The domain within your query sequence starts at position 81 and ends at position 167; the E-value for the ACBP domain shown below is 3.2e-18.

EELYGLALRFYKIKDGKAFHPTYEEKLKFVALHKQVLLGPYNPDTSPEVGFFDVLGNDRR
REWAALGNMSKEDAMVEFVKLLNKCCP

ACBP

ACBP
PFAM accession number:PF00887
Interpro abstract (IPR000582):

Acyl-CoA-binding protein (ACBP) is a small (10 Kd) protein that binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters [(PUBMED:1454809)]. ACBP is also known as diazepam binding inhibitor (DBI) or endozepine (EP) because of its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor [(PUBMED:1649940)].

ACBP is a highly conserved protein of about 90 residues that is found in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and in some eubacterial species [(PUBMED:16018771)].

Although ACBP occurs as a completely independent protein, intact ACB domains have been identified in a number of large, multifunctional proteins in a variety of eukaryotic species. These include large membrane-associated proteins with N-terminal ACB domains, multifunctional enzymes with both ACB and peroxisomal enoyl-CoA Delta(3), Delta(2)-enoyl-CoA isomerase domains, and proteins with both an ACB domain and ankyrin repeats (IPR002110) [(PUBMED:16018771)].

The ACB domain consists of four alpha-helices arranged in a bowl shape with a highly exposed acyl-CoA-binding site. The ligand is bound through specific interactions with residues on the protein, most notably several conserved positive charges that interact with the phosphate group on the adenosine-3'phosphate moiety, and the acyl chain is sandwiched between the hydrophobic surfaces of CoA and the protein [(PUBMED:11491287)].

Other proteins containing an ACB domain include:

  • Endozepine-like peptide (ELP) (gene DBIL5) from mouse [(PUBMED:8898349)]. ELP is a testis-specific ACBP homologue that may be involved in the energy metabolism of the mature sperm.
  • MA-DBI, a transmembrane protein of unknown function which has been found in mammals. MA-DBI contains a N-terminal ACB domain.
  • DRS-1 [(PUBMED:10354522)], a human protein of unknown function that contains a N-terminal ACB domain and a C-terminal enoyl-CoA isomerase/hydratase domain.

GO function:fatty-acyl-CoA binding (GO:0000062)

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