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):|
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)|
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