RLI, domain 1 (IPR034348)

Short name: RLI_dom_1

Overlapping homologous superfamilies

Domain relationships


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 [PMID: 7539425]; however, it lacks the transmembrane domains required for membrane transport functions [PMID: 7539425,PMID: 11435397].

RLI is a key enzyme in ribosomal biogenesis, formation of translation pre-initiation complexes, and assembly of HIV capsids [PMID: 15837203, PMID: 11780123]. 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) [PMID: 7539425]. 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 [PMID: 15837203]. 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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
  • cd03236 (ABC_RNaseL_inhibitor_domain1)