The domain within your query sequence starts at position 1325 and ends at position 1416; the E-value for the RA domain shown below is 2.1e-7.

DLLIEVFVERKEPDCSIIIRISPVMEAEELTNDILAIKNIIPMKGDIWATFEVIENEELE
RPLHYTENVLEQVLQWSSLAEPGSAYLVVKRF

RA

RA
PFAM accession number:PF00788
Interpro abstract (IPR000159):

Ras proteins are signal-transducing GTPases that cycle between inactive GDP- bound and active GTP-bound forms. Ras is a prolific signalling molecule interacting with a spectrum of effector molecules and acting through more than one signalling pathway. A domain of about 100 residues, termed RA for RalGDS/AF-6 or Ras-Associating, interacts with Ras and other small GTPases. It occurs in one or two copies in a variety of signalling molecules. It can be found associated with many other domains, such as PDZ, Dilute (DIL), GEF, myosin motor, IQ, C1, C2, protein kinase, VPS9 or sterile alpha motif (SAM) [(PUBMED:8987396), (PUBMED:11723130)].

Structurally, the RA domain of RalGDS consists of a five-stranded mixed beta- sheet interrupted by a 12 residue alpha-helix and two additional small alpha- helices. The structure of the RA domain belongs to the ubiquitin alpha/beta roll superfold and is similar to that of the RBD domain and the N-terminal third of the FERM domain [(PUBMED:9253406), (PUBMED:10334925)]. The RA domain forms a homodimer where the interdimer surface is composed of two cysteines (Cys 2 in each monomer) forming an intermolecular disulfide bond and two interacting intermolecular antiparallel beta-sheets [(PUBMED:9253406)]. The major interaction between Ras and RalGDS RA domain occurs between two antiparallel beta-strands: beta 2 of Ras and beta 2 of RA. This interaction occurs both at the backbone as well as the side chain level [(PUBMED:9628477)].

GO process:signal transduction (GO:0007165)

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