The domain within your query sequence starts at position 159 and ends at position 200; the E-value for the Biotin_carb_C domain shown below is 1.5e-9.

EARIYAEDPDNNFMPGAGPLVHLSTPSADMSTRIETGVRQDW

Biotin_carb_C

Biotin_carb_C
PFAM accession number:PF02785
Interpro abstract (IPR005482):

Acetyl-CoA carboxylase is found in all animals, plants, and bacteria and catalyzes the first committed step in fatty acid synthesis. It is a multicomponent enzyme containing a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase functionality. The "B-domain" extends from the main body of the subunit where it folds into two alpha-helical regions and three strands of beta-sheet. Following the excursion into the B-domain, the polypeptide chain folds back into the body of the protein where it forms an eight-stranded antiparallel beta-sheet. In addition to this major secondary structural element, the C-terminal domain also contains a smaller three-stranded antiparallel beta-sheet and seven alpha-helices [(PUBMED:7915138)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Biotin_carb_C