InterPro : IPR004161

Name  Translation elongation factor EFTu/EF1A, domain 2 Short Name  Transl_elong_EFTu/EF1A_2
Type  Domain 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).EF1A consists of three structural domains. This entry represents domain 2 of EF2, which adopts a beta-barrel structure, and is involved in binding to both charged tRNA []. This domain is structurally related to the C-terminal domain of EF2 (), to which it displays weak sequence matches. This domain is also found in other proteins such as translation initiation factor IF-2 and tetracycline-resistance proteins.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

14 Found In

Id Name Short Name Type
IPR004540 Translation elongation factor EFG/EF2 Transl_elong_EFG/EF2 Family
IPR004539 Translation elongation factor EF1A, eukaryotic/archaeal Transl_elong_EF1A_euk/arc Family
IPR004541 Translation elongation factor EFTu/EF1A, bacterial/organelle Transl_elong_EFTu/EF1A_bac/org Family
IPR015760 Translation initiation factor IF- 2 TIF_IF2 Family
IPR006298 GTP-binding protein TypA TypA_GTP-bd Family
IPR003285 Yeast eukaryotic release factor Yeast_ERF Family
IPR004535 Translation elongation factor, selenocysteine-specific Transl_elong_SelB Family
IPR004548 Peptide chain release factor 3 PrfC Family
IPR011779 Sulphate adenylyltransferase, large subunit SO4_adenylTrfase_lsu Family
IPR022424 Translation initiation factor 2, gamma subunit TIF2_gsu Family
IPR000178 Translation initiation factor aIF-2, bacterial-like TF_IF2_bacterial-like Family
IPR004544 Translation initiation factor aIF-2, archaea TIF_aIF-2_arc Family
IPR004543 Translation elongation factor EFG/EF2, archaeal Transl_elong_EFG/EF2_arc Family
IPR006297 Elongation factor 4 EF-4 Family

1 Parent Features

Id Name Short Name Type
IPR009000 Translation protein, beta-barrel domain Transl_B-barrel Domain

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
Nissen P Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. 1995 Science 270 1464-72

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)