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Conserved domains on  [gi|1207188301|ref|XP_021327454|]
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auxilin isoform X8 [Danio rerio]

Protein Classification

cyclin-G-associated kinase( domain architecture ID 13212238)

cyclin-G-associated kinase (GAK) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2, and associates with cyclin G and CDK5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1-71 1.18e-45

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member cd14563:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 163  Bit Score: 160.82  E-value: 1.18e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYVCSL 71
Cdd:cd14563    93 MHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYICDL 163
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 79-214 5.97e-30

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: 115.07  E-value: 5.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  79 PHSKPLVIKTVTISPVPCFNKQrSGCRPFCDVLIGETKIFSTAQEYERMREHRIQEGKVVFPVGVSAQGDVVISVYHMRS 158
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207188301 159 HALQAKVtntqIFQIQFHTGFIApgSTVLKFMKTELDACDSP---EKYPQLFHVLIDIE 214
Cdd:pfam10409  80 DLLSEEK----MFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 721-762 3.92e-09

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: 52.93  E-value: 3.92e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207188301 721 TPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWS 762
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYE 51
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 332-636 5.20e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  332 DGDAAKIPPSSPQP-----------PANNTTTDLLGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQ 383
Cdd:PHA03247  2606 GDPRGPAPPSPLPPdthapdppppsPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  384 SSSPGPSPRSGNTFDPFGSGPAPAPKPQDFMGAF---LGPGNMGQPDPFLHAARSPSPTMqnmgmgrSSPVPPSTPTVNI 460
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPAVP-------AGPATPGGPARPA 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  461 QQQNSTGAwewnkPAAAGGGFGMGSKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTG 540
Cdd:PHA03247  2759 RPPTTAGP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  541 GAfpPMGSPQRPAPSPQHTASGGWhpntgfpsWQAGGGAQWQPQAQGTPTKapPASMPHTSPQNRPNYNVSFSAMSGASP 620
Cdd:PHA03247  2834 AQ--PTAPPPPPGPPPPSLPLGGS--------VAPGGDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALP 2901

                          330
                   ....*....|....*..
gi 1207188301  621 -GAAGPKAQPNMGTRPK 636
Cdd:PHA03247  2902 pDQPERPPQPQAPPPPQ 2918
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 1-71 1.18e-45

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: 160.82  E-value: 1.18e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYVCSL 71
Cdd:cd14563    93 MHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYICDL 163
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 79-214 5.97e-30

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: 115.07  E-value: 5.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  79 PHSKPLVIKTVTISPVPCFNKQrSGCRPFCDVLIGETKIFSTAQEYERMREHRIQEGKVVFPVGVSAQGDVVISVYHMRS 158
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207188301 159 HALQAKVtntqIFQIQFHTGFIApgSTVLKFMKTELDACDSP---EKYPQLFHVLIDIE 214
Cdd:pfam10409  80 DLLSEEK----MFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 721-762 3.92e-09

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: 52.93  E-value: 3.92e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207188301 721 TPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWS 762
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
721-762 1.57e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.77  E-value: 1.57e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207188301  721 TPEQVKKVYRKAVLVVHPDKATGQPYEqyAKMIFMELNDAWS 762
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYE 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
 332-636 5.20e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  332 DGDAAKIPPSSPQP-----------PANNTTTDLLGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQ 383
Cdd:PHA03247  2606 GDPRGPAPPSPLPPdthapdppppsPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  384 SSSPGPSPRSGNTFDPFGSGPAPAPKPQDFMGAF---LGPGNMGQPDPFLHAARSPSPTMqnmgmgrSSPVPPSTPTVNI 460
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPAVP-------AGPATPGGPARPA 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  461 QQQNSTGAwewnkPAAAGGGFGMGSKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTG 540
Cdd:PHA03247  2759 RPPTTAGP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  541 GAfpPMGSPQRPAPSPQHTASGGWhpntgfpsWQAGGGAQWQPQAQGTPTKapPASMPHTSPQNRPNYNVSFSAMSGASP 620
Cdd:PHA03247  2834 AQ--PTAPPPPPGPPPPSLPLGGS--------VAPGGDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALP 2901

                          330
                   ....*....|....*..
gi 1207188301  621 -GAAGPKAQPNMGTRPK 636
Cdd:PHA03247  2902 pDQPERPPQPQAPPPPQ 2918
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 721-762 1.02e-05

