InterPro : IPR004541

Name  Translation elongation factor EFTu/EF1A, bacterial/organelle Short Name  Transl_elong_EFTu/EF1A_bac/org
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 (or EF-Tu) proteins found primarily in bacteria, mitochondria and chloroplasts. Eukaryotic and archaeal EF1A () are excluded from this entry. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

5 Contains

Id Name Short Name Type
IPR009000 Translation protein, beta-barrel domain Transl_B-barrel Domain
IPR009001 Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal Transl_elong_EF1A/Init_IF2_C Domain
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
Sergiev PV How can elongation factors EF-G and EF-Tu discriminate the functional state of the ribosome using the same binding site? 2005 FEBS Lett 579 5439-42



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)