eIF2B_5domain present in translation initiation factor eIF2B and eIF5
|SMART accession number:||SM00653|
|Interpro abstract (IPR002735):|
The beta subunit of archaeal and eukaryotic translation initiation factor 2 (IF2beta) and the N-terminal domain of translation initiation factor 5 (IF5) show significant sequence homology [(PUBMED:11980477)]. Archaeal IF2beta contains two independent structural domains: an N-terminal mixed alpha/beta core domain (topological similarity to the common core of ribosomal proteins L23 and L15e), and a C-terminal domain consisting of a zinc-binding C4 finger [(PUBMED:14978306)]. Archaeal IF2beta is a ribosome-dependent GTPase that stimulates the binding of initiator Met-tRNA(i)(Met) to the ribosomes, even in the absence of other factors [(PUBMED:17608795)]. The C-terminal domain of eukaryotic IF5 is involved in the formation of the multi-factor complex (MFC), an important intermediate for the 43S pre-initiation complex assembly [(PUBMED:16781736)]. IF5 interacts directly with IF1, IF2beta and IF3c, which together with IF2-bound Met-tRNA(i)(Met) form the MFC.
This entry represents both the N-terminal and zinc-binding domains of IF2, as well as a domain in IF5.
|GO process:||translational initiation (GO:0006413)|
|GO function:||translation initiation factor activity (GO:0003743)|
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