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Conserved domains on  [gi|1207179073|ref|XP_021332834|]
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auxilin isoform X1 [Danio rerio]

Protein Classification

cyclin-G-associated kinase( domain architecture ID 12998533)

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_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 115-277 3.72e-118

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: 358.04  E-value: 3.72e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 115 VATYTKGELDIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQA 194
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 195 PSLHNLFAVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYV 274
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1207179073 275 CSL 277
Cdd:cd14563   161 CDL 163
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 285-420 7.77e-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: 7.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 285 PHSKPLVIKTVTISPVPCFNKQrSGCRPFCDVLIGETKIFSTAQEYERMREHRIQEGKVVFPVGVSAQGDVVISVYHMRS 364
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 365 HALQAKVtntqIFQIQFHTGFIApgSTVLKFMKTELDACDSP---EKYPQLFHVLIDIE 420
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 ...
 927-968 4.97e-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: 4.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207179073 927 TPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWS 968
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYE 51
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 538-842 1.08e-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: 53.02  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  538 DGDAAKIPPSSPQP-----------PANNTTTDLLGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQ 589
Cdd:PHA03247  2606 GDPRGPAPPSPLPPdthapdppppsPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  590 SSSPGPSPRSGNTFDPFGSGPAPAPKPQDFMGAF---LGPGNMGQPDPFLHAARSPSPTMqnmgmgrSSPVPPSTPTVNI 666
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPAVP-------AGPATPGGPARPA 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  667 QQQNSTGAwewnkPAAAGGGFGMGSKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTG 746
Cdd:PHA03247  2759 RPPTTAGP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  747 GAfpPMGSPQRPAPSPQHTASGGWhpntgfpsWQAGGGAQWQPQAQGTPTKapPASMPHTSPQNRPNYNVSFSAMSGASP 826
Cdd:PHA03247  2834 AQ--PTAPPPPPGPPPPSLPLGGS--------VAPGGDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALP 2901

                          330
                   ....*....|....*..
gi 1207179073  827 -GAAGPKAQPNMGTRPK 842
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 ...
 115-277 3.72e-118

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: 358.04  E-value: 3.72e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 115 VATYTKGELDIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQA 194
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 195 PSLHNLFAVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYV 274
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1207179073 275 CSL 277
Cdd:cd14563   161 CDL 163
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 285-420 7.77e-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: 7.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 285 PHSKPLVIKTVTISPVPCFNKQrSGCRPFCDVLIGETKIFSTAQEYERMREHRIQEGKVVFPVGVSAQGDVVISVYHMRS 364
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 365 HALQAKVtntqIFQIQFHTGFIApgSTVLKFMKTELDACDSP---EKYPQLFHVLIDIE 420
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 ...
 927-968 4.97e-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: 4.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207179073 927 TPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWS 968
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
927-968 1.99e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.77  E-value: 1.99e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207179073  927 TPEQVKKVYRKAVLVVHPDKATGQPYEqyAKMIFMELNDAWS 968
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYE 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
 538-842 1.08e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  538 DGDAAKIPPSSPQP-----------PANNTTTDLLGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQ 589
Cdd:PHA03247  2606 GDPRGPAPPSPLPPdthapdppppsPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  590 SSSPGPSPRSGNTFDPFGSGPAPAPKPQDFMGAF---LGPGNMGQPDPFLHAARSPSPTMqnmgmgrSSPVPPSTPTVNI 666
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPAVP-------AGPATPGGPARPA 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  667 QQQNSTGAwewnkPAAAGGGFGMGSKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTG 746
Cdd:PHA03247  2759 RPPTTAGP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  747 GAfpPMGSPQRPAPSPQHTASGGWhpntgfpsWQAGGGAQWQPQAQGTPTKapPASMPHTSPQNRPNYNVSFSAMSGASP 826
Cdd:PHA03247  2834 AQ--PTAPPPPPGPPPPSLPLGGS--------VAPGGDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALP 2901

                          330
                   ....*....|....*..
gi 1207179073  827 -GAAGPKAQPNMGTRPK 842
Cdd:PHA03247  2902 pDQPERPPQPQAPPPPQ 2918
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 927-968 1.29e-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: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207179073 927 TPEQVKKVYRKAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 968
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
926-967 2.05e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207179073 926 VTPEQVKKVYRKAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 967
Cdd:COG1076    16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 537-808 2.05e-03

