Very large inducible GTPASE (VLIG)-type guanine nucleotide-binding (G) domain (IPR030383)

Short name: G_VLIG_dom

Overlapping homologous superfamilies


Domain relationships



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 very large inducible GTPase (VLIG) family contributes to the cellular response to both type I and type II interferons (IFNs). Phylogenetically, the VLIG family is relatively old, since there are representatives in zebrafish and salmon. The potential GTP-binding activity of mouse VLIG-1, the prototype VLIG, 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. The G4 motif ([NT]-K-x-D), associated in canonical GTPases with contact to the guanine base, is not immediately apparent [PMID: 11916378, PMID: 12874213].

This entry represents the VLIG-type G domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005525 GTP binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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