRAMLQVNPE 77
Cdd:cd14118    181 FMAPEALSESRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGlhekIKTDPVVFPDDPVVSEQLKDLILRMLDKNPS 260


                   ....*...
gi 2462596344   78 ERLSIAEV 85
Cdd:cd14118    261 ERITLPEI 268
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 2-84 1.56e-08

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: 57.43  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPH--DTQYTVFHSLIRAMLQVN 75
Cdd:cd14086    169 YLSPEVL---RKDPYGKPVDIWACGVILYILLVGYPPFwdEDQHRLyaQIKAGAYDYPSPewDTVTPEAKDLINQMLTVN 245


                   ....*....
gi 2462596344   76 PEERLSIAE 84
Cdd:cd14086    246 PAKRITAAE 254
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
 21-86 2.22e-08

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: 56.53  E-value: 2.22e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596344   21 DIWALGCILY-LLC-----FRQH--PFEDGAKLRIVNGKYSIPphDTQYTVFHS----LIRAMLQVNPEERLSIAEVV 86
Cdd:cd14089    184 DMWSLGVIMYiLLCgyppfYSNHglAISPGMKKRIRNGQYEFP--NPEWSNVSEeakdLIRGLLKTDPSERLTIEEVM 259
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 2-85 2.57e-08

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: 56.51  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYsNFpigeKQDIWALGCILYLLCFRQHPFE-DGAKL-----RIVNGKYSIPPHDTQYTVFHSLIRAMLQ 73
Cdd:cd08224    170 YMSPERIreQGY-DF----KSDIWSLGCLLYEMAALQSPFYgEKMNLyslckKIEKCEYPPLPADLYSQELRDLVAACIQ 244

                           90
                   ....*....|..
gi 2462596344   74 VNPEERLSIAEV 85
Cdd:cd08224    245 PDPEKRPDISYV 256
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 21-86 2.99e-08

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: 56.09  E-value: 2.99e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   21 DIWALGCILYLLCFRQHPFEDG----AKLRIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14187    189 DIWSIGCIMYTLLVGKPPFETSclkeTYLRIKKNEYSIPKHIN--PVAASLIQKMLQTDPTARPTINELL 256
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 2-85 4.01e-08

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: 55.48  E-value: 4.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIID--LYSnfpiGEKQDIWALGCILYLLCFRQHPFeDGAKL-----RIVNGKYSIPphdtqytVFHS-----LIR 69
Cdd:cd14071    164 YAAPEVFEgkEYE----GPQLDIWSLGVVLYVLVCGALPF-DGSTLqtlrdRVLSGRFRIP-------FFMStdcehLIR 231

                           90
                   ....*....|....*.
gi 2462596344   70 AMLQVNPEERLSIAEV 85
Cdd:cd14071    232 RMLVLDPSKRLTIEQI 247
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 2-85 4.75e-08

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: 55.68  E-value: 4.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGA----KLRIVNGKYSIP---PHDTQytvfhSLIRAMLQV 74
Cdd:cd05581    184 YVSPELL---NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNeyltFQKIVKLEYEFPenfPPDAK-----DLIQKLLVL 255

                           90
                   ....*....|.
gi 2462596344   75 NPEERLSIAEV 85
Cdd:cd05581    256 DPSKRLGVNEN 266
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 1-87 6.49e-08

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: 55.09  E-value: 6.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDlysNFP-IGEKQDIWALGCILYLLCFRQHPFE--DGAKLR--IVNGKYSIPPHDTqytVFHSLIRAMLQVN 75
Cdd:cd14073    165 LYASPEIVN---GTPyQGPEVDCWSLGVLLYTLVYGTMPFDgsDFKRLVkqISSGDYREPTQPS---DASGLIRWMLTVN 238

                           90
                   ....*....|..
gi 2462596344   76 PEERLSIAEVVH 87
Cdd:cd14073    239 PKRRATIEDIAN 250
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 1-85 7.02e-08

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: 54.96  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDlysNFP-IGEKQDIWALGCILYLLCFRQHPFE--DGAKL--RIVNGKYSIPPHDTQYTvfhSLIRAMLQVN 75
Cdd:cd14161    166 LYASPEIVN---GRPyIGPEVDSWSLGVLLYILVHGTMPFDghDYKILvkQISSGAYREPTKPSDAC---GLIRWLLMVN 239

                           90
                   ....*....|
gi 2462596344   76 PEERLSIAEV 85
Cdd:cd14161    240 PERRATLEDV 249
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1080-1124 2.47e-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: 48.31  E-value: 2.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462596344 1080 PEQVKRHYRRAVLAVHPDKAAGQPYeqhAKMIFMELNDAWSEFEN 1124
Cdd:cd06257     14 DEEIKKAYRKLALKYHPDKNPDDPE---AEEKFKEINEAYEVLSD 55
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 2-87 2.68e-07

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: 53.34  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFP-IGEKQDIWALGCILYLLCFRQHPFEDG--AKL--RIVNGKYSIPPHDTQYTV-FHSLIRAMLQVN 75
Cdd:cd14080    170 YAAPEIL---QGIPyDPKKYDIWSLGVILYIMLCGSMPFDDSniKKMlkDQQNRKVRFPSSVKKLSPeCKDLIDQLLEPD 246