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: 42.06  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 537 LDGDAAKIPPSSPQPPANNTTTD-------------LLGDLFGAPPTPQPASCPGSAQSTPrrsaqssspgPSPRSGNTF 603
Cdd:pfam03154 137 IDQDNRSTSPSIPSPQDNESDSDssaqqqilqtqppVLQAQSGAASPPSPPPPGTTQAATA----------GPTPSAPSV 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 604 DPFGSgPAPAPKPQDFMGAfLGPGNMGQPDPFLHAARSPSPTMQNMGMGRSSPvPPSTPTVNIQQQNSTGawewnkpaaa 683
Cdd:pfam03154 207 PPQGS-PATSQPPNQTQST-AAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPP-PSQVSPQPLPQPSLHG---------- 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 684 gggfgmgsksASTSPTSSAHGTPTHQTKPNTLDPFadlgnlgaglggggsgfsskPTTPTGTGGAFPPMGSPQRPAPSPQ 763
Cdd:pfam03154 274 ----------QMPPMPHSLQTGPSHMQHPVPPQPF--------------------PLTPQSSQSQVPPGPSPAAPGQSQQ 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1207179073 764 HTASggwhpntgfPSWQAGGGAQWQPQAQgtPTKAPPASMPHTSP 808
Cdd:pfam03154 324 RIHT---------PPSQSQLQSQQPPREQ--PLPPAPLSMPHIKP 357
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 115-277 3.72e-118

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: 358.04  E-value: 3.72e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 115 VATYTKGELDIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQA 194
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 195 PSLHNLFAVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYV 274
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1207179073 275 CSL 277
Cdd:cd14563   161 CDL 163
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 115-277 9.58e-86

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: 272.30  E-value: 9.58e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 115 VATYTKGELDIAYITSRIIVMSYPAETVEMGYR-NHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQ 193
Cdd:cd14511     1 QQSYARNDLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 194 APSLHNLFAVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGY 273
Cdd:cd14511    81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYY 160


                  ....
gi 1207179073 274 VCSL 277
Cdd:cd14511   161 FSDI 164
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 115-277 1.37e-79

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: 255.98  E-value: 1.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 115 VATYTKGELDIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQA 194
Cdd:cd14564     1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 195 PSLHNLFAVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLWPSHRRYIGYV 274
Cdd:cd14564    81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                  ...
gi 1207179073 275 CSL 277
Cdd:cd14564   161 CDM 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 124-277 1.48e-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: 1.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 124 DIAYITSRIIVMSYPAETV-EMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRG-AKFSNRVSECNWPSRQAPSLHNLF 201
Cdd:cd14497     1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 202 AVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLW----PSHRRYIGYVCSL 277
Cdd:cd14497    81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPgvtiPSQLRYLQYFERL 160
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 124-273 1.86e-42

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: 151.97  E-value: 1.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 124 DIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNL-SQRNYRGAKFSNRVSECNWPSRQAPSLHNLFA 202
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207179073 203 VCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRP--GSGL-WPSHRRYIGY 273
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTknKKGVtIPSQRRYVYY 154
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 124-277 4.08e-42

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: 151.00  E-value: 4.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 124 DIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQAPSLHNLFAV 203
Cdd:cd14508     1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 204 CKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKR-----PGSGLWPSHRRYIGYVCSL 277
Cdd:cd14508    81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRfyddkVGPLGQPSQKRYVGYFSGL 159
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 118-277 1.23e-34

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: 130.56  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 118 YTKGE--LDIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNL-SQRNYRGAKFSNRVSECNWPSRQA 194
Cdd:cd14510     7 YQKDGfdLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 195 PSLHNLFAVCKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKRPGSGLW--------PS 266
Cdd:cd14510    87 PTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPS 166

                         170
                  ....*....|.
gi 1207179073 267 HRRYIGYVCSL 277
Cdd:cd14510   167 QSRYVGYFEKL 177
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 285-420 7.77e-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: 7.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 285 PHSKPLVIKTVTISPVPCFNKQrSGCRPFCDVLIGETKIFSTAQEYERMREHRIQEGKVVFPVGVSAQGDVVISVYHMRS 364
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 365 HALQAKVtntqIFQIQFHTGFIApgSTVLKFMKTELDACDSP---EKYPQLFHVLIDIE 420
Cdd:pfam10409  80 DLLSEEK----MFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 124-277 3.30e-29

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: 114.27  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 124 DIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQAPSLHNLFAV 203
Cdd:cd14561     1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 204 CKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAK-----RPGSGLWPSHRRYIGYVCSL 277
Cdd:cd14561    81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKkfyddKVSALMQPSQKRYVQFLSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 124-277 9.65e-29

