The domain within your query sequence starts at position 1034 and ends at position 1104; the E-value for the RBD domain shown below is 2.44e-21.



Raf-like Ras-binding domain
SMART accession number:SM00455
Description: -
Interpro abstract (IPR003116):

Ras and heterotrimeric G proteins' alpha subunits are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound forms. The activities of these GTPases are regulated in part by GTPase-activating protein (GAPs) that stimulate hydrolysis of GTP, and guanine nucleotide exchange factors (GEFs) that stimulate GDP release. Ras and G alpha GTPases are prolific signalling molecules interacting with a spectrum of effector molecules and acting through more than one signalling pathway. The Ras-binding domain (RBD) is an independent domain of about 75 residues, which is sufficient for GTP-dependent binding of Ras and other G alpha GTPases. The RBD domain can be present singly or in tandem and it can be found associated with many other domains, such as PDZ, RGS, PID, PH, C1, DH, or protein kinase [ (PUBMED:10606204) ].

Structurally, the RBD domain of Raf-1 consists of a five-stranded mixed beta- sheet with an interrupted alpha-helix and two additional small alpha-helices. The structure of the RBD domain belongs to the ubiquitin alpha/beta roll superfold and is similar to that of the RA domain despite the lack of significant sequence identity. The major interaction between Ras and Raf-1 RBD domain occurs between two antiparallel beta-strands: beta 2 of Ras and beta 2 of RBD [ (PUBMED:7791872) ].

This entry represents the entire RBD domain.

GO process:signal transduction (GO:0007165)
Family alignment:
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There are 4454 RBD domains in 3476 proteins in SMART's nrdb database.

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