Protein Domain : eIF3B, RNA recognition motif IPR034363

Type	Domain
Description	This entry represents the RNA recognition motif (RRM) found in eukaryotic translation initiation factor 3 (eIF-3), a large multisubunit complex that plays a central role in the initiation of translation by binding to the 40 S ribosomal subunit and promoting the binding of methionyl-tRNAi and mRNA. eIF-3B is the major scaffolding subunit of eIF-3. It interacts with eIF-3 subunits A, G, I, and J [ ]. eIF-3B contains an N-terminal RNA recognition motif (RRM), which is involved in the interaction with eIF-3J. The interaction between eIF-3B and eIF-3J is crucial for the eIF-3 recruitment to the 40 S ribosomal subunit []. eIF-3B also binds directly to domain III of the internal ribosome-entry site (IRES) element of hepatitis-C virus (HCV) RNA through its N-terminal RRM, which may play a critical role in both cap-dependent and cap-independent translation []. Additional research has shown that eIF-3B may function as an oncogene in glioma cells and can be served as a potential therapeutic target for anti-glioma therapy []. Proteins containing this domain also include eIF-3 yeast homologue subunit B (also termed Prt1) that interacts with the yeast homologues of eIF-3 subunits A(TIF32), G(TIF35), I(TIF34), J(HCR1), and E(Pci8). In yeast, eIF-3B (Prt1) contains an N-terminal RRM that is directly involved in the interaction with eIF-3A (TIF32) and eIF-3J (HCR1) [ ]. In contrast to its human homologue, yeast eIF-3B (Prt1) may have potential to bind its total RNA through its RRM [].
Short Name	eIF3B_RRM