The domain within your query sequence starts at position 147 and ends at position 234; the E-value for the GFA domain shown below is 3.2e-12.

FDCNCSICKKKQNRHFIVPASRFKLLKGAESITTYTFNTHKAQHTFCKRCGVQSFYTPRS
NPGGFGIAPHCLDEGTVRSVVTEEFNGS

GFA

GFA
PFAM accession number:PF04828
Interpro abstract (IPR006913):

Centrome protein (CENP)-V is a kinetochore protein that drives the progression of mitosis by coordinating chromatin condensation, positioning of sister chromatid centromeres and targeting of the chromosome passager complex (CPC), a machinery that regulates the attachment of spindle microtubules (MTs) to kinetochores. CENP-V homologues are found in all vertebrates as well as in plants and nematodes. At the C-terminal end, CENP-V possesses an evolutionally conserved domain that comprises an array of seven cysteines and shows high structural similarity to glutathione-dependent formaldehyde-activating enzyme (Gfa), an enzyme responsible for formaldehyde detoxification in prokaryotes. CENP-V could be an enzyme that scavenges the formaldehyde produced in histone demethylation reactions. The three central cysteines and the flanking four cysteines separately coordinate to zinc, forming a catalytic centre and a structural fold for a tertiary structure, respectively [ (PUBMED:18772885) (PUBMED:19930468) (PUBMED:15548539) ].

The main topological feature of the CENP-V/GFA domain is an extremely twisted mixed eight-stranded beta-shee. Within this beta-sheet, the strands beta8, beta9, and beta4 form a sandwich with another triple stranded mixed beta-sheet (beta5, beta2, beta1). The interconnection between the sheets is mediated by four 3(10) helices and two alpha helices. The sandwich arrangement of the beta-strands is further buttressed by a terahedral zinc coordinated by the side chains of four cysteines. It appears that this zinc atom has only a structural role. A second zinc ion stabilizes a large hairpin loop that connects beta3 and beta4 via residues of three cysteines [ (PUBMED:15548539) ].

This entry represents the CENP-V/GFA domain.

GO function:carbon-sulfur lyase activity (GO:0016846)

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