1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
| Type: | Domain | Name: | Very large inducible GTPASE (VLIG)-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 very large inducible GTPase (VLIG) family contributes to the cellular response to both type I and type II interferons (IFNs). Phylogenetically, theVLIG family is relatively old, since there are representatives in zebrafish and salmon. The potential GTP-binding activity of mouse VLIG-1, the prototypeVLIG, possesses a classical GTP-binding sequence motif. The G1 or P-loop (G- x(4)-G-K-S) and G3 (D-x(2)-G) motifs are both present in a canonical form. TheG4 motif ([NT]-K-x-D), associated in canonical GTPases with contact to theguanine base, is not immediately apparent [, ].This entry represents the VLIG-type G domain. | Short Name: | G_VLIG_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
