Elongation factor 1 gamma, conserved domain
SMART accession number:SM01183
Description: -
Interpro abstract (IPR001662):

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ (PUBMED:12762045) (PUBMED:15922593) (PUBMED:12932732) ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution.

Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta) [ (PUBMED:12762045) ].

This entry represents a conserved domain usually found near the C terminus of EF1B-gamma chains, a peptide of 410-440 residues. The gamma chain appears to play a role in anchoring the EF1B complex to the beta and delta chains and to other cellular components.

GO process:translational elongation (GO:0006414)
GO function:translation elongation factor activity (GO:0003746)
Family alignment:
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There are 2200 EF1G domains in 2196 proteins in SMART's nrdb database.

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