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


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 43.62  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207188301 721 TPEQVKKVYRKAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 762
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
720-761 1.61e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207188301 720 VTPEQVKKVYRKAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 761
Cdd:COG1076    16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 1-71 1.18e-45

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: 160.82  E-value: 1.18e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYVCSL 71
Cdd:cd14563    93 MHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYICDL 163
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 1-71 1.31e-30

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: 118.22  E-value: 1.31e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYVCSL 71
Cdd:cd14511    94 IYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYYFSDI 164
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 79-214 5.97e-30

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: 115.07  E-value: 5.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  79 PHSKPLVIKTVTISPVPCFNKQrSGCRPFCDVLIGETKIFSTAQEYERMREHRIQEGKVVFPVGVSAQGDVVISVYHMRS 158
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207188301 159 HALQAKVtntqIFQIQFHTGFIApgSTVLKFMKTELDACDSP---EKYPQLFHVLIDIE 214
Cdd:pfam10409  80 DLLSEEK----MFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 1-71 4.58e-26

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: 104.99  E-value: 4.58e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYVCSL 71
Cdd:cd14564    93 MHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDM 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1-71 1.26e-16

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: 77.62  E-value: 1.26e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLW----PSHRRYIGYVCSL 71
Cdd:cd14497    86 IDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPgvtiPSQLRYLQYFERL 160
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 721-762 3.92e-09

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: 52.93  E-value: 3.92e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207188301 721 TPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWS 762
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYE 51
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 1-67 4.71e-09

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: 56.06  E-value: 4.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRP--GSGL-WPSHRRYIGY 67
Cdd:cd14509    85 VDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTknKKGVtIPSQRRYVYY 154
DnaJ smart00271
DnaJ molecular chaperone homology domain;
721-762 1.57e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.77  E-value: 1.57e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207188301  721 TPEQVKKVYRKAVLVVHPDKATGQPYEqyAKMIFMELNDAWS 762
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYE 53
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 1-71 1.44e-06

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: 48.92  E-value: 1.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKR-----PGSGLWPSHRRYIGYVCSL 71
Cdd:cd14508    84 MDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRfyddkVGPLGQPSQKRYVGYFSGL 159
PHA03247 PHA03247
large tegument protein UL36; Provisional
 332-636 5.20e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  332 DGDAAKIPPSSPQP-----------PANNTTTDLLGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQ 383
Cdd:PHA03247  2606 GDPRGPAPPSPLPPdthapdppppsPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  384 SSSPGPSPRSGNTFDPFGSGPAPAPKPQDFMGAF---LGPGNMGQPDPFLHAARSPSPTMqnmgmgrSSPVPPSTPTVNI 460
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPAVP-------AGPATPGGPARPA 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  461 QQQNSTGAwewnkPAAAGGGFGMGSKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTG 540
Cdd:PHA03247  2759 RPPTTAGP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  541 GAfpPMGSPQRPAPSPQHTASGGWhpntgfpsWQAGGGAQWQPQAQGTPTKapPASMPHTSPQNRPNYNVSFSAMSGASP 620
Cdd:PHA03247  2834 AQ--PTAPPPPPGPPPPSLPLGGS--------VAPGGDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALP 2901

                          330
                   ....*....|....*..
gi 1207188301  621 -GAAGPKAQPNMGTRPK 636
Cdd:PHA03247  2902 pDQPERPPQPQAPPPPQ 2918
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 721-762 1.02e-05

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


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 43.62  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207188301 721 TPEQVKKVYRKAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 762
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 3-71 1.26e-05

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: 46.20  E-value: 1.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207188301   3 NWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLW--------PSHRRYIGYVCSL 71
Cdd:cd14510   101 EWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPSQSRYVGYFEKL 177
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 1-71 1.41e-05

