PROSITE documentation PDOC51717
Very large inducible GTPase (VLIG)-type guanine nucleotide-binding (G) domain profile


The P-loop (see <PDOC00017>) 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 [1,2].

The profile we developed covers the entire VLIG-type G domain.

Last update:

April 2014 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

G_VLIG, PS51717; Very large inducible GTPASE (VLIG)-type guanine nucleotide-binding (G) domain profile  (MATRIX)


1AuthorsLeipe D.D. Wolf Y.I. Koonin E.V. Aravind L.
TitleClassification and evolution of P-loop GTPases and related ATPases.
SourceJ. Mol. Biol. 317:41-72(2002).
PubMed ID11916378

2AuthorsKlamp T. Boehm U. Schenk D. Pfeffer K. Howard J.C.
TitleA giant GTPase, very large inducible GTPase-1, is inducible by IFNs.
SourceJ. Immunol. 171:1255-1265(2003).
PubMed ID12874213

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