Raf-like Ras-binding (IPR003116)

Short name: RBD_dom

Overlapping homologous superfamilies


Domain relationships



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 [PMID: 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 [PMID: 7791872].

This entry represents the entire RBD domain.

GO terms

Biological Process

GO:0007165 signal transduction

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles