The domain within your query sequence starts at position and ends at position ; the E-value for the RasGAP domain shown below is < 1e-12.
RasGAPGTPase-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):|
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 stimulated by a family of proteins collectively known as 'GAP' or GTPase-activating proteins [(PUBMED:1883874), (PUBMED:7945277)]. As it is the GTP bound form of ras which is active, these proteins are said to be down-regulators of ras.
The Ras GTPase-activating proteins are 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.
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 small GTPase mediated signal transduction (GO:0051056)|
|GO component:||intracellular (GO:0005622)|
|GO function:||GTPase activator activity (GO:0005096)|
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