| Description | The P-loop guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G) domain that is responsible for binding and hydrolysis of guanine nucleotides.The p47 or immunity-related GTPases (IRG) are at least as old as the vertebrates. The IRG proteins are an essential resistance system for immunity against pathogens that enter the cell via a vacuole. They act as a dynamin-like proteins that bind to intracellular membranes and promotes remodeling and trafficking of those membranes [ , ]. These proteins are required for clearance of acute protozoan and bacterial infections by interacting with autophagy and lysosome regulatory proteins, thereby promoting the fusion of phagosomes with lysosomes for efficient degradation of cargo including microbes [, , ]. The IRG proteins appear to be accompanied phylogenetically by homologous proteins, named 'quasi IRG' (IRGQ) proteins, that probably lack nucleotide binding or hydrolysis function, and that may form regulatory heterodimers with functional IRG proteins. The region of lowest similarity is in the G domain, and conserved GTP-binding motifs are lacking [, , ]. | Name | IRG-type guanine nucleotide-binding (G) domain |
| Short Name | G_IRG_dom | Type | Domain |
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