                           90
                   ....*....|..
gi 2462596344   76 PEERLSIAEVVH 87
Cdd:cd14080    247 PTKRATIEEILN 258
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-86 2.78e-07

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: 53.20  E-value: 2.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDL--YSNfpigeKQDIWALGCILYLLCFRQHPFeDGAKL-----RIVNGKY-SIPPHDTqyTVFHSLIRAMLQ 73
Cdd:cd08222    171 YMSPEVLKHegYNS-----KSDIWSLGCILYEMCCLKHAF-DGQNLlsvmyKIVEGETpSLPDKYS--KELNAIYSRMLN 242

                           90
                   ....*....|...
gi 2462596344   74 VNPEERLSIAEVV 86
Cdd:cd08222    243 KDPALRPSAAEIL 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 2-85 3.12e-07

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: 53.17  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFED-----GAKLRIVNGKYS-IPPHDTQYTV-FHSLIRAMLQV 74
Cdd:cd14084    179 YLAPEVLRSFGTEGYTRAVDCWSLGVILFICLSGYPPFSEeytqmSLKEQILSGKYTfIPKAWKNVSEeAKDLVKKMLVV 258

                           90
                   ....*....|.
gi 2462596344   75 NPEERLSIAEV 85
Cdd:cd14084    259 DPSRRPSIEEA 269
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
 9-90 3.41e-07

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: 53.18  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    9 DLYSNFP-IGEKQDIWALGCILYLLCFRQHPFEDGA--KL--RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIA 83
Cdd:cd13974    203 DVLSGKPyLGKPSDMWALGVVLFTMLYGQFPFYDSIpqELfrKIKAAEYTIPEDGRVSENTVCLIRKLLVLNPQKRLTAS 282


                   ....*..
gi 2462596344   84 EVVHQLQ 90
Cdd:cd13974    283 EVLDSLE 289
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 2-86 3.41e-07

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: 52.77  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIidLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDgaKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERLS 81
Cdd:cd14004    173 YAAPEV--LRGNPYGGKEQDIWALGVLLYTLVFKENPFYN--IEEILEADLRIPYAVSEDLI--DLISRMLNRDVGDRPT 246


                   ....*
gi 2462596344   82 IAEVV 86
Cdd:cd14004    247 IEELL 251
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 2-84 3.48e-07

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: 53.04  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRqHPFEDGAKL-----RIVNGKYSIPPH-----DTQYTVFHSLIRAM 71
Cdd:cd14133    167 YRAPEVI---LGLPYDEKIDMWSLGCILAELYTG-EPLFPGASEvdqlaRIIGTIGIPPAHmldqgKADDELFVDFLKKL 242

                           90
                   ....*....|...
gi 2462596344   72 LQVNPEERLSIAE 84
Cdd:cd14133    243 LEIDPKERPTASQ 255
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 1-81 4.36e-07

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: 52.52  E-value: 4.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQytVFHSLIRAMLQVNP 76
Cdd:cd05123    158 EYLAPEVL---LGKGYGKAVDWWSLGVLLYEMLTGKPPFyaENRKEIyeKILKSPLKFPEYVSP--EAKSLISGLLQKDP 232


                   ....*
gi 2462596344   77 EERLS 81
Cdd:cd05123    233 TKRLG 237
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 584-965 9.07e-07

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: 53.23  E-value: 9.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  584 ENASSKESESALMEDRDESEVSDEG----GSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQ-----E 654
Cdd:pfam03154  140 DNRSTSPSIPSPQDNESDSDSSAQQqilqTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAtsqppN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  655 DGVDLLGLHSEVGAGPAVPPQACKAPSSntdllscllgPPEAASQGPPEDLLSEDPL---LLASPAPPL--SVQSTPRGG 729
Cdd:pfam03154  220 QTQSTAAPHTLIQQTPTLHPQRLPSPHP----------PLQPMTQPPPPSQVSPQPLpqpSLHGQMPPMphSLQTGPSHM 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  730 P-PAAADPFGPLLPSSGNNSQPCSNPDLFGEflNSDSVTVPPSFPSAHSAPPPS------CSADFLHLGDLPGEP-SKMT 801
Cdd:pfam03154  290 QhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ--SQQRIHTPPSQSQLQSQQPPReqplppAPLSMPHIKPPPTTPiPQLP 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  802 ASSSN--PDLLGGWAAWTetAASAVAPTPATEgPLFSPGGQPAPcgsqaswtkSQNPDPFaDLGDLSSGLQDPQAQSTVS 879
Cdd:pfam03154  368 NPQSHkhPPHLSGPSPFQ--MNSNLPPPPALK-PLSSLSTHHPP---------SAHPPPL-QLMPQSQQLPPPPAQPPVL 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  880 PRGQRVCTCSRRLPTgklkPGVADTGTAASPhrhcgspagFPPGGFIPKTATT--------PKGSSSWQTSRPPAQGASW 951
Cdd:pfam03154  435 TQSQSLPPPAASHPP----TSGLHQVPSQSP---------FPQHPFVPGGPPPitppsgppTSTSSAMPGIQPPSSASVS 501

