InterPro : IPR004543

Name  Translation elongation factor EFG/EF2, archaeal Short Name  Transl_elong_EFG/EF2_arc
Type  Family Description  Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [, , ]. 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 EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position [, ]. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome.This entry represents archaeal EF2 proteins (also known as aEF2), which are more similar to eukaryotic EF2 than to bacterial EF2 (or EFG), both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

8 Contains

Id Name Short Name Type
IPR009022 Elongation factor G, III-V domain EFG_III-V Domain
IPR000640 Translation elongation factor EFG, V domain EFG_V Domain
IPR009000 Translation protein, beta-barrel domain Transl_B-barrel Domain
IPR020568 Ribosomal protein S5 domain 2-type fold Ribosomal_S5_D2-typ_fold Domain
IPR004161 Translation elongation factor EFTu/EF1A, domain 2 Transl_elong_EFTu/EF1A_2 Domain
IPR005517 Translation elongation factor EFG/EF2, domain IV Transl_elong_EFG/EF2_IV Domain
IPR000795 Elongation factor, GTP-binding domain EF_GTP-bd_dom Domain
IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup Ribosomal_S5_D2-typ_fold_subgr Domain

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Frank J Ratchet-like movements between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation. 2001 Cold Spring Harb Symp Quant Biol 66 67-75
Wintermeyer W Mechanism of elongation factor G function in tRNA translocation on the ribosome. 2001 Cold Spring Harb Symp Quant Biol 66 449-58
Andersen GR Elongation factors in protein biosynthesis. 2003 Trends Biochem Sci 28 434-41
Nilsson J Elongation factors on the ribosome. 2005 Curr Opin Struct Biol 15 349-54
Andersen GR Structural studies of eukaryotic elongation factors. 2001 Cold Spring Harb Symp Quant Biol 66 425-37

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)