DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana]
J domain-containing protein( domain architecture ID 1003637)
J domain-containing protein with protein disulfide isomerase (PDI) domain(s), similar to human DnaJ homolog subfamily C member 10 (also called ER-resident protein ERdj5) that is involved in the correct folding of proteins and degradation of misfolded proteins
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 ... |
27-88 | 1.22e-30 | ||||
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: 113.72 E-value: 1.22e-30
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PRK14289 super family | cl36358 | molecular chaperone DnaJ; |
27-204 | 1.90e-23 | ||||
molecular chaperone DnaJ; The actual alignment was detected with superfamily member PRK14289: Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 102.60 E-value: 1.90e-23
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Thioredoxin_like super family | cl00388 | Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ... |
435-558 | 5.32e-03 | ||||
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. The actual alignment was detected with superfamily member cd02983: Pssm-ID: 469754 Cd Length: 130 Bit Score: 37.33 E-value: 5.32e-03
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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 ... |
27-88 | 1.22e-30 | ||||
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: 113.72 E-value: 1.22e-30
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
27-180 | 6.20e-30 | ||||
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: 120.78 E-value: 6.20e-30
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
27-94 | 5.27e-29 | ||||
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: 112.10 E-value: 5.27e-29
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
27-100 | 7.90e-27 | ||||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 113.38 E-value: 7.90e-27
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
27-103 | 1.06e-26 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 112.10 E-value: 1.06e-26
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
27-204 | 1.90e-23 | ||||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 102.60 E-value: 1.90e-23
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
26-83 | 1.06e-22 | ||||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 91.53 E-value: 1.06e-22
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
27-80 | 1.28e-22 | ||||
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: 91.07 E-value: 1.28e-22
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P5_C | cd02983 | P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ... |
435-558 | 5.32e-03 | ||||
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI. Pssm-ID: 239281 Cd Length: 130 Bit Score: 37.33 E-value: 5.32e-03
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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 ... |
27-88 | 1.22e-30 | ||||
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: 113.72 E-value: 1.22e-30
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
27-180 | 6.20e-30 | ||||
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: 120.78 E-value: 6.20e-30
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
27-94 | 5.27e-29 | ||||
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: 112.10 E-value: 5.27e-29
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
27-100 | 7.90e-27 | ||||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 113.38 E-value: 7.90e-27
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
27-103 | 1.06e-26 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 112.10 E-value: 1.06e-26
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
27-168 | 2.73e-26 | ||||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 110.58 E-value: 2.73e-26
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
27-102 | 9.67e-26 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 109.08 E-value: 9.67e-26
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
27-104 | 4.40e-25 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 105.41 E-value: 4.40e-25
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SEC63 | COG5407 | Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
27-85 | 4.99e-25 | ||||
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 98.15 E-value: 4.99e-25
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
27-93 | 7.83e-24 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 103.70 E-value: 7.83e-24
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
27-91 | 1.48e-23 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 102.62 E-value: 1.48e-23
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
27-204 | 1.90e-23 | ||||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 102.60 E-value: 1.90e-23
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
27-103 | 7.58e-23 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 100.51 E-value: 7.58e-23
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
26-83 | 1.06e-22 | ||||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 91.53 E-value: 1.06e-22
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
27-80 | 1.28e-22 | ||||
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: 91.07 E-value: 1.28e-22
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
27-104 | 2.02e-22 | ||||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 99.29 E-value: 2.02e-22
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
27-102 | 5.06e-22 | ||||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 98.32 E-value: 5.06e-22
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
26-100 | 1.30e-21 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 96.88 E-value: 1.30e-21
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
23-175 | 9.84e-21 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 94.12 E-value: 9.84e-21
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
27-104 | 1.01e-20 | ||||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 94.53 E-value: 1.01e-20
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
27-102 | 1.76e-20 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 93.71 E-value: 1.76e-20
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
27-102 | 4.01e-20 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 92.56 E-value: 4.01e-20
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
29-104 | 6.53e-19 | ||||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 89.11 E-value: 6.53e-19
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
27-103 | 1.08e-18 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 87.90 E-value: 1.08e-18
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
27-99 | 1.12e-18 | ||||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 80.92 E-value: 1.12e-18
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
27-99 | 6.26e-18 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 86.05 E-value: 6.26e-18
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
27-103 | 7.57e-18 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 85.56 E-value: 7.57e-18
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
24-103 | 1.50e-17 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 84.61 E-value: 1.50e-17
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
29-102 | 2.17e-17 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 84.27 E-value: 2.17e-17
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
25-103 | 3.10e-17 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 83.53 E-value: 3.10e-17
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
27-91 | 2.44e-16 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 80.99 E-value: 2.44e-16
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
27-102 | 9.10e-16 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 79.20 E-value: 9.10e-16
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
27-103 | 1.26e-15 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 78.49 E-value: 1.26e-15
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PRK14279 | PRK14279 | molecular chaperone DnaJ; |
27-88 | 3.02e-15 | ||||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 77.85 E-value: 3.02e-15
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
27-102 | 4.06e-15 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 77.36 E-value: 4.06e-15
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PRK10266 | PRK10266 | curved DNA-binding protein; |
27-103 | 2.82e-13 | ||||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 70.62 E-value: 2.82e-13
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
29-93 | 7.39e-12 | ||||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 67.02 E-value: 7.39e-12
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
27-81 | 7.02e-11 | ||||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 58.27 E-value: 7.02e-11
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PTZ00341 | PTZ00341 | Ring-infected erythrocyte surface antigen; Provisional |
29-91 | 6.56e-08 | ||||
Ring-infected erythrocyte surface antigen; Provisional Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 55.56 E-value: 6.56e-08
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ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
24-88 | 5.79e-07 | ||||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 51.96 E-value: 5.79e-07
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djlA | PRK09430 | co-chaperone DjlA; |
27-78 | 1.03e-06 | ||||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 50.58 E-value: 1.03e-06
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PHA03102 | PHA03102 | Small T antigen; Reviewed |
43-102 | 2.11e-03 | ||||
Small T antigen; Reviewed Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 38.88 E-value: 2.11e-03
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hscB | PRK01356 | co-chaperone HscB; Provisional |
43-89 | 4.00e-03 | ||||
co-chaperone HscB; Provisional Pssm-ID: 167217 [Multi-domain] Cd Length: 166 Bit Score: 38.32 E-value: 4.00e-03
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P5_C | cd02983 | P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ... |
435-558 | 5.32e-03 | ||||
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI. Pssm-ID: 239281 Cd Length: 130 Bit Score: 37.33 E-value: 5.32e-03
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PHA02624 | PHA02624 | large T antigen; Provisional |
43-104 | 5.73e-03 | ||||
large T antigen; Provisional Pssm-ID: 222912 [Multi-domain] Cd Length: 647 Bit Score: 39.58 E-value: 5.73e-03
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Blast search parameters | ||||
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