                          410
                   ....*....|....
gi 2462596344  952 PPQAKPPPKACTQP 965
Cdd:pfam03154  502 SSGPVPAAVSCPLP 515
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 1-87 1.06e-06

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: 51.47  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIdlYSNFPIGEKQDIWALGCILYLLCFRQHPFEDG------AKLRIVNGKYSipphdtqytvFHSLIRAMLQV 74
Cdd:cd05118    165 WYRAPEVL--LGAKPYGSSIDIWSLGCILAELLTGRPLFPGDsevdqlAKIVRLLGTPE----------ALDLLSKMLKY 232

                           90
                   ....*....|...
gi 2462596344   75 NPEERLSIAEVVH 87
Cdd:cd05118    233 DPAKRITASQALA 245
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 2-86 1.14e-06

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: 51.32  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--------DLYSNfpigeKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPhDTQYTVFH---S 66
Cdd:cd14098    168 YLAPEILmskeqnlqGGYSN-----LVDMWSVGCLVYVMLTGALPFDGSSQLpvekRIRKGRYTQPP-LVDFNISEeaiD 241

                           90       100
                   ....*....|....*....|
gi 2462596344   67 LIRAMLQVNPEERLSIAEVV 86
Cdd:cd14098    242 FILRLLDVDPEKRMTAAQAL 261
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 2-85 1.30e-06

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: 51.45  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPE 77
Cdd:cd05579    174 YLAPEIL---LGQGHGKTVDWWSLGVILYEFLVGIPPFhaETPEEIfqNILNGKIEWPEDPEVSDEAKDLISKLLTPDPE 250

                           90
                   ....*....|.
gi 2462596344   78 ERL---SIAEV 85
Cdd:cd05579    251 KRLgakGIEEI 261
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
 2-86 1.43e-06

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 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 TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 50.81  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPiGEKQDIWALGCILYLLCFRQHPFED------GAKLRivNGKYSIPphDTQYTVFHSLIRAMLQVN 75
Cdd:cd14022    152 YVSPEILNTSGSYS-GKAADVWSLGVMLYTMLVGRYPFHDiepsslFSKIR--RGQFNIP--ETLSPKAKCLIRSILRRE 226

                           90
                   ....*....|.
gi 2462596344   76 PEERLSIAEVV 86
Cdd:cd14022    227 PSERLTSQEIL 237
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 2-85 2.81e-06

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: 50.02  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILY-LLC----FRQhPFEDGAKL--RIVNGKYSIPPH--DTQYTVFHSLIRAML 72
Cdd:cd14095    165 YVAPEIL---AETGYGLKVDIWAAGVITYiLLCgfppFRS-PDRDQEELfdLILAGEFEFLSPywDNISDSAKDLISRML 240

                           90
                   ....*....|...
gi 2462596344   73 QVNPEERLSIAEV 85
Cdd:cd14095    241 VVDPEKRYSAGQV 253
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 2-91 3.88e-06

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: 49.51  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGK--YSIPPHDTQYTVFHS----LIRAMLQVN 75
Cdd:cd14014    167 YMAPEQA---RGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHlqEAPPPPSPLNPDVPPaldaIILRALAKD 243

                           90
                   ....*....|....*..
gi 2462596344   76 PEERL-SIAEVVHQLQE 91
Cdd:cd14014    244 PEERPqSAAELLAALRA 260
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1080-1125 4.29e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 44.92  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2462596344  1080 PEQVKRHYRRAVLAVHPDKAAGQPYEqhAKMIFMELNDAWSEFENQ 1125
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 2-84 4.99e-06

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 49.74  E-value: 4.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYSnfpigEKQDIWALGCILY-LLC-FRqhPFEDGAK----LRIVNGKYSI--PPHDTQYTVFHSLIRAM 71
Cdd:cd14096    203 YTAPEVVkdERYS-----KKVDMWALGCVLYtLLCgFP--PFYDESIetltEKISRGDYTFlsPWWDEISKSAKDLISHL 275

                           90
                   ....*....|...
gi 2462596344   72 LQVNPEERLSIAE 84
Cdd:cd14096    276 LTVDPAKRYDIDE 288
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 2-85 5.02e-06

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: 49.66  E-value: 5.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYSNFP-IGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSI--PPHDTQYTVFHSLIRAML 72
Cdd:cd14093    174 YLAPEVLkcSMYDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMvmlrNIMEGKYEFgsPEWDDISDTAKDLISKLL 253

                           90
                   ....*....|...
gi 2462596344   73 QVNPEERLSIAEV 85
Cdd:cd14093    254 VVDPKKRLTAEEA 266
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-88 5.04e-06

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: 49.35  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIppHDTQYTV-FHSLIRAMLQVNP 76
Cdd:cd08221    167 YMSPELV---QGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRlavkIVQGEYED--IDEQYSEeIIQLVHDCLHQDP 241

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd08221    242 EDRPTAEELLER 253
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 2-86 5.60e-06

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: 49.09  E-value: 5.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPPHDTQYTvfHSLIRAMLQVNPE 77
Cdd:cd14186    168 YISPEIA---TRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNkvvlADYEMPAFLSREA--QDLIHQLLRKNPA 242


