| Primary Identifier | IPR034348 | Type | Domain |
| Short Name | RLI_dom_1 |
| description | This entry represents an N-terminal domain of the ABC ATPase, RNase L inhibitor (RLI). RLI is also known as ABCE1, which contains two nucleotide-binding domains (NBDs) typical of the ABC transporter protein superfamily []; however, it lacks the transmembrane domains required for membrane transport functions [, ].RLI is a key enzyme in ribosomal biogenesis, formation of translation pre-initiation complexes, and assembly of HIV capsids [, ]. RLI1 was first identified as an endoribonuclease inhibitor that interacts directly with RNase L to prevent it from binding 2-5A (5'-phosphorylated 2',5'-linked oligo- adenylates) []. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft []. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology. |
