{PDOC51709}
{PS51709; G_TRME}
{BEGIN}
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* TrmE-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.

TrmE (also  called MnmE) contains a canonical G domain and is conserved in all
three kingdoms  of  life.  It is involved in the modification of uridine bases
(U34) at  the  first  anticodon (wobble) position of tRNAs decoding two-family
box triplets.  TrmE  is  organized  as  a multidomain protein consisting of an
~220-amino acid  N-terminal  domain,  probably  required  for self-assembly, a
middle GTPase  domain, of about 160 residues, and an ~75-amino acid C-terminal
domain, which  contains a  highly conserved CxGK motif. TrmE contains at least
four of  the  five  conserved  nucleotide-binding motifs G1 (GxxxxGK[ST] or P-
loop), G2  (T),  G3  (DxxG) and G4 ([NT]KxD). The totally invariant alanine in
the SA[KL]  (G5)  motif  of  Ras  anGalph  proteins  is  less  well  conserved
[1,2,3,4,5].

The structure  of  the  TrmE-type G domain consists of a central four-stranded
beta-sheet flanked  by  five alpha-helices (see <PDB:1XZP>). It dimerises in a
potassium-dependent manner [4,5].

The profile we developed covers the entire TmrE-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: March 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] Yamanaka K., Hwang J., Inouye M.
     "Characterization of GTPase activity of TrmE, a member of a novel
     GTPase superfamily, from Thermotoga maritima."
     J. Bacteriol. 182:7078-7082(2000).
     PubMed=11092873
[ 3] Yim L., Martinez-Vicente M., Villarroya M., Aguado C., Knecht E.,
     Armengod M.-E.
     "The GTPase activity and C-terminal cysteine of the Escherichia coli
     MnmE protein  are essential for its tRNA modifying function."
     J. Biol. Chem. 278:28378-28387(2003).
     PubMed=12730230; DOI=10.1074/jbc.M301381200
[ 4] Scrima A., Vetter I.R., Armengod M.E., Wittinghofer A.
     "The structure of the TrmE GTP-binding protein and its implications
     for tRNA modification."
     EMBO J. 24:23-33(2005).
     PubMed=15616586; DOI=10.1038/sj.emboj.7600507
[ 5] Monleon D., Martinez-Vicente M., Esteve V., Yim L., Prado S.,
     Armengod M.-E., Celda B.
     "Structural insights into the GTPase domain of Escherichia coli MnmE
     protein."
     Proteins 66:726-739(2007).
     PubMed=17143896; DOI=10.1002/prot.21186

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