Translation elongation factor, IF5A C-terminal (IPR020189)

Short name: Transl_elong_IF5A_C

Overlapping homologous superfamilies

Domain relationships



A five-stranded beta-barrel was first noted as a common structure among four proteins binding single-stranded nucleic acids (staphylococcal nuclease and aspartyl-tRNA synthetase) or oligosaccharides (B subunits of enterotoxin and verotoxin-1), and has been termed the oligonucleotide/oligosaccharide binding motif, or OB fold, a five-stranded beta-sheet coiled to form a closed beta-barrel capped by an alpha helix located between the third and fourth strands [PMID: 12769718]. Two ribosomal proteins, S17 and S1, are members of this class, and have different variations of the OB fold theme. Comparisons with other OB fold nucleic acid binding proteins suggest somewhat different mechanisms of nucleic acid recognition in each case [PMID: 9862955].

There are many nucleic acid-binding proteins that contain domains with this OB-fold structure, including anticodon-binding tRNA synthetases, ssDNA-binding proteins (CDC13, telomere-end binding proteins), phage ssDNA-binding proteins (gp32, gp2.5, gpV), cold shock proteins, DNA ligases, RNA-capping enzymes, DNA replication initiators and RNA polymerase subunit RBP8 [PMID: 15178340].

This entry represents the RNA-binding domain of translation elongation factor IF5A [PMID: 19424157].

GO terms

Biological Process

GO:0045901 positive regulation of translational elongation
GO:0045905 positive regulation of translational termination
GO:0006452 translational frameshifting

Molecular Function

GO:0003723 RNA binding
GO:0043022 ribosome binding
GO:0003746 translation elongation factor activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.