                   ....*....
gi 2462596344   78 ERLSIAEVV 86
Cdd:cd14186    243 DRLSLSSVL 251
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 1-87 5.92e-06

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: 49.17  E-value: 5.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIDlysNFPIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPphDTQYTVFHSLIRAMLQVNP 76
Cdd:cd14002    164 LYMAPELVQ---EQPYDHTADLWSLGCILYELFVGQPPFytNSIYQLvqMIVKDPVKWP--SNMSPEFKSFLQGLLNKDP 238

                           90
                   ....*....|.
gi 2462596344   77 EERLSIAEVVH 87
Cdd:cd14002    239 SKRLSWPDLLE 249
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 2-88 6.38e-06

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: 48.85  E-value: 6.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNfpiGEKQDIWALGCILYLLCFRQHPFEDgAKLR-----IVNGKYSIPphDTQYTVFHSLIRAMLQVNP 76
Cdd:cd14188    167 YLSPEVLNKQGH---GCESDIWALGCVMYTMLLGRPPFET-TNLKetyrcIREARYSLP--SSLLAPAKHLIASMLSKNP 240

                           90
                   ....*....|..
gi 2462596344   77 EERLSIAEVVHQ 88
Cdd:cd14188    241 EDRPSLDEIIRH 252
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 2-85 6.85e-06

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: 48.94  E-value: 6.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYsnfpIGEKQDIWALGCILYLLCFRQHPFEDG--AKL--RIVNGKYSIPPHDTQYTVfhSLIRAMLQVN 75
Cdd:cd14663    168 YVAPEVLarRGY----DGAKADIWSCGVILFVLLAGYLPFDDEnlMALyrKIMKGEFEYPRWFSPGAK--SLIKRILDPN 241

                           90
                   ....*....|
gi 2462596344   76 PEERLSIAEV 85
Cdd:cd14663    242 PSTRITVEQI 251
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 21-87 7.07e-06

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: 49.00  E-value: 7.07e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596344   21 DIWALGCILY-LLC-----FRQHP---FEDGAKLRIVNGKYSIPPHDTQYT--VFHSLIRAMLQVNPEERLSIAEVVH 87
Cdd:cd14171    208 DMWSLGVIIYiMLCgyppfYSEHPsrtITKDMKRKIMTGSYEFPEEEWSQIseMAKDIVRKLLCVDPEERMTIEEVLH 285
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 2-85 8.73e-06

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: 48.62  E-value: 8.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPigEKQDIWALGCILYLLCFRQHPFEDG---AKLRI-VNGKYSIPPHDTQYTVFHSLIRAMLQVNPE 77
Cdd:cd14165    172 YAAPEVLQGIPYDP--RIYDIWSLGVILYIMVCGSMPYDDSnvkKMLKIqKEHRVRFPRSKNLTSECKDLIYRLLQPDVS 249


                   ....*...
gi 2462596344   78 ERLSIAEV 85
Cdd:cd14165    250 QRLCIDEV 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-141 1.58e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 48.86  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   21 DIWALGCILYLLCFRQHPFE---DGAKLRIVNGKYSIPPHDTQYTV---FHSLIRAMLQVNPEERL-SIAEVVHQLQEIA 93
Cdd:COG0515    190 DVYSLGVTLYELLTGRPPFDgdsPAELLRAHLREPPPPPSELRPDLppaLDAIVLRALAKDPEERYqSAAELAAALRAVL 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462596344   94 AARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALA 141
Cdd:COG0515    270 RSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 317
PHA03247 PHA03247
large tegument protein UL36; Provisional
 615-945 1.90e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  615 EGQEPRADPEPPGLAAGLVQQdlvfevETPAVLPEPVPqedgvdllglHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPP 694
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP------PPPPPTPEPAP----------HALVSATPLPPGPAAARQASPALPAAPAPPAV 2744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  695 EAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPS 774
Cdd:PHA03247  2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  775 AHSAPPPSCSAdflhlgdlPGEPSKMTASSSNPDLLGGWAAwtetAASAVAPTPATEGPLFSPGGQPAPCGSQ-ASWTKS 853
Cdd:PHA03247  2825 AGPLPPPTSAQ--------PTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS 2892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  854 QNPDPFADLGDLSSGLQDPQAQS----TVSPRGQRVCTCSRRLPTGKLKPGVADTGTAASPHRHCGSPA----GFPPGGF 925
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgALVPGRV 2972

                          330       340
                   ....*....|....*....|
gi 2462596344  926 IPKTATTPKGSSSWQTSRPP 945
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAPASS 2992
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 16-86 2.12e-05

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: 47.44  E-value: 2.12e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596344   16 IGEKQDIWALGCILYLLCFRQHPFED----GAKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14077    190 TGPEVDVWSFGVVLYVLVCGKVPFDDenmpALHAKIKKGKVEYPSYLSSECK--SLISRMLVVDPKKRATLEQVL 262
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
 17-86 2.36e-05

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: 47.13  E-value: 2.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596344   17 GEKQDIWALGCILYLLCFRQHPFeDGAKL-----RIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14072    177 GPEVDVWSLGVILYTLVSGSLPF-DGQNLkelreRVLRGKYRIPFYMS--TDCENLLKKFLVLNPSKRGTLEQIM 248
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
 4-81 3.64e-05