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: 112.73  E-value: 9.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 124 DIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQAPSLHNLFAV 203
Cdd:cd14562     1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 204 CKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAK-----RPGSGLWPSHRRYIGYVCSL 277
Cdd:cd14562    81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRkfcedKVATSLQPSQRRYISYFGGL 159
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 124-277 1.86e-27

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: 109.30  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 124 DIAYITSRIIVMSYPAETVEMGYRNHTEDIRSFLDSRHADHYTVFNLSQRNYRGAKFSNRVSECNWPSRQAPSLHNLFAV 203
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 204 CKNMYNWLKQNPKNVCVITCSDGRAPSGVLVCAMFCFCHLFANPVPAMQLLSAKR-------PGSGlwPSHRRYIGYVCS 276
Cdd:cd14560    81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRfyedkvvPVGQ--PSQKRYVHYFSG 158


                  .
gi 1207179073 277 L 277
Cdd:cd14560   159 L 159
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 927-968 4.97e-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: 4.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207179073 927 TPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWS 968
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
927-968 1.99e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.77  E-value: 1.99e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207179073  927 TPEQVKKVYRKAVLVVHPDKATGQPYEqyAKMIFMELNDAWS 968
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYE 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
 538-842 1.08e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  538 DGDAAKIPPSSPQP-----------PANNTTTDLLGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQ 589
Cdd:PHA03247  2606 GDPRGPAPPSPLPPdthapdppppsPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  590 SSSPGPSPRSGNTFDPFGSGPAPAPKPQDFMGAF---LGPGNMGQPDPFLHAARSPSPTMqnmgmgrSSPVPPSTPTVNI 666
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPAVP-------AGPATPGGPARPA 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  667 QQQNSTGAwewnkPAAAGGGFGMGSKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTG 746
Cdd:PHA03247  2759 RPPTTAGP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  747 GAfpPMGSPQRPAPSPQHTASGGWhpntgfpsWQAGGGAQWQPQAQGTPTKapPASMPHTSPQNRPNYNVSFSAMSGASP 826
Cdd:PHA03247  2834 AQ--PTAPPPPPGPPPPSLPLGGS--------VAPGGDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALP 2901

                          330
                   ....*....|....*..
gi 1207179073  827 -GAAGPKAQPNMGTRPK 842
Cdd:PHA03247  2902 pDQPERPPQPQAPPPPQ 2918
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 927-968 1.29e-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: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1207179073 927 TPEQVKKVYRKAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 968
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
PHA03247 PHA03247
large tegument protein UL36; Provisional
 539-841 2.12e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  539 GDAAKIPPSSPQPPANNTTTdllgdlfgapPTPQPASCPG--SAQSTPRRSAQSSSPGPSPRSGNTFDPFGSGPAPAPKP 616
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSV----------PPPRPAPRPSepAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  617 QDfmgaflgpgnMGQPDPflhAARSPSPTMQNMGMGRSSPVPPSTptvniQQQNSTGAWEWNKPAAAGGGFGMGSKSAST 696
Cdd:PHA03247  2619 PD----------THAPDP---PPPSPSPAANEPDPHPPPTVPPPE-----RPRDDPAPGRVSRPRRARRLGRAAQASSPP 2680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  697 SPTSSAHGTPTHQTKPNTLDPfADLGNLGAGLGGGGSGFSSKPTTPTGTGGAFPPmgSPQRPAPSPQHTAsggwhpntgf 776
Cdd:PHA03247  2681 QRPRRRAARPTVGSLTSLADP-PPPPPTPEPAPHALVSATPLPPGPAAARQASPA--LPAAPAPPAVPAG---------- 2747

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207179073  777 PSWQAGGGAQWQPQAQGTPTKAPPASMPHTSPQNR--PNYNVSFSAMSGASPGAAGPKAQPNMGTRP 841
Cdd:PHA03247  2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRltRPAVASLSESRESLPSPWDPADPPAAVLAP 2814
PHA03247 PHA03247
large tegument protein UL36; Provisional
 546-822 6.13e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  546 PSSPQPPANNTTTDLLGDLFGAPPTPQPASCPGSAQSTPRRSAQSSSPGPSPRSgntfDPFGSGPAPAPKPQDFMGAFLG 625
Cdd:PHA03247  2720 PLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA----APAAGPPRRLTRPAVASLSESR 2795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  626 PGNMGQPDPFLHAARSPSPTMQNMGMGR----------SSPVPPSTPTVNIQQQNSTGAW-----EWNKPAAAGGGFGMG 690
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASpagplppptsAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKP 2875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  691 SKSASTSPTSSAHGTPTHQTKPNTLDPFADLGNLGAGLGGGGSGFSSKPTTPTGTgGAFPPMGSPQRPAPsPQHTASGGW 770
Cdd:PHA03247  2876 AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPPLA-PTTDPAGAG 2953

