| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
The RimM protein is essential for efficient processing of 16S rRNA [1]. The RimM protein was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes [1]. This N-terminal domain is found associated with a PRC-barrel domain [2].
The RimM protein is essential for efficient processing of 16S rRNA [PUBMED:9422595]. It was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes [PUBMED:9422595]. RimM contains a characteristic N-terminal domain and a PRC-barrel C-terminal domain, linked by an unstructured region [PUBMED:17616598]. The N-terminal domain folds into a closed beta-barrel structure.
Bylund GO, Wipemo LC, Lundberg LA, Wikstrom PM; , J Bacteriol 1998;180:73-82.: RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli. PUBMED:9422595 EPMC:9422595 .
Anantharaman V, Aravind L; , Genome Biol 2002;3:RESEARCH0061.: The PRC-barrel: a widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism. PUBMED:12429060 EPMC:12429060.