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: 46.76  E-value: 3.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    4 TPEII--DLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPPH--DTQYTVFHSLIRAMLQVN 75
Cdd:cd14087    164 TPEYIapEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRlyrqILRAKYSYSGEpwPSVSNLAKDFIDRLLTVN 243


                   ....*.
gi 2462596344   76 PEERLS 81
Cdd:cd14087    244 PGERLS 249
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
 2-86 4.72e-05

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: 46.77  E-value: 4.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEdGAKLR----IVNGKYSIPPH--DTQYTVFHSLIRAMLQVN 75
Cdd:cd14094    178 FMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERlfegIIKGKYKMNPRqwSHISESAKDLVRRMLMLD 253

                           90
                   ....*....|.
gi 2462596344   76 PEERLSIAEVV 86
Cdd:cd14094    254 PAERITVYEAL 264
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
 21-86 8.79e-05

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: 45.70  E-value: 8.79e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596344   21 DIWALGCILYLLCFRQHPF----EDGAK---LRIVNGKYSI--PPHDTQYTVFHSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14091    180 DIWSLGVLLYTMLAGYTPFasgpNDTPEvilARIGSGKIDLsgGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVL 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 5-84 9.42e-05

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: 45.27  E-value: 9.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    5 PEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRI-----VNGKYSIpPHDTQYT-VFHSLIRAMLQVNPEE 78
Cdd:cd05122    166 PEVI---QGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKAlfliaTNGPPGL-RNPKKWSkEFKDFLKKCLQKDPEK 241


                   ....*.
gi 2462596344   79 RLSIAE 84
Cdd:cd05122    242 RPTAEQ 247
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 2-86 1.08e-04

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: 45.30  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNfpiGEKQDIWALGCILYLLCFRQHPFEDgAKLR-----IVNGKYSIPPHDTQYTvfHSLIRAMLQVNP 76
Cdd:cd14189    167 YLAPEVLLRQGH---GPESDVWSLGCVMYTLLCGNPPFET-LDLKetyrcIKQVKYTLPASLSLPA--RHLLAGILKRNP 240

                           90
                   ....*....|
gi 2462596344   77 EERLSIAEVV 86
Cdd:cd14189    241 GDRLTLDQIL 250
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
 2-85 1.23e-04

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 45.11  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIID---LYSnfpiGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTvfHSLIRAMLQV 74
Cdd:cd13976    152 YVSPEILNsgaTYS----GKAADVWSLGVILYTMLVGRYPFHDSEPAslfaKIRRGQFAIPETLSPRA--RCLIRSLLRR 225

                           90
                   ....*....|.
gi 2462596344   75 NPEERLSIAEV 85
Cdd:cd13976    226 EPSERLTAEDI 236
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 578-950 1.38e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  578 EAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQdlvfEVETPAVLPEPVPQEDGV 657
Cdd:PHA03307    78 EAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLS----EMLRPVGSPGPPPAASPP 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  658 DLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPF 737
Cdd:PHA03307   154 AAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  738 GPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPppscsadflhlgdLPGEPSKMTASSSNPDllggwaawt 817
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW-------------NGPSSRPGPASSSSSP--------- 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  818 etAASAVAPTPAtegplfSPGGQPAPCGSQASWTKSQNPDpfadlGDLSSGLQDPQAQSTVSPRGQRVCTCSRRLPTGKL 897
Cdd:PHA03307   292 --RERSPSPSPS------SPGSGPAPSSPRASSSSSSSRE-----SSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596344  898 KPGVADTGTAASPHRHCGSPAGFPPGGFIPKTATTPKGSSSWQtSRPPAQGAS 950
Cdd:PHA03307   359 PADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRR-DATGRFPAG 410
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 21-86 1.39e-04

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: 44.98  E-value: 1.39e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596344   21 DIWALGCILYLLCFRQHPF--EDGAKL--RIVNG--KYSIPPHDTQYTV-FHSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14010    192 DLWALGCVLYEMFTGKPPFvaESFTELveKILNEdpPPPPPKVSSKPSPdFKSLLKGLLEKDPAKRLSWDELV 264
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 580-982 1.64e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  580 ETGAENASSKESESALMEDRDESEVSDEGGSPISSEGqePRADPePPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDL 659
Cdd:PHA03307    12 EAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSA--ELAAV-TVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  660 LGLHSEVGAGPAVPPQACKAPSSNTDllscllGPPEAASQgPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGP 739
Cdd:PHA03307    89 TWSLSTLAPASPAREGSPTPPGPSSP------DPPPPTPP-PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  740 LlPSSGNNSQPCSNPdlfgefLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTET 819
Cdd:PHA03307   162 V-ASDAASSRQAALP------LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  820 AASAVAPT--------PATEGPLFSPGGQPAP-CGSQASWTKSQNPDPfadlgdlssglqdpqaqSTVSPRGqrvctcSR 890
Cdd:PHA03307   235 SSSDSSSSessgcgwgPENECPLPRPAPITLPtRIWEASGWNGPSSRP-----------------GPASSSS------SP 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  891 RLPTGKLKPGVADTGTAASPHRHCGSPAGFPPGGfIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKAC------TQ 964
Cdd:PHA03307   292 RERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS-SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPssprkrPR 370

