The domain within your query sequence starts at position 124 and ends at position 195; the E-value for the SpoU_sub_bind domain shown below is 1.99e-5.

LLEGRRLIADALKAGAVPKAFFFSRLEYVKELPVDKLKDVSLIKVKFEDIKDWSDLVTPQ
GIMGIFAKPDPV

SpoU_sub_bind

RNA 2'-O ribose methyltransferase substrate binding
SpoU_sub_bind
SMART accession number:SM00967
Description: This domain is a RNA 2'-O ribose methyltransferase substrate binding domain.
Interpro abstract (IPR013123):

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 [ (PUBMED:8266080) (PUBMED: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 [ (PUBMED: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 [ (PUBMED:11698387) (PUBMED:8266080) ]. This domain forms a four-stranded mixed beta sheet similar to that found in other RNA binding enzymes [ (PUBMED:12377117) ]. It shows considerable conformational flexibility which is thought to be important for its ability to bind RNA.

GO function:methyltransferase activity (GO:0008168)
Family alignment:
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There are 29726 SpoU_sub_bind domains in 29725 proteins in SMART's nrdb database.

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