dnaJ homolog subfamily C member 14 [Rattus norvegicus]
DnaJ homolog subfamily C member 14( domain architecture ID 10446388)
DnaJ homolog subfamily C member 14 (DNAJC14) regulates the export of target proteins, such as dopamine D1 receptor (DRD1), from the endoplasmic reticulum to the cell surface
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Jiv90 | pfam14901 | Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ... |
533-621 | 5.70e-46 | |||
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown. : Pssm-ID: 464360 Cd Length: 92 Bit Score: 158.28 E-value: 5.70e-46
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
444-505 | 1.21e-22 | |||
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: 91.38 E-value: 1.21e-22
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Name | Accession | Description | Interval | E-value | |||
Jiv90 | pfam14901 | Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ... |
533-621 | 5.70e-46 | |||
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown. Pssm-ID: 464360 Cd Length: 92 Bit Score: 158.28 E-value: 5.70e-46
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
444-505 | 1.21e-22 | |||
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: 91.38 E-value: 1.21e-22
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
444-516 | 3.62e-20 | |||
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: 87.07 E-value: 3.62e-20
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
444-500 | 1.48e-17 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 76.89 E-value: 1.48e-17
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
444-497 | 1.54e-16 | |||
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: 74.12 E-value: 1.54e-16
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
448-504 | 4.12e-15 | |||
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family. Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 77.26 E-value: 4.12e-15
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
446-508 | 5.57e-14 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 74.11 E-value: 5.57e-14
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
446-505 | 1.45e-11 | |||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 67.15 E-value: 1.45e-11
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Name | Accession | Description | Interval | E-value | |||
Jiv90 | pfam14901 | Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ... |
533-621 | 5.70e-46 | |||
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown. Pssm-ID: 464360 Cd Length: 92 Bit Score: 158.28 E-value: 5.70e-46
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
444-505 | 1.21e-22 | |||
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: 91.38 E-value: 1.21e-22
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
444-516 | 3.62e-20 | |||
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: 87.07 E-value: 3.62e-20
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SEC63 | COG5407 | Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
444-503 | 2.44e-19 | |||
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 81.97 E-value: 2.44e-19
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
444-500 | 1.48e-17 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 76.89 E-value: 1.48e-17
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
441-504 | 7.97e-17 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 75.91 E-value: 7.97e-17
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
444-497 | 1.54e-16 | |||
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: 74.12 E-value: 1.54e-16
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
448-504 | 4.12e-15 | |||
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family. Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 77.26 E-value: 4.12e-15
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
446-508 | 5.57e-14 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 74.11 E-value: 5.57e-14
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
446-505 | 1.77e-13 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 72.57 E-value: 1.77e-13
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
446-506 | 3.03e-13 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 72.11 E-value: 3.03e-13
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
446-505 | 3.15e-13 | |||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 71.79 E-value: 3.15e-13
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PRK14279 | PRK14279 | molecular chaperone DnaJ; |
449-509 | 6.03e-13 | |||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 71.30 E-value: 6.03e-13
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
448-504 | 9.09e-13 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 70.17 E-value: 9.09e-13
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
446-519 | 1.01e-12 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 70.24 E-value: 1.01e-12
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
446-505 | 1.25e-12 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 70.12 E-value: 1.25e-12
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
446-505 | 3.07e-12 | |||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 68.66 E-value: 3.07e-12
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
448-506 | 4.62e-12 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 68.16 E-value: 4.62e-12
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
446-505 | 1.45e-11 | |||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 67.15 E-value: 1.45e-11
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
446-505 | 1.51e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 66.75 E-value: 1.51e-11
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
446-505 | 1.69e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 66.76 E-value: 1.69e-11
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
446-505 | 2.98e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 64.96 E-value: 2.98e-11
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
446-505 | 4.97e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 65.01 E-value: 4.97e-11
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
446-505 | 6.15e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 64.65 E-value: 6.15e-11
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
446-505 | 8.78e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 64.38 E-value: 8.78e-11
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PRK10266 | PRK10266 | curved DNA-binding protein; |
446-513 | 1.37e-10 | |||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 62.92 E-value: 1.37e-10
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
446-505 | 1.75e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 63.37 E-value: 1.75e-10
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
446-505 | 2.26e-10 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 62.82 E-value: 2.26e-10
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
446-505 | 2.85e-10 | |||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 62.70 E-value: 2.85e-10
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
444-502 | 3.73e-10 | |||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 56.34 E-value: 3.73e-10
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
446-505 | 4.42e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 61.87 E-value: 4.42e-10
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
446-537 | 4.44e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 62.17 E-value: 4.44e-10
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
446-505 | 1.62e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 60.19 E-value: 1.62e-09
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
446-505 | 1.63e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 60.35 E-value: 1.63e-09
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
446-505 | 2.01e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 59.78 E-value: 2.01e-09
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
446-505 | 3.28e-09 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 59.45 E-value: 3.28e-09
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
446-505 | 3.51e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 59.26 E-value: 3.51e-09
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
446-505 | 2.49e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 53.46 E-value: 2.49e-07
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
442-527 | 6.26e-06 | |||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 48.92 E-value: 6.26e-06
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djlA | PRK09430 | co-chaperone DjlA; |
446-475 | 1.66e-04 | |||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 44.03 E-value: 1.66e-04
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Blast search parameters | ||||
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