                          410
                   ....*....|....*...
gi 2462596344  965 PRPNyASNFSVIGAREER 982
Cdd:PHA03307   371 PSRA-PSSPAASAGRPTR 387
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1080-1119 1.75e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 40.94  E-value: 1.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462596344 1080 PEQVKRHYRRAVLAVHPDK-AAGQPyeQHAKMIFME----LNDAW 1119
Cdd:COG1076     18 DAELKRAYRKLQREHHPDRlAAGLP--EEEQRLALQkaaaINEAY 60
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1081-1120 1.91e-04

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: 40.53  E-value: 1.91e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462596344 1081 EQVKRHYRRAVLAVHPDKAAGQPyeqHAKMIFMELNDAWS 1120
Cdd:pfam00226   15 EEIKKAYRKLALKYHPDKNPGDP---EAEEKFKEINEAYE 51
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
 2-86 2.11e-04

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 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 TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 44.10  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFPiGEKQDIWALGCILYLLCFRQHPFEDG------AKLRivNGKYSIPphDTQYTVFHSLIRAMLQVN 75
Cdd:cd14024    152 YVGPEILSSRRSYS-GKAADVWSLGVCLYTMLLGRYPFQDTepaalfAKIR--RGAFSLP--AWLSPGARCLVSCMLRRS 226

                           90
                   ....*....|.
gi 2462596344   76 PEERLSIAEVV 86
Cdd:cd14024    227 PAERLKASEIL 237
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 2-86 2.13e-04

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: 44.25  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKL------RIVNGKYSIP-PH-DTQYTVFHSLIRAMLQ 73
Cdd:cd14184    166 YVAPEII---AETGYGLKVDIWAAGVITYILLCGFPPFRSENNLqedlfdQILLGKLEFPsPYwDNITDSAKELISHMLQ 242

                           90
                   ....*....|...
gi 2462596344   74 VNPEERLSIAEVV 86
Cdd:cd14184    243 VNVEARYTAEQIL 255
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 2-80 2.16e-04

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: 44.52  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILY-LLCFRQhPF----EDGAKL--RIVNGKYSI--PPHDTQytVFHSLIRAML 72
Cdd:cd05572    158 YVAPEII---LNKGYDFSVDYWSLGILLYeLLTGRP-PFggddEDPMKIynIILKGIDKIefPKYIDK--NAKNLIKQLL 231


                   ....*...
gi 2462596344   73 QVNPEERL 80
Cdd:cd05572    232 RRNPEERL 239
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 5-89 4.13e-04

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: 43.30  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    5 PEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKY----------SIPPHdtqytvFHSLIRAMLQV 74
Cdd:cd13999    160 PEVL---RGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVqkglrppippDCPPE------LSKLIKRCWNE 230

                           90
                   ....*....|....*
gi 2462596344   75 NPEERLSIAEVVHQL 89
Cdd:cd13999    231 DPEKRPSFSEIVKRL 245
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 719-932 4.65e-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: 44.52  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  719 PLSVQSTPRGGPPAAADPFGPL-LPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSAdflhlgdlpgEP 797
Cdd:pfam05109  425 PESTTTSPTLNTTGFAAPNTTTgLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSP----------SP 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  798 SKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPlfSPGGQPAPCGSQASWTKSQNPDPFADlgDLSSGLQDPQAQST 877
Cdd:pfam05109  495 RDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTP--TPNATSPTLGKTSPTSAVTTPTPNAT--SPTPAVTTPTPNAT 570

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596344  878 VSPRGQRVCTCSRRLPT-GKLKPGVADTGTAASPHRHC-GSPAGFPPGGFIPKTATT 932
Cdd:pfam05109  571 IPTLGKTSPTSAVTTPTpNATSPTVGETSPQANTTNHTlGGTSSTPVVTSPPKNATS 627
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
 2-100 1.12e-03

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: 42.16  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNfpiGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPE 77
Cdd:cd14117    170 YLPPEMIEGRTH---DEKVDLWCIGVLCYELLVGMPPFESASHTetyrRIVKVDLKFPPFLSDGS--RDLISKLLRYHPS 244

                           90       100
                   ....*....|....*....|...
gi 2462596344   78 ERLSIAEVVHQLQEIAAARNVNP 100
Cdd:cd14117    245 ERLPLKGVMEHPWVKANSRRVLP 267
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 1-84 1.18e-03

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: 41.82  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    1 MYRTPEIIdLYSNFpiGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPPHDTQYTVFH--SLIRAMLQV 74
Cdd:cd14009    159 LYMAPEIL-QFQKY--DAKADLWSVGAILFEMLVGKPPFRGSNHVqllrNIERSDAVIPFPIAAQLSPDckDLLRRLLRR 235

                           90
                   ....*....|
gi 2462596344   75 NPEERLSIAE 84
Cdd:cd14009    236 DPAERISFEE 245
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 2-84 1.24e-03

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: 42.00  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDlYSNFPIGEKQDIWALGCILYLLCFRQHPFED----GAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPE 77
Cdd:cd06632    167 WMAPEVIM-QKNSGYGLAVDIWSLGCTVLEMATGKPPWSQyegvAAIFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDPE 245


