The domain within your query sequence starts at position 392 and ends at position 729; the E-value for the RasGAP domain shown below is 2.2e-120.



GTPase-activator protein for Ras-like GTPases
SMART accession number:SM00323
Description: All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.
Interpro abstract (IPR001936):

This entry represents a conserved domain in the RasGAPs (Ras GTPase-activating proteins). This domain is also known as the RasGAP domain.

Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP [ (PUBMED:1898771) ]. This intrinsic GTPase activity of Ras is regulated by a family of proteins collectively known as 'GAP' or GTPase-activating proteins [ (PUBMED:1883874) (PUBMED:7945277) ]. RasGAP proteins are usually quite large (from 765 residues for sar1 to 3079 residues for IRA2) but share only a limited (about 250 residues) region of sequence similarity, referred to as the 'catalytic domain' or RasGAP domain. The most conserved region within this domain contains a 15 residue motif which seems to be characteristic of this family of proteins [ (PUBMED:1883874) ].

Note: There are distinctly different GAPs for the rap and rho/rac subfamilies of Ras-like proteins (reviewed in reference [ (PUBMED:8259209) ]) that do not share sequence similarity with ras GAPs.

GO process:regulation of GTPase activity (GO:0043087)
Family alignment:
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There are 8958 RasGAP domains in 8955 proteins in SMART's nrdb database.

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