InterPro : IPR009022

Name  Elongation factor G, III-V domain Short Name  EFG_III-V
Type  Domain Description  EF2 (or EFG) participates in the elongation phase of protein synthesis by promoting the GTP-dependent translocation of the peptidyl tRNA of the nascent protein chain from the A-site (acceptor site) to the P-site (peptidyl tRNA site) of the ribosome. EF2 also has a role after the termination phase of translation, where, together with the ribosomal recycling factor, it facilitates the release of tRNA and mRNA from the ribosome, and the splitting of the ribosome into two subunits []. EF2 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. Domains III and V have the same fold (although they are not completely superimposable and domain III lacks some of the superfamily characteristics), consisting of an alpha/beta sandwich with an antiparallel beta-sheet in a (beta/alpha/beta)x2 topology []. This double split beta/alpha/beta fold is also seen in a number of ribonucleotide binding proteins. It is the most common motif occurring in the translation system and is referred to as the ribonucleoprotein (RNP) or RNA recognition (RRM) motif. This domain is found in EF2 proteins from both prokaryotes and eukaryotes, as well as in some tetracycline resistance proteins, peptide chain release factors [], and in the C-terminal region of the bacterial hypothetical protein, YigZ.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR015269 Uncharacterised domain UPF0029, Impact, C-terminal UPF0029_Impact_C Domain

0 Contains

7 Found In

Id Name Short Name Type
IPR002140 Ribosome maturation protein SBDS Ribosome_maturation_pr_SBDS Family
IPR004540 Translation elongation factor EFG/EF2 Transl_elong_EFG/EF2 Family
IPR006298 GTP-binding protein TypA TypA_GTP-bd Family
IPR004548 Peptide chain release factor 3 PrfC Family
IPR004543 Translation elongation factor EFG/EF2, archaeal Transl_elong_EFG/EF2_arc Family
IPR006297 Elongation factor 4 EF-4 Family
IPR015796 Impact family, bacterial/archaeal Impact_bac/arc Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Laurberg M Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. 2000 J Mol Biol 303 593-603
Wintermeyer W Translational elongation factor G: a GTP-driven motor of the ribosome. 2000 Essays Biochem 35 117-29
Ito K Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. 1996 Proc Natl Acad Sci U S A 93 5443-8



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)