MULTISPECIES: J domain-containing protein [Bacteria]
J domain-containing protein( domain architecture ID 11422315)
J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70
List of domain hits
Name | Accession | Description | Interval | E-value | ||
DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
9-50 | 2.05e-07 | ||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 47.77 E-value: 2.05e-07
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Name | Accession | Description | Interval | E-value | ||
DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
9-50 | 2.05e-07 | ||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 47.77 E-value: 2.05e-07
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
9-50 | 2.41e-07 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 49.03 E-value: 2.41e-07
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
9-50 | 2.86e-07 | ||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 45.30 E-value: 2.86e-07
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
9-47 | 1.13e-06 | ||
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: 43.69 E-value: 1.13e-06
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
9-50 | 3.15e-06 | ||
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 42.46 E-value: 3.15e-06
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Name | Accession | Description | Interval | E-value | ||
DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
9-50 | 2.05e-07 | ||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 47.77 E-value: 2.05e-07
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
9-50 | 2.41e-07 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 49.03 E-value: 2.41e-07
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
9-50 | 2.86e-07 | ||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 45.30 E-value: 2.86e-07
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
9-47 | 1.13e-06 | ||
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: 43.69 E-value: 1.13e-06
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
11-50 | 1.29e-06 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 46.68 E-value: 1.29e-06
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
11-58 | 1.57e-06 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 46.81 E-value: 1.57e-06
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
9-59 | 2.60e-06 | ||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 45.97 E-value: 2.60e-06
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
9-50 | 3.15e-06 | ||
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 42.46 E-value: 3.15e-06
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
11-50 | 3.47e-06 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 45.46 E-value: 3.47e-06
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
11-47 | 3.59e-06 | ||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 45.37 E-value: 3.59e-06
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
9-73 | 6.70e-06 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 44.54 E-value: 6.70e-06
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
5-50 | 9.97e-06 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 44.37 E-value: 9.97e-06
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
11-45 | 1.06e-05 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 44.41 E-value: 1.06e-05
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
11-50 | 1.54e-05 | ||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 43.62 E-value: 1.54e-05
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
11-58 | 1.68e-05 | ||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 43.56 E-value: 1.68e-05
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
9-50 | 3.81e-05 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 42.52 E-value: 3.81e-05
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
5-58 | 4.98e-05 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 42.14 E-value: 4.98e-05
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
11-63 | 4.99e-05 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 42.28 E-value: 4.99e-05
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
9-50 | 1.13e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 41.19 E-value: 1.13e-04
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
9-62 | 1.72e-04 | ||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 40.58 E-value: 1.72e-04
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
11-54 | 1.76e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 40.50 E-value: 1.76e-04
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
9-58 | 3.13e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 39.99 E-value: 3.13e-04
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
9-50 | 3.70e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 39.75 E-value: 3.70e-04
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
11-58 | 3.99e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 39.59 E-value: 3.99e-04
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
4-58 | 6.45e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 39.16 E-value: 6.45e-04
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
9-45 | 7.27e-04 | ||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 36.31 E-value: 7.27e-04
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
12-58 | 8.64e-04 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 38.46 E-value: 8.64e-04
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
11-59 | 1.05e-03 | ||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 38.52 E-value: 1.05e-03
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
9-66 | 1.06e-03 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 38.24 E-value: 1.06e-03
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
5-57 | 1.27e-03 | ||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 38.29 E-value: 1.27e-03
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PHA03102 | PHA03102 | Small T antigen; Reviewed |
9-59 | 1.84e-03 | ||
Small T antigen; Reviewed Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 36.96 E-value: 1.84e-03
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
11-50 | 3.14e-03 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 37.11 E-value: 3.14e-03
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Blast search parameters | ||||
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