InterPro : IPR000795

Name  Elongation factor, GTP-binding domain Short Name  EF_GTP-bd_dom
Type  Domain Description  Elongation factors belong to a family of proteins that promote the GTP-dependent binding of aminoacyl tRNA to the A site of ribosomes during protein biosynthesis, and catalyse the translocation of the synthesised protein chain from the A to the P site. The proteins are all relatively similar in the vicinity of their C-termini, and are also highly similar to a range of proteins that includes the nodulation Q protein from Rhizobium meliloti(Sinorhizobium meliloti), bacterial tetracycline resistance proteins []and the omnipotent suppressorprotein 2 from yeast. In both prokaryotes and eukaryotes, there are three distinct types of elongation factors, EF-1alpha (EF-Tu), which binds GTP and an aminoacyl-tRNAand delivers the latter to the A site of ribosomes; EF-1beta (EF-Ts), which interacts with EF-1a/EF-Tu to displace GDP and thus allows theregeneration of GTP-EF-1a; and EF-2 (EF-G), which binds GTP and peptidyl-tRNA and translocates the latter from the A site to the P site. In EF-1-alpha, a specific region has been shown []to be involved in a conformational change mediated by the hydrolysis of GTP to GDP. This region is conserved in both EF-1alpha/EF-Tu as well as EF-2/EF-G and thus seems typical for GTP-dependent proteins which bind non-initiator tRNAs to the ribosome. The GTP-binding protein synthesis factor family also includes the eukaryotic peptide chain release factor GTP-binding subunits []and prokaryotic peptide chain release factor 3 (RF-3) []; the prokaryotic GTP-binding protein lepA and its homologue in yeast(GUF1) and Caenorhabditis elegans(ZK1236.1); yeast HBS1 []; rat statin S1 []; and the prokaryotic selenocysteine-specific elongation factor selB [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

13 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
IPR004543 Translation elongation factor EFG/EF2, archaeal Transl_elong_EFG/EF2_arc Family
IPR006297 Elongation factor 4 EF-4 Family

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Möller W A conserved amino acid sequence around Arg-68 of Artemia elongation factor 1 alpha is involved in the binding of guanine nucleotides and aminoacyl transfer RNAs. 1987 Biochimie 69 983-9
Nelson RJ The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. 1992 Cell 71 97-105
Stansfield I The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. 1995 EMBO J 14 4365-73
LeBlanc DJ Nucleotide sequence analysis of tetracycline resistance gene tetO from Streptococcus mutans DL5. 1988 J Bacteriol 170 3618-26
Ann DK Isolation and characterization of the rat chromosomal gene for a polypeptide (pS1) antigenically related to statin. 1991 J Biol Chem 266 10429-37
Grentzmann G Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals. 1995 J Biol Chem 270 10595-600
Forchhammer K Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. 1989 Nature 342 453-6



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)