![](files/infoQ.gif)
dnaJ homolog subfamily B member 6 isoform X1 [Homo sapiens]
J domain-containing protein( domain architecture ID 1000550)
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
![](files/help.png)
Name | Accession | Description | Interval | E-value | |||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
3-66 | 5.15e-37 | |||
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: 127.20 E-value: 5.15e-37
|
|||||||
terminal_TopJ super family | cl41578 | terminal organelle assembly protein TopJ; |
3-151 | 5.15e-28 | |||
terminal organelle assembly protein TopJ; The actual alignment was detected with superfamily member NF037946: Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 112.99 E-value: 5.15e-28
|
|||||||
Name | Accession | Description | Interval | E-value | |||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
3-66 | 5.15e-37 | |||
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: 127.20 E-value: 5.15e-37
|
|||||||
DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
3-106 | 6.13e-37 | |||
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: 135.81 E-value: 6.13e-37
|
|||||||
PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
3-107 | 2.46e-36 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 134.50 E-value: 2.46e-36
|
|||||||
DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
3-68 | 3.63e-33 | |||
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: 119.81 E-value: 3.63e-33
|
|||||||
DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
2-61 | 6.13e-32 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 113.87 E-value: 6.13e-32
|
|||||||
DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
3-58 | 6.53e-29 | |||
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: 105.71 E-value: 6.53e-29
|
|||||||
terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
3-151 | 5.15e-28 | |||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 112.99 E-value: 5.15e-28
|
|||||||
Name | Accession | Description | Interval | E-value | |||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
3-66 | 5.15e-37 | |||
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: 127.20 E-value: 5.15e-37
|
|||||||
DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
3-106 | 6.13e-37 | |||
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: 135.81 E-value: 6.13e-37
|
|||||||
PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
3-107 | 2.46e-36 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 134.50 E-value: 2.46e-36
|
|||||||
DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
3-68 | 3.63e-33 | |||
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: 119.81 E-value: 3.63e-33
|
|||||||
DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
2-61 | 6.13e-32 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 113.87 E-value: 6.13e-32
|
|||||||
PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
3-105 | 1.14e-30 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 119.10 E-value: 1.14e-30
|
|||||||
PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
3-107 | 3.01e-30 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 117.97 E-value: 3.01e-30
|
|||||||
PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
3-106 | 9.34e-30 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 116.57 E-value: 9.34e-30
|
|||||||
DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
3-58 | 6.53e-29 | |||
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: 105.71 E-value: 6.53e-29
|
|||||||
PRK14280 | PRK14280 | molecular chaperone DnaJ; |
3-109 | 1.53e-28 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 113.66 E-value: 1.53e-28
|
|||||||
terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
3-151 | 5.15e-28 | |||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 112.99 E-value: 5.15e-28
|
|||||||
PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
3-106 | 1.01e-27 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 111.40 E-value: 1.01e-27
|
|||||||
PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
3-106 | 4.11e-27 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 109.55 E-value: 4.11e-27
|
|||||||
PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
3-105 | 4.82e-27 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 109.55 E-value: 4.82e-27
|
|||||||
PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
3-68 | 1.44e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 108.36 E-value: 1.44e-26
|
|||||||
PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
3-109 | 2.09e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 107.48 E-value: 2.09e-26
|
|||||||
PRK14297 | PRK14297 | molecular chaperone DnaJ; |
3-106 | 2.23e-26 | |||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 107.56 E-value: 2.23e-26
|
|||||||
SEC63 | COG5407 | Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
3-62 | 2.36e-26 | |||
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 99.30 E-value: 2.36e-26
|
|||||||
PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
3-105 | 4.28e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 106.81 E-value: 4.28e-26
|
|||||||
PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
3-105 | 6.09e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 106.36 E-value: 6.09e-26
|
|||||||
CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
1-66 | 5.31e-25 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 96.33 E-value: 5.31e-25
|
|||||||
PRK14289 | PRK14289 | molecular chaperone DnaJ; |
3-68 | 1.05e-24 | |||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 102.99 E-value: 1.05e-24
|
|||||||
PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
3-106 | 4.12e-24 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 101.44 E-value: 4.12e-24
|
|||||||
PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
3-106 | 4.87e-24 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 100.90 E-value: 4.87e-24
|
|||||||
PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
1-106 | 1.49e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 99.58 E-value: 1.49e-23
|
|||||||
PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
4-106 | 2.73e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 98.91 E-value: 2.73e-23
|
|||||||
PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
3-107 | 1.27e-22 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 96.98 E-value: 1.27e-22
|
|||||||
PRK14279 | PRK14279 | molecular chaperone DnaJ; |
3-66 | 7.24e-22 | |||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 95.18 E-value: 7.24e-22
|
|||||||
PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
3-110 | 3.74e-21 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 91.54 E-value: 3.74e-21
|
|||||||
PRK14293 | PRK14293 | molecular chaperone DnaJ; |
1-68 | 5.16e-21 | |||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 92.36 E-value: 5.16e-21
|
|||||||
termin_org_DnaJ | TIGR03835 | terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ... |
3-104 | 9.48e-20 | |||
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility] Pssm-ID: 274808 [Multi-domain] Cd Length: 871 Bit Score: 90.26 E-value: 9.48e-20
|
|||||||
PRK14295 | PRK14295 | molecular chaperone DnaJ; |
3-66 | 4.65e-19 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 86.83 E-value: 4.65e-19
|
|||||||
PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
3-106 | 5.34e-19 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 86.60 E-value: 5.34e-19
|
|||||||
PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
4-106 | 6.18e-19 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 86.80 E-value: 6.18e-19
|
|||||||
PRK14288 | PRK14288 | molecular chaperone DnaJ; |
2-94 | 8.44e-19 | |||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 86.28 E-value: 8.44e-19
|
|||||||
PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
3-105 | 4.60e-18 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 83.84 E-value: 4.60e-18
|
|||||||
PRK10266 | PRK10266 | curved DNA-binding protein; |
3-105 | 5.45e-17 | |||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 80.25 E-value: 5.45e-17
|
|||||||
PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
3-68 | 4.77e-16 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 78.13 E-value: 4.77e-16
|
|||||||
DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
1-64 | 1.07e-15 | |||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 70.98 E-value: 1.07e-15
|
|||||||
PTZ00341 | PTZ00341 | Ring-infected erythrocyte surface antigen; Provisional |
4-68 | 3.76e-10 | |||
Ring-infected erythrocyte surface antigen; Provisional Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 61.34 E-value: 3.76e-10
|
|||||||
ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
2-66 | 7.45e-08 | |||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 53.50 E-value: 7.45e-08
|
|||||||
djlA | PRK09430 | co-chaperone DjlA; |
3-61 | 4.56e-07 | |||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 50.20 E-value: 4.56e-07
|
|||||||
hscB | PRK01356 | co-chaperone HscB; Provisional |
1-65 | 1.01e-04 | |||
co-chaperone HscB; Provisional Pssm-ID: 167217 [Multi-domain] Cd Length: 166 Bit Score: 42.17 E-value: 1.01e-04
|
|||||||
PHA03102 | PHA03102 | Small T antigen; Reviewed |
6-37 | 1.79e-03 | |||
Small T antigen; Reviewed Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 38.50 E-value: 1.79e-03
|
|||||||
Blast search parameters | ||||
|