TM2 and DnaJ domain-containing protein wurst [Bombyx mori]
J domain-containing protein( domain architecture ID 11155597)
J domain-containing protein containing a similar domain as 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 | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
286-349 | 1.13e-20 | ||
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: 84.45 E-value: 1.13e-20
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TM2 | pfam05154 | TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a ... |
6-55 | 4.93e-12 | ||
TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts. : Pssm-ID: 428337 Cd Length: 50 Bit Score: 60.20 E-value: 4.93e-12
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Name | Accession | Description | Interval | E-value | ||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
286-349 | 1.13e-20 | ||
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: 84.45 E-value: 1.13e-20
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
286-343 | 1.23e-18 | ||
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: 78.74 E-value: 1.23e-18
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
285-345 | 2.62e-18 | ||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 77.66 E-value: 2.62e-18
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
286-348 | 3.28e-18 | ||
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: 80.13 E-value: 3.28e-18
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
284-348 | 7.89e-14 | ||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 71.80 E-value: 7.89e-14
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TM2 | pfam05154 | TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a ... |
6-55 | 4.93e-12 | ||
TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts. Pssm-ID: 428337 Cd Length: 50 Bit Score: 60.20 E-value: 4.93e-12
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TM2 | COG2314 | Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction ... |
1-76 | 2.61e-09 | ||
Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction only]; Pssm-ID: 441888 Cd Length: 79 Bit Score: 53.38 E-value: 2.61e-09
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PHA01886 | PHA01886 | TM2 domain-containing protein |
8-83 | 2.94e-08 | ||
TM2 domain-containing protein Pssm-ID: 222840 Cd Length: 78 Bit Score: 50.35 E-value: 2.94e-08
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Name | Accession | Description | Interval | E-value | |||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
286-349 | 1.13e-20 | |||
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: 84.45 E-value: 1.13e-20
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
286-343 | 1.23e-18 | |||
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: 78.74 E-value: 1.23e-18
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
285-345 | 2.62e-18 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 77.66 E-value: 2.62e-18
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
286-348 | 3.28e-18 | |||
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: 80.13 E-value: 3.28e-18
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SEC63 | COG5407 | Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
286-348 | 3.03e-17 | |||
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 75.04 E-value: 3.03e-17
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
283-345 | 3.39e-16 | |||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 72.52 E-value: 3.39e-16
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
284-348 | 2.41e-15 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 70.52 E-value: 2.41e-15
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
284-348 | 7.89e-14 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 71.80 E-value: 7.89e-14
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
288-348 | 1.78e-13 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 70.85 E-value: 1.78e-13
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
288-349 | 3.65e-12 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 66.67 E-value: 3.65e-12
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TM2 | pfam05154 | TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a ... |
6-55 | 4.93e-12 | |||
TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts. Pssm-ID: 428337 Cd Length: 50 Bit Score: 60.20 E-value: 4.93e-12
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
288-348 | 9.95e-12 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 65.56 E-value: 9.95e-12
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
288-347 | 1.61e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 64.81 E-value: 1.61e-11
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
283-348 | 2.84e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 64.05 E-value: 2.84e-11
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
284-347 | 3.83e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 63.57 E-value: 3.83e-11
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
288-348 | 5.53e-11 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 63.30 E-value: 5.53e-11
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
288-348 | 7.17e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 62.90 E-value: 7.17e-11
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
288-347 | 1.23e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 62.08 E-value: 1.23e-10
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
288-348 | 1.29e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 61.49 E-value: 1.29e-10
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
288-347 | 3.78e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 60.63 E-value: 3.78e-10
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
284-348 | 4.26e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 60.39 E-value: 4.26e-10
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
288-347 | 8.12e-10 | |||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 59.62 E-value: 8.12e-10
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PRK10266 | PRK10266 | curved DNA-binding protein; |
288-347 | 1.68e-09 | |||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 58.29 E-value: 1.68e-09
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djlA | PRK09430 | co-chaperone DjlA; |
260-345 | 1.83e-09 | |||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 57.90 E-value: 1.83e-09
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
288-348 | 2.35e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 58.02 E-value: 2.35e-09
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TM2 | COG2314 | Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction ... |
1-76 | 2.61e-09 | |||
Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction only]; Pssm-ID: 441888 Cd Length: 79 Bit Score: 53.38 E-value: 2.61e-09
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
288-348 | 2.89e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 57.85 E-value: 2.89e-09
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
288-348 | 3.58e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 57.53 E-value: 3.58e-09
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
288-347 | 5.84e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 57.16 E-value: 5.84e-09
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
288-349 | 8.10e-09 | |||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 56.72 E-value: 8.10e-09
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
288-355 | 2.14e-08 | |||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 55.22 E-value: 2.14e-08
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PHA01886 | PHA01886 | TM2 domain-containing protein |
8-83 | 2.94e-08 | |||
TM2 domain-containing protein Pssm-ID: 222840 Cd Length: 78 Bit Score: 50.35 E-value: 2.94e-08
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
288-347 | 1.27e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 52.97 E-value: 1.27e-07
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
288-347 | 2.92e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 51.67 E-value: 2.92e-07
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
284-348 | 4.57e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 51.10 E-value: 4.57e-07
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
284-347 | 6.29e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 50.78 E-value: 6.29e-07
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
284-355 | 7.70e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 50.38 E-value: 7.70e-07
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
285-347 | 1.95e-06 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 49.24 E-value: 1.95e-06
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
284-347 | 1.51e-05 | |||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 46.61 E-value: 1.51e-05
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ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
283-348 | 7.28e-05 | |||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 44.25 E-value: 7.28e-05
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Blast search parameters | ||||
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