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):|
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)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Disease (disease genes where sequence variants are found in this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)