InterPro domain: IPR004160

Elongation factor EF1A (also known as EF-1alpha or EF-Tu) promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. EF1A consists of three structural domains. Release factor eRF3, which governs translation termination, has a similar overall structure. RF3 has an N-terminal extension and a EF1A-like C-terminal region which comprises a GTP-binding domain (G domain) and two beta-barrel domains that are similar to the three respective domains of elongation factor EF-Tu/eEF1A [ 1 ]. Archaeal EF1A is both involved in translational elongation and termination, as well as in mRNA surveillance, which explains the lack of an eRF3 orthologue in archaea [ 2 ].

This entry represents the C-terminal domain of both EF1A and eRF3, which adopts a beta-barrel structure. In EF1A, this domain is involved in binding to both charged tRNA and to EF1B (or EF-Ts, IPR001816 ) [ 3 ].

1. The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100, 311-21
2. Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination, and quality control of protein synthesis. Proc. Natl. Acad. Sci. U.S.A. 107, 19242-7
3. Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Nat. Struct. Biol. 4, 650-6