| Primary Identifier | IPR039007 | Type | Domain |
| Short Name | pG1 |
| description | 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 [].The p190RhoGAP proteins, p190RhoGAP-A (ARHGAP35) andp190RhoGAP-B (ARHGAP5), are key regulators of Rho GTP hydrolysis and arehighly important for maintenance of proper Rho signaling. They share a domainorganization containing a GTP-binding GTPase domain, four FF domains, twoGTPase-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 []. This entry represents the pG1 domain. |