                   ....*..
gi 2462596344   78 ERLSIAE 84
Cdd:cd06632    246 DRPTASQ 252
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 728-923 1.28e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  728 GGPPAAADPFGPLLPSSGNNSQPCSNPDlfgeflnSDSVTVPPSFPSAHSAP-PPSCSADFLHLGDLPGEPSKMTASSSN 806
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPA-------APAAPAAPAAPAPAGAAaAPAEASAAPAPGVAAPEHHPKHVAVPD 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  807 P-DLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPdpfadlGDLSSGLQDPQAQSTVSPRgQRV 885
Cdd:PRK07764   662 AsDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG------QADDPAAQPPQAAQGASAP-SPA 734

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462596344  886 CTCSRRLPTGKLKPGVADTGTAASPHRHCGSPAGFPPG 923
Cdd:PRK07764   735 ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 2-85 1.29e-03

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: 41.89  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdLYSNFPiGEKQDIWALGCILYLLCFRQHPFEDGAK--------LRIVNGKYSIPPHDTQYTVFHSLIRAMLQ 73
Cdd:cd14665    163 YIAPEVL-LKKEYD-GKIADVWSCGVTLYVMLVGAYPFEDPEEprnfrktiQRILSVQYSIPDYVHISPECRHLISRIFV 240

                           90
                   ....*....|..
gi 2462596344   74 VNPEERLSIAEV 85
Cdd:cd14665    241 ADPATRITIPEI 252
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
 21-88 1.31e-03

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: 42.31  E-value: 1.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596344   21 DIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ 88
Cdd:cd14178    183 DIWSLGILLYTMLAGFTPFANGPDdtpeeilARIGSGKYALSGGnwDSISDAAKDIVSKMLHVDPHQRLTAPQVLRH 259
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
 18-88 1.40e-03

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: 41.94  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   18 EKQDIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVVHQ 88
Cdd:cd14175    178 EGCDIWSLGILLYTMLAGYTPFANGPSdtpeeilTRIGSGKFTLSGGnwNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQH 257
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
667-849 1.45e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  667 GAGPAVPPQACKAPSSNTdllscllGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPfgpllPSSGN 746
Cdd:PRK07003   370 GGVPARVAGAVPAPGARA-------AAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAP-----PATAD 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344  747 NSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAP 826
Cdd:PRK07003   438 RGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517

                          170       180
                   ....*....|....*....|...
gi 2462596344  827 TPATEGPLFSPGGQPAPCGSQAS 849
Cdd:PRK07003   518 REDAPAAAAPPAPEARPPTPAAA 540
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 2-86 1.98e-03

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: 41.44  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIID--LYSNFP-IGEKQDIWALGCILYLLCFRQHPF---EDGAKLR-IVNGKYSI--PPHDTQYTVFHSLIRAML 72
Cdd:cd14182    175 YLAPEIIEcsMDDNHPgYGKEVDMWSTGVIMYTLLAGSPPFwhrKQMLMLRmIMSGNYQFgsPEWDDRSDTVKDLISRFL 254

                           90
                   ....*....|....
gi 2462596344   73 QVNPEERLSIAEVV 86
Cdd:cd14182    255 VVQPQKRYTAEEAL 268
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 2-84 2.06e-03

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: 41.18  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDlySNFPIGE-----KQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKY---------SIPPhDTQytVFHSL 67
Cdd:cd13993    171 YMAPECFD--EVGRSLKgypcaAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYylnspnlfdVILP-MSD--DFYNL 245

                           90
                   ....*....|....*..
gi 2462596344   68 IRAMLQVNPEERLSIAE 84
Cdd:cd13993    246 LRQIFTVNPNNRILLPE 262
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 21-88 2.23e-03

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: 41.56  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   21 DIWALGCILYLLCFRQHPF--------EDGAKLRIVNGKYSIPphDTQYTVF----HSLIRAMLQVNPEERLSIAEVVHQ 88
Cdd:cd14170    185 DMWSLGVIMYILLCGYPPFysnhglaiSPGMKTRIRMGQYEFP--NPEWSEVseevKMLIRNLLKTEPTQRMTITEFMNH 262
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 21-88 2.55e-03

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: 41.13  E-value: 2.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596344   21 DIWALGCILYLLCFRQHPF--------EDGAKLRIVNGKYSIP-PHDTQYTV-FHSLIRAMLQVNPEERLSIAEVVHQ 88
Cdd:cd14172    187 DMWSLGVIMYILLCGFPPFysntgqaiSPGMKRRIRMGQYGFPnPEWAEVSEeAKQLIRHLLKTDPTERMTITQFMNH 264
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1080-1119 2.83e-03

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 38.16  E-value: 2.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462596344 1080 PEQVKRHYRRAVLAVHPDKAAGQPyeQHAKMIFMELNDAW 1119
Cdd:COG2214     19 LEEIRQAYRRLAKLLHPDRGGELK--ALAEELFQRLNEAY 56
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
 21-86 3.16e-03

