InterPro domain: IPR035649

Elongation factor G (EFG) is folded into five domains, with domains I and II forming the N-terminal block, domains IV and V forming the C-terminal block, and domain III providing the covalently-linked flexible connection between the two [ 1 ].

This entry consists of domains similar to the C-terminal domain (domain V) of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C terminus of mitochondrial elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins [ 2 ].

1. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. J. Mol. Biol. 303, 593-603
2. Identification and characterization of two novel human mitochondrial elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved through evolution. Hum. Genet. 109, 542-50