InterPro : IPR009001

Name  Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal Short Name  Transl_elong_EF1A/Init_IF2_C
Type  Domain Description  A beta barrel of circularly permuted topology is found in the C terminus of many translation elongation and initiation factors. This domain is found in the elongation factors EF1A (or EF-Tu) of both eukaryotes and prokaryotes, which functions to recognise and transport aminoacyl-tRNA to the acceptor (A) site of the ribosome during the elongation process [, ]. This domain is also found in the initiation factor IF2 gamma subunit of eukaryotes [], which functions to transport the initiator methionyl-tRNA to the ribosome. The C-terminal extension of mitochondrial EF1A (or EF-Tu) has structural similarities with DNA recognising zinc fingers, suggesting that the extension may be involved in recognition of RNA.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR004160 Translation elongation factor EFTu/EF1A, C-terminal Transl_elong_EFTu/EF1A_C Domain
IPR015256 Translation initiation factor 2, gamma subunit, C-terminal TIF2_gsu_C Domain

0 Contains

4 Found In

Id Name Short Name Type
IPR004541 Translation elongation factor EFTu/EF1A, bacterial/organelle Transl_elong_EFTu/EF1A_bac/org Family
IPR004535 Translation elongation factor, selenocysteine-specific Transl_elong_SelB Family
IPR011779 Sulphate adenylyltransferase, large subunit SO4_adenylTrfase_lsu Family
IPR022424 Translation initiation factor 2, gamma subunit TIF2_gsu Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Andersen GR Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. 2000 Mol Cell 6 1261-6
Andersen GR High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. 2000 J Mol Biol 297 421-36
Schmitt E The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. 2002 EMBO J 21 1821-32

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)