{PDOC01001}
{PS50040; EF1G_C}
{BEGIN}
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* Elongation factor 1 (EF-1) gamma C-terminal domain profile *
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Eukaryotic elongation  factor  1  (EF-1)  is responsible for the GTP-dependent
binding of aminoacyl-tRNAs  to  the ribosomes [1].  EF-1  is  composed of four
subunits:  the alpha chain which  binds GTP  and  aminoacyl-tRNAs,   the gamma
chain that probably plays  a  role in anchoring the complex to other  cellular
components and  the  beta  and  delta  (or beta') chains. The gamma chain is a
protein of  about  410  to  440  residues,  which  consists of two independent
domains, a   glutathione  S-transferase  (GST)  homologous  N-terminal  region
responsible for  the  interaction  with  EF-1  alpha  and  a  highly conserved
exceptionally protease resistant ~160 residue C-terminal domain [2].

The structure  of the EF-1 gamma C-terminal domain consists of a five-stranded
antiparallel beta-sheet  surrounded  by  five  alpha-helices  and  resembles a
contact lens  (see  <PDB:1PBU>). The EF-1 gamma C-terminal domain  contains an
usually high  number  of aromatic amino acids. These residues pack together in
two clusters,  which  are located on opposite faces of the central beta-sheet.
The distribution  of the surface-exposed, conserved residues in the EF-1 gamma
C-terminal domain  is  highly  asymmetric. The concave surface and part of the
edge surrounding  it contain the majority of the conserved amino acids whereas
the convex  surface is relatively poorly conserved. It has been suggested that
the concave face of the EF-1 gamma C-terminal domain might be involved in some
biologically relevant interface(s) [2].

The profile we developed covers the entire EF-1 gamma C-terminal domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2005 / Text and profile revised.

[ 1] Riis B., Rattan S.I., Clark B.F.C., Merrick W.C.
     "Eukaryotic protein elongation factors."
     Trends Biochem. Sci. 15:420-424(1990).
     PubMed=2278101
[ 2] Vanwetswinkel S., Kriek J., Andersen G.R., Guentert P., Dijk J.,
     Canters G.W., Siegal G.
     "Solution structure of the 162 residue C-terminal domain of human
     elongation factor 1Bgamma."
     J. Biol. Chem. 278:43443-43451(2003).
     PubMed=12920118; DOI=10.1074/jbc.M306031200

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