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protein SSUH2 homolog isoform X5 [Homo sapiens]
DnaJ_zf domain-containing protein( domain architecture ID 10180502)
DnaJ_zf domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||
DnaJ_zf | cd10719 | Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ... |
292-359 | 7.37e-07 | ||
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ 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 chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding. : Pssm-ID: 199908 [Multi-domain] Cd Length: 65 Bit Score: 46.48 E-value: 7.37e-07
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Name | Accession | Description | Interval | E-value | ||
DnaJ_zf | cd10719 | Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ... |
292-359 | 7.37e-07 | ||
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ 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 chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding. Pssm-ID: 199908 [Multi-domain] Cd Length: 65 Bit Score: 46.48 E-value: 7.37e-07
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DnaJ_CXXCXGXG | pfam00684 | DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ... |
292-359 | 6.88e-06 | ||
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found. Pssm-ID: 459904 [Multi-domain] Cd Length: 65 Bit Score: 43.70 E-value: 6.88e-06
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PLN03165 | PLN03165 | chaperone protein dnaJ-related; Provisional |
292-348 | 2.99e-05 | ||
chaperone protein dnaJ-related; Provisional Pssm-ID: 178709 [Multi-domain] Cd Length: 111 Bit Score: 43.27 E-value: 2.99e-05
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Name | Accession | Description | Interval | E-value | |||
DnaJ_zf | cd10719 | Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ... |
292-359 | 7.37e-07 | |||
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ 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 chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding. Pssm-ID: 199908 [Multi-domain] Cd Length: 65 Bit Score: 46.48 E-value: 7.37e-07
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DnaJ_CXXCXGXG | pfam00684 | DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ... |
292-359 | 6.88e-06 | |||
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found. Pssm-ID: 459904 [Multi-domain] Cd Length: 65 Bit Score: 43.70 E-value: 6.88e-06
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PLN03165 | PLN03165 | chaperone protein dnaJ-related; Provisional |
292-348 | 2.99e-05 | |||
chaperone protein dnaJ-related; Provisional Pssm-ID: 178709 [Multi-domain] Cd Length: 111 Bit Score: 43.27 E-value: 2.99e-05
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
291-351 | 4.93e-05 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 45.48 E-value: 4.93e-05
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
291-348 | 1.38e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 43.92 E-value: 1.38e-04
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
247-358 | 2.11e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 43.66 E-value: 2.11e-04
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
254-360 | 2.48e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 43.30 E-value: 2.48e-04
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
278-343 | 2.51e-04 | |||
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region. Pssm-ID: 460251 [Multi-domain] Cd Length: 213 Bit Score: 42.24 E-value: 2.51e-04
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
288-348 | 3.29e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 43.01 E-value: 3.29e-04
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
290-340 | 5.31e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 42.09 E-value: 5.31e-04
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
273-348 | 5.38e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 42.30 E-value: 5.38e-04
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
280-340 | 8.18e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 41.72 E-value: 8.18e-04
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
292-313 | 9.28e-04 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 41.28 E-value: 9.28e-04
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
289-312 | 6.76e-03 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 38.76 E-value: 6.76e-03
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Blast search parameters | ||||
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