InterPro : IPR004539

Name  Translation elongation factor EF1A, eukaryotic/archaeal Short Name  Transl_elong_EF1A_euk/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.EF1A (also known as EF-1alpha or EF-Tu) is a G-protein. It forms a ternary complex of EF1A-GTP-aminoacyltRNA. The binding of aminoacyl-tRNA stimulates GTP hydrolysis by EF1A, causing a conformational change in EF1A that causes EF1A-GDP to detach from the ribosome, leaving the aminoacyl-tRNA attached at the A-site. Only the cognate aminoacyl-tRNA can induce the required conformational change in EF1A through its tight anticodon-codon binding [, ]. EF1A-GDP is returned to its active state, EF1A-GTP, through the action of another elongation factor, EF1B (also known as EF-Ts or EF-1beta/gamma/delta).This entry represents EF1A proteins from in eukaryotic (eEF1alpha) and archaeal (aEF1alpha) organisms, these proteins being more closely related to one another than to EF1A (or EF-Tu) from bacteria ().Archaeal EF1-alpha is not only involved in translation elongation. It interacts with Pelota, a mRNA surveillance protein involved in no-go mRNA decay and non-stop mRNA decay; and with RF1, a tRNA-mimicking protein which recognises stop codons and catalyses polypeptide-chain release. Through these interactions archaeal EF1-alpha also has a role in translational termination and mRNA surveillance pathways [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

3 Contains

Id Name Short Name Type
IPR004161 Translation elongation factor EFTu/EF1A, domain 2 Transl_elong_EFTu/EF1A_2 Domain
IPR004160 Translation elongation factor EFTu/EF1A, C-terminal Transl_elong_EFTu/EF1A_C Domain
IPR000795 Elongation factor, GTP-binding domain EF_GTP-bd_dom Domain

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
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
Rodnina MV Recognition and selection of tRNA in translation. 2005 FEBS Lett 579 938-42
Krab IM Mechanisms of EF-Tu, a pioneer GTPase. 2002 Prog Nucleic Acid Res Mol Biol 71 513-51
Saito K Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination, and quality control of protein synthesis. 2010 Proc Natl Acad Sci U S A 107 19242-7

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)