DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana]
J domain-containing protein( domain architecture ID 10644999)
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 | |||
CbpA super family | cl34431 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
39-103 | 1.63e-06 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; The actual alignment was detected with superfamily member COG2214: Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 46.63 E-value: 1.63e-06
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DnaJ super family | cl33903 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
43-179 | 9.06e-05 | |||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; The actual alignment was detected with superfamily member COG0484: Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 43.15 E-value: 9.06e-05
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Name | Accession | Description | Interval | E-value | |||
CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
39-103 | 1.63e-06 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 46.63 E-value: 1.63e-06
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
42-94 | 4.35e-06 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 44.53 E-value: 4.35e-06
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
43-102 | 6.58e-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: 44.00 E-value: 6.58e-06
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
43-179 | 9.06e-05 | |||
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: 43.15 E-value: 9.06e-05
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
44-94 | 1.70e-04 | |||
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: 39.84 E-value: 1.70e-04
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
44-102 | 4.60e-03 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 39.91 E-value: 4.60e-03
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Name | Accession | Description | Interval | E-value | |||
CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
39-103 | 1.63e-06 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 46.63 E-value: 1.63e-06
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
42-94 | 4.35e-06 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 44.53 E-value: 4.35e-06
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
43-102 | 6.58e-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: 44.00 E-value: 6.58e-06
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
43-179 | 9.06e-05 | |||
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: 43.15 E-value: 9.06e-05
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
44-94 | 1.70e-04 | |||
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: 39.84 E-value: 1.70e-04
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
44-102 | 4.60e-03 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 39.91 E-value: 4.60e-03
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Blast search parameters | ||||
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