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

HSCB_C
PFAM accession number:PF07743
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