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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)
co-chaperone HscB
co-chaperone HscB is involved in the maturation of iron-sulfur cluster-containing proteins
J-type co-chaperone that regulates the ATPase and peptide-binding activity of Hsc66 chaperone
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.
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