{PDOC51717}
{PS51717; G_VLIG}
{BEGIN}
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* Very large inducible GTPase (VLIG)-type guanine nucleotide-binding (G) domain profile *
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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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2014 / First entry.

[ 1] Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L.
     "Classification and evolution of P-loop GTPases and related ATPases."
     J. Mol. Biol. 317:41-72(2002).
     PubMed=11916378; DOI=10.1006/jmbi.2001.5378
[ 2] Klamp T., Boehm U., Schenk D., Pfeffer K., Howard J.C.
     "A giant GTPase, very large inducible GTPase-1, is inducible by
     IFNs."
     J. Immunol. 171:1255-1265(2003).
     PubMed=12874213

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