1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
| Type: | Domain | Name: | GB1/RHD3-type guanine nucleotide-binding (G) domain |
| 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 andan 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 GB1/RHD3 GTPase family contains a large G domain (~230 amino acids). It is widespread in eukaryotes, but not detectable in bacteria or archaea. Oneconserved subfamily is typified by the Arabidopsis protein root hair defective 3 (RHD3), whose othologs are present in all crown group eukaryotes. The othersubfamily is typified by the interferon gamma-induced antiviral GB1 protein that is conserved in animals. The other GTPases of this subfamily are thebrain finger proteins (BFPs), in which the GTPase domain is combined with an N-terminal RING finger domain, which implicates theseproteins in ubiquitin-mediated signaling. Most members of this family have a large C-terminal, alpha-helical extension that probably participates inprotein-protein interactions. The GB1/RHD3-type G domain has a low intrinsic affinity for nucleotide and often depends on nucleotide-dependenthomodimerization to facilitate GTP hydrolysis [, , , , , ].The large GB1/RHD3-type G domain consists of a six-stranded beta-sheet surrounded by eight helices. It contains the conservedsequence elements of GTP-binding proteins with modifications [, , ]. | Short Name: | G_GB1_RHD3_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
