The domain within your query sequence starts at position 1242 and ends at position 1341; the E-value for the RasGEF_N domain shown below is 2.2e-17.

ILQAGTPLGLMAYLYSSDAFLEGYVQQFLYTFRYFCTPHDFLHFLLDRISSTLSRAHQDP
TSTFTKIYRRSLCVLQAWVEDCYTVDFIRNAGLLGQLEDF

RasGEF_N

RasGEF_N
PFAM accession number:PF00618
Interpro abstract (IPR000651):

The N-terminal domain of guanine nucleotide exchange factor (GEF) for Ras-like GTPases is also called REM domain (Ras exchanger motif). REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few [(PUBMED:18541156), (PUBMED:18236214), (PUBMED:7786285), (PUBMED:8259209), (PUBMED:8479541), (PUBMED:16452984), (PUBMED:12628188), (PUBMED:9690470)].

The crystal structure of the GEF region of human Sos1 complexes with Ras has been solved [(PUBMED:9690470)]. The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure.

This entry represents a domain found in several GEF for Ras-like small GTPases which lies N-terminal to the RasGef (Cdc25-like) domain.

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