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: 46.09  E-value: 1.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKR-----PGSGLWPSHRRYIGYVCSL 71
Cdd:cd14562    84 METWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfcedkVATSLQPSQRRYISYFGGL 159
PHA03247 PHA03247
large tegument protein UL36; Provisional
 333-635 7.86e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 7.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  333 GDAAKIPPSSPQPPANNTTTdllgdlfgapPTPQPASCPG--SAQSTPRRSAQSSSPGPSPRSGNTFDPFGSGPAPAPKP 410
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSV----------PPPRPAPRPSepAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  411 QDfmgaflgpgnMGQPDPflhAARSPSPTMQNMGMGRSSPVPPSTptvniQQQNSTGAWEWNKPAAAGGGFGMGSKSAST 490
Cdd:PHA03247  2619 PD----------THAPDP---PPPSPSPAANEPDPHPPPTVPPPE-----RPRDDPAPGRVSRPRRARRLGRAAQASSPP 2680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  491 SPTSSAHGTPTHQTKPNTLDPfADLGNLGAGLGGGGSGFSSKPTTPTGTGGAFPPmgSPQRPAPSPQHTAsggwhpntgf 570
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP-PPPPPTPEPAPHALVSATPLPPGPAAARQASPA--LPAAPAPPAVPAG---------- 2747

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207188301  571 PSWQAGGGAQWQPQAQGTPTKAPPASMPHTSPQNR--PNYNVSFSAMSGASPGAAGPKAQPNMGTRP 635
Cdd:PHA03247  2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRltRPAVASLSESRESLPSPWDPADPPAAVLAP 2814
PHA03247 PHA03247
large tegument protein UL36; Provisional
 340-616 7.92e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  340 PSSPQPPANNTTTDLLGDLFGAPPTPQPASCPGSAQSTPRRSAQSSSPGPSPRSgntfDPFGSGPAPAPKPQDFMGAFLG 419
Cdd:PHA03247  2720 PLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA----APAAGPPRRLTRPAVASLSESR 2795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  420 PGNMGQPDPFLHAARSPSPTMQNMGMGR----------SSPVPPSTPTVNIQQQNSTGAW-----EWNKPAAAGGGFGMG 484
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASpagplppptsAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKP 2875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  485 SKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTgGAFPPMGSPQRPAPsPQHTASGGW 564
Cdd:PHA03247  2876 AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPPLA-PTTDPAGAG 2953

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207188301  565 HPNTGFPSWQAGGGAQWQPQAQGTPTKAPPASMPHTSPQNRPNYNVSFSAMS 616
Cdd:PHA03247  2954 EPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
720-761 1.61e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207188301 720 VTPEQVKKVYRKAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 761
Cdd:COG1076    16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 1-71 1.98e-03

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: 39.54  E-value: 1.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207188301   1 MYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAK-----RPGSGLWPSHRRYIGYVCSL 71
Cdd:cd14561    84 MESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKkfyddKVSALMQPSQKRYVQFLSGL 159
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
721-761 3.80e-03

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 37.39  E-value: 3.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1207188301 721 TPEQVKKVYRKAVLVVHPDkaTGQPYEQYAKMIFMELNDAW 761
Cdd:COG2214    18 SLEEIRQAYRRLAKLLHPD--RGGELKALAEELFQRLNEAY 56
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 711-771 3.95e-03

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 36.13  E-value: 3.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207188301 711 WKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFESQGQKA 771
Cdd:COG5407     3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP---KAEERFKEINEAYELLSDAEKRA 60
PHA03247 PHA03247
large tegument protein UL36; Provisional
 338-638 4.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 4.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  338 IPPSSPQPPANNTTTDLLGDLFGAPPTPQPASCPGSAQSTPRRSAQSSSPGPSPRSGN---------TFDPFGSGPAPAP 408
Cdd:PHA03247  2568 VPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDppppspspaANEPDPHPPPTVP 2647

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  409 KPQDFMGAfLGPGNMGQPDPFLHAARSPSPTMQNMGMGRSSPVPPSTPTVNIQQQNSTGAWEwnKPAAAGGGFGMGSKSA 488
Cdd:PHA03247  2648 PPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP--EPAPHALVSATPLPPG 2724

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  489 STSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTGGAFPPMGSPQRPAPSPQHTASGGWHPNT 568
Cdd:PHA03247  2725 PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP 2804

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188301  569 GFPSWQAGGGAQWQPQAQG-TPTKAPPASMPHTSPQNRPNYNVSFSAMSGA-SPG--------AAGPKAQPNMGTRPKVS 638
Cdd:PHA03247  2805 ADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvAPGgdvrrrppSRSPAAKPAAPARPPVR 2884
 
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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