The domain within your query sequence starts at position 2591 and ends at position 2717; the E-value for the BRCA-2_OB1 domain shown below is 5.3e-44.

SALKKILERDDTAAKTLVLCISDIISPSTKVSETSGGKTSGEDANKVDTIELTDGWYAVR
AQLDPPLMALVKSGKLTVGQKIITQGAELVGSPDACAPLEAPDSLRLKISANSTRPARWH
SRLGFFR

BRCA-2_OB1

BRCA-2_OB1
PFAM accession number:PF09103
Interpro abstract (IPR015187):

This entry represents OB1, which consists of a highly curved five-stranded beta-sheet that closes on itself to form a beta-barrel. OB1 has a shallow groove formed by one face of the curved sheet and is demarcated by two loops, one between beta 1 and beta 2 and another between beta 4 and beta 5, which allows for weak single strand DNA binding. The domain also binds the 70-amino acid DSS1 (deleted in split-hand/split foot syndrome) protein, which was originally identified as one of three genes that map to a 1.5-Mb locus deleted in an inherited developmental malformation syndrome [ (PUBMED:12228710) ].

BRCA2 participates in homologous recombination-mediated repair of double-strand DNA breaks [ (PUBMED:12228710) (PUBMED:12727514) ]. It stimulates the displacement of Replication protein A (RPA), the most abundant eukaryotic ssDNA binding protein [ (PUBMED:12442171) ]. Mutations that map throughout the BRCA2 protein are associated with breast cancer susceptibility [ (PUBMED:20513136) ]. BRCA2 is a large nuclear protein and its most conserved region is the C-terminal BRCA2DBD. BRCA2DBD binds ssDNA in vitro, and is composed of five structural domains, three of which are OB folds (OB1, OB2, and OB3). BRCA2DBD OB2 and OB3 are arranged in tandem, and their mode of binding can be considered qualitatively similar to two OB folds of RPA1, DBD-A and DBD-B (the major DBDs of RPA) [ (PUBMED:15102447) ].

GO process:double-strand break repair via homologous recombination (GO:0000724)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry BRCA-2_OB1