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Links from Protein

Items: 6

1.

iron-sulfur cluster co-chaperone HscB C-terminal domain-containing protein

This domain is the HSCB C-terminal oligomerisation domain and is found on co-chaperone proteins. (from Pfam)

GO Terms:
Biological Process:
protein complex oligomerization (GO:0051259)
Date:
2024-08-14
Family Accession:
NF019363.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

co-chaperone HscB

co-chaperone HscB is involved in the maturation of iron-sulfur cluster-containing proteins

Date:
2019-07-29
Family Accession:
11480322
Method:
Sparcle
5.

co-chaperone HscB

J-type co-chaperone that regulates the ATPase and peptide-binding activity of Hsc66 chaperone

Gene:
hscB
GO Terms:
Molecular Function:
protein-folding chaperone binding (GO:0051087)
Biological Process:
protein maturation by iron-sulfur cluster transfer (GO:0097428)
Date:
2021-09-10
Family Accession:
NF003449.0
Method:
HMM
6.

Fe-S protein assembly co-chaperone HscB

This HMM describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock.

Gene:
hscB
GO Terms:
Molecular Function:
ATPase activator activity (GO:0001671)
Biological Process:
[2Fe-2S] cluster assembly (GO:0044571)
Molecular Function:
protein-folding chaperone binding (GO:0051087)
Date:
2024-05-15
Family Accession:
TIGR00714.1
Method:
HMM
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