RNA 2-O ribose methyltransferase, substrate binding (IPR013123)

Short name: SpoU_subst-bd

Overlapping homologous superfamilies

Domain relationships



Most cellular RNAs undergo a number of post-transcriptional nucleoside modifications. While the biological role of many of these modifications is unknown, some have been shown to be necessary for cell growth or for resistance to antibiotics [PMID: 8266080, PMID: 9187657]. One of the most common modifications is 2'O-ribose methylation catalysed by the RNA 2'O-ribose methyltransferases, a large enzyme family that transfer a methyl group from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of the backbone ribose [PMID: 9917067].

This entry represents a substrate-binding domain found in a variety of bacterial and mitochondrial RNA 2'-O ribose methyltransferases. These include the bacterial enzyme RlmB, which specifically methylates the conserved nucleotide guanosine 2251 in 23S RNA, and PET56, which specifically methylates the equivalent guanosine in mitochondrial 21S RNA [PMID: 11698387, PMID: 8266080]. This domain forms a four-stranded mixed beta sheet similar to that found in other RNA binding enzymes [PMID: 12377117]. It shows considerable conformational flexibility which is thought to be important for its ability to bind RNA.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0008168 methyltransferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.