InterPro domain: IPR044126

Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue [ 1 ]. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria.

This entry represents the S1-like domain found in alpha subunit of both eukaryotic and archaeal translation initiator factor 2. The S1 domain is a RNA binding domain identified in Escherichia coli polynucleotide phosphorylase [ 2 ].

1. Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha. J. Biol. Chem. 277, 17057-61
2. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 88, 235-42