Rho GTPase-activating protein, pG1 domain (IPR039007)

Short name: pG1

Overlapping homologous superfamilies


Domain relationships



GTPases bind to guanosine triphosphate (GTP), hydrolyze gamma-phosphate, release guanosine diphosphate (GDP) and then rebind GTP, a process termed 'GTPase cycling'. GTPases are regulated by GTPase activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs). The Ras superfamily of small GTPases consists of five subgroups (Ras, Rho, Rab, Ran and Arf) that act as molecular switches in broad and diverse cellular pathways and processes. The Ras superfamily members contain five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases by definition would consist of a GTPase fold lacking one or more of these G motifs [PMID: 28894085].

The p190RhoGAP proteins, p190RhoGAP-A (ARHGAP35) and p190RhoGAP-B (ARHGAP5), are key regulators of Rho GTP hydrolysis and are highly important for maintenance of proper Rho signaling. They share a domain organization containing a GTP-binding GTPase domain, four FF domains, two GTPase-like folds (pG1 and pG2) and a C-terminal GAP domain. Their pG1 (pseudoGTPase1) and pG2 (pseudoGTPase2) domains lack conserved GTPase motifs and don't have nucleotide-binding activity [PMID: 28894085].

This entry represents the pG1 domain.

Contributing signatures

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