The domain within your query sequence starts at position 156 and ends at position 228; the E-value for the HSCB_C domain shown below is 9.4e-23.
ADSQFLVEIMEINERLADAQSEAAMEEIEATVRAKQKEFTDNINSAFEQGDFEKAKELLT KMRYFSNIEEKIK
HSCB_C |
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| PFAM accession number: | PF07743 |
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| Interpro abstract (IPR009073): | This entry represents the C-terminal oligomerisation domain found in HscB (heat shock cognate protein B), which is also known as HSC20 (20K heat shock cognate protein) and J-protein Jac1 in yeast mitochondria [ (PUBMED:22306468) ]. HscB acts as a co-chaperone to regulate the ATPase activity and peptide-binding specificity of the molecular chaperone HscA, also known as HSC66 (HSP70 class). HscB proteins contain two domains, an N-terminal J-domain, which is involved in interactions with HscA, connected by a short loop to the C-terminal oligomerisation domain; the two domains make contact through a hydrophobic interface. The core of the oligomerisation domain is thought to bind and target proteins to HscA and consists of an open, three-helical bundle [ (PUBMED:11124030) ]. HscB, along with HscA, has been shown to play a role in the biogenesis of iron-sulphur proteins. |
| GO process: | protein complex oligomerization (GO:0051259) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry HSCB_C