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207179073  771 HPNTGFPSWQAGGGAQWQPQAQGTPTKAPPASMPHTSPQNRPNYNVSFSAMS 822
Cdd:PHA03247  2954 EPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005
PHA03247 PHA03247
large tegument protein UL36; Provisional
 545-844 1.95e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  545 PPSSPQPPANNTTTdllGDLFGAPPTPQPASCPG-----------------SAQSTPRRSAQSSSPGPSPRSGNTFDPFG 607
Cdd:PHA03247  2627 PPPSPSPAANEPDP---HPPPTVPPPERPRDDPApgrvsrprrarrlgraaQASSPPQRPRRRAARPTVGSLTSLADPPP 2703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  608 SGPAPAPKPQDFMGAFLGPgnmgqPDPFLHAARSPSPTMqnmgmgrsSPVPPSTPTvniqqqnstgawewnkpaaagggf 687
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLP-----PGPAAARQASPALPA--------APAPPAVPA------------------------ 2746

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  688 gmgsksastspTSSAHGTPTHQTKPNTldpfadlgnlgaglggggSGFSSKPTTPTGTGGAFPPMGSPQRPAPSPQHTAS 767
Cdd:PHA03247  2747 -----------GPATPGGPARPARPPT------------------TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073  768 GGWHPNTGFPSWQAGGGAQWQPQAQG-TPTKAPPASMPHTSPQNRPNYNVSFSAMSGA-SPG--------AAGPKAQPNM 837
Cdd:PHA03247  2798 LPSPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvAPGgdvrrrppSRSPAAKPAA 2877


                   ....*..
gi 1207179073  838 GTRPKVS 844
Cdd:PHA03247  2878 PARPPVR 2884
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
926-967 2.05e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207179073 926 VTPEQVKKVYRKAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 967
Cdd:COG1076    16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 537-808 2.05e-03

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: 42.06  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 537 LDGDAAKIPPSSPQPPANNTTTD-------------LLGDLFGAPPTPQPASCPGSAQSTPrrsaqssspgPSPRSGNTF 603
Cdd:pfam03154 137 IDQDNRSTSPSIPSPQDNESDSDssaqqqilqtqppVLQAQSGAASPPSPPPPGTTQAATA----------GPTPSAPSV 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 604 DPFGSgPAPAPKPQDFMGAfLGPGNMGQPDPFLHAARSPSPTMQNMGMGRSSPvPPSTPTVNIQQQNSTGawewnkpaaa 683
Cdd:pfam03154 207 PPQGS-PATSQPPNQTQST-AAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPP-PSQVSPQPLPQPSLHG---------- 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207179073 684 gggfgmgsksASTSPTSSAHGTPTHQTKPNTLDPFadlgnlgaglggggsgfsskPTTPTGTGGAFPPMGSPQRPAPSPQ 763
Cdd:pfam03154 274 ----------QMPPMPHSLQTGPSHMQHPVPPQPF--------------------PLTPQSSQSQVPPGPSPAAPGQSQQ 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1207179073 764 HTASggwhpntgfPSWQAGGGAQWQPQAQgtPTKAPPASMPHTSP 808
Cdd:pfam03154 324 RIHT---------PPSQSQLQSQQPPREQ--PLPPAPLSMPHIKP 357
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
927-967 4.87e-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: 4.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1207179073 927 TPEQVKKVYRKAVLVVHPDkaTGQPYEQYAKMIFMELNDAW 967
Cdd:COG2214    18 SLEEIRQAYRRLAKLLHPD--RGGELKALAEELFQRLNEAY 56
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 917-977 5.02e-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: 5.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207179073 917 WKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFESQGQKA 977
Cdd:COG5407     3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP---KAEERFKEINEAYELLSDAEKRA 60
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 188-261 7.11e-03

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 38.81  E-value: 7.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207179073 188 NWPSRQAP-SLHNLFAVCKNMYNWLKQNPKNVCVItCSDGRAPSGVLVCAMFCFCHLFANPVP----AMQLLSAKRPGS 261
Cdd:cd00047   111 GWPDHGVPsSPEDLLALVRRVRKEARKPNGPIVVH-CSAGVGRTGTFIAIDILLERLEAEGEVdvfeIVKALRKQRPGM 188
 
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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