The domain within your query sequence starts at position 1824 and ends at position 2003; the E-value for the Rap_GAP domain shown below is 7.4e-66.

ILTNIGGSQAYEDFVAGLGWEVNLTNHCGFMGGLQKNRSTGLTTPYFATSTVEVIFHVST
RMPSDSDDSLTKKLRHLGNDEVHIVWSEHTRDYRRGIIPTEFGDVLIVIYPMKNHMFSIQ
IMKKPEVPFFGPLFDGAIVNGKVLPIMVRSTAINASRALKSLIPLYQNFYEERARYLQTI

Rap_GAP

Rap_GAP
PFAM accession number:PF02145
Interpro abstract (IPR000331):

Rap small G proteins have been implicated in various cellular processes such as exocytosis, cAMP signalling, cell adhesion and cell proliferation. Rap proteins acts as molecular switches, with an active GTP-bound form and an inactive GDP-bound form [(PUBMED:11331911)]. The inactive GDP bound form is promoted by GTPase-activating proteins (GAPs). GAP proteins specific for Rap contain a conserved region of around 200 amino-acid residues, the RapGAP domain. This domain can accelerate the GTP hydrolysis activity of Rap by five orders of magnitude [(PUBMED:9346962)].

Proteins known to contain a Rap-GAP domain include:

  • RAP1 GTPase activating protein (RAP1GAP).
  • Mammalian tuberin protein, the product of a familial tuberous sclerosis gene which, when deleted, causes begnin tumours. It also have a GAP activity for Rab5 [(PUBMED:9045618)].
  • Drosophila Gigas protein, an homologue of tuberin involved in regulation of cell cycle.
  • Mammalian tuberin-like protein TULIP.
  • GTPase-activating protein Spa-1. It functions as a negative regulator for the activation of Rap1, thereby having a negative effect on cell adhesion [(PUBMED:10373454)].

GO process:regulation of small GTPase mediated signal transduction (GO:0051056)
GO function:GTPase activator activity (GO:0005096)

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