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: 41.16  E-value: 3.16e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596344   21 DIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVV 86
Cdd:cd14176    199 DIWSLGVLLYTMLTGYTPFANGPDdtpeeilARIGSGKFSLSGGywNSVSDTAKDLVSKMLHVDPHQRLTAALVL 273
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 17-85 3.30e-03

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: 40.68  E-value: 3.30e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596344   17 GEKQDIWALGCILYLLCFRQHPFEDgaKLRIVNGKYSIPPHDTqyTVFHSLIRAMLQVNPEERLSIAEV 85
Cdd:cd14005    185 GRPATVWSLGILLYDMLCGDIPFEN--DEQILRGNVLFRPRLS--KECCDLISRCLQFDPSKRPSLEQI 249
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
 2-81 3.41e-03

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: 40.70  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDL-YSNFPIgekqDIWALGCILYLLCFRQHPFE-------DGAKLRIVNGKYSIPPHDTQYTVfhSLIRAMLQ 73
Cdd:cd05578    165 YMAPEVFMRaGYSFAV----DWWSLGVTAYEMLRGKRPYEihsrtsiEEIRAKFETASVLYPAGWSEEAI--DLINKLLE 238


                   ....*...
gi 2462596344   74 VNPEERLS 81
Cdd:cd05578    239 RDPQKRLG 246
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 2-84 3.67e-03

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: 41.12  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIdlySNFPIGEKQDIWALGCILYLLCFRQHPFED----GAKLRIVNGKYS--IPPHDTQYTVFHSLIRAMLqVN 75
Cdd:cd05573    196 YIAPEVL---RGTGYGPECDWWSLGVILYEMLYGFPPFYSdslvETYSKIMNWKESlvFPDDPDVSPEAIDLIRRLL-CD 271


                   ....*....
gi 2462596344   76 PEERLSIAE 84
Cdd:cd05573    272 PEDRLGSAE 280
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 2-86 3.76e-03

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: 40.33  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNfpiGEKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPPHDTQYTvfHSLIRAMLQVNPE 77
Cdd:cd14116    169 YLPPEMIEGRMH---DEKVDLWSLGVLCYEFLVGKPPFEANTYqetyKRISRVEFTFPDFVTEGA--RDLISRLLKHNPS 243


                   ....*....
gi 2462596344   78 ERLSIAEVV 86
Cdd:cd14116    244 QRPMLREVL 252
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
 21-100 4.22e-03

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: 40.38  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344   21 DIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPPH--DTQYTVFHSLIRAMLQVNPEERLSIAEVVHqlQE 91
Cdd:cd14177    184 DIWSLGVLLYTMLAGYTPFANGPNdtpeeilLRIGSGKFSLSGGnwDTVSDAAKDLLSHMLHVDPHQRYTAEQVLK--HS 261


                   ....*....
gi 2462596344   92 IAAARNVNP 100
Cdd:cd14177    262 WIACRDQLP 270
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 2-116 5.03e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 40.77  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEiidLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPPHDTQYTVfHSLIRAMLQVNPE 77
Cdd:PTZ00267   237 YLAPE---LWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQqvlyGKYDPFPCPVSSGM-KALLDPLLSKNPA 312

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462596344   78 ERLSIAEVVHQ---------LQEIAAARNVNPKSPITELLEQNGGYGS 116
Cdd:PTZ00267   313 LRPTTQQLLHTeflkyvanlFQDIVRHSETISPHDREEILRQLQESGE 360
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 2-84 5.45e-03

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 39.87  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEII--DLYSNFPIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYS-IPPHDTQYTV-FHSLIRAMLQ 73
Cdd:cd14107    160 YGSPEFVapEIVHQEPVSAATDIWALGVIAYLSLTCHSPFagenDRATLLNVAEGVVSwDTPEITHLSEdAKDFIKRVLQ 239

                           90
                   ....*....|.
gi 2462596344   74 VNPEERLSIAE 84
Cdd:cd14107    240 PDPEKRPSASE 250
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 21-86 6.28e-03

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: 39.98  E-value: 6.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596344   21 DIWALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPPHdTQYTVFH-----SLIRAMLQVNPEERLSIAEVV 86
Cdd:cd13994    185 DVWSCGIVLFALFTGRFPWrsakksDSAYKAYEKSGDFTNGPY-EPIENLLpsecrRLIYRMLHPDPEKRITIDEAL 260
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 2-85 7.21e-03

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: 39.98  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDLYSNFP-IGEKQDIWALGCILYLLCFRQHPFEDGAKL--------RIVNGKYSIppHDTQYTVF----HSLI 68
Cdd:cd14092    167 YAAPEVLKQALSTQgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaeimkRIKSGDFSF--DGEEWKNVsseaKSLI 244

                           90
                   ....*....|....*..
gi 2462596344   69 RAMLQVNPEERLSIAEV 85
Cdd:cd14092    245 QGLLTVDPSKRLTMSEL 261
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 2-84 9.62e-03

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 39.27  E-value: 9.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596344    2 YRTPEIIDlySNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHdtqytvFHSLIRAMLQVNPEERLS 81
Cdd:cd14012    174 WLPPELAQ--GSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLDLSAS------LQDFLSKCLSLDPKKRPT 245


                   ...
gi 2462596344   82 IAE 84
Cdd:cd14012    246 ALE 248
 
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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