Prediction of a novel RNA 2'-O-ribose methyltransferase subfamily encoded by the Escherichia coli YgdE open reading frame and its orthologs.
The amino acid sequence of the RNA 2'-O-ribose methyltranserase RrmJ was used as a probe for detecting putative homologs through iterative searches of genomic databases. We found a previously unannotated YgdE open reading frame (ORF) in the genome sequences of Escherichia coli and other gamma-Proteobacteria, which shares key features with RrmJ, despite the mutual sequence similarity of these proteins is relatively low. The predicted structural compatibility and the conservation of all functionally important residues between RrmJ and YgdE strongly suggests that the newly identified methyltranserase also modifies 2'-OH groups of ribose. The N-terminal region of YgdE, which has no counterpart in RrmJ, is predicted to form an independent domain, possibly involved in target recognition.
Bujnicki
J M
JM
Bioinformatics Laboratory, International Institute of Molecular and Cell Biology, Warsaw, Poland. iamb@bioinfo.pl
Rychlewski
L
L
D000595:Amino Acid Sequence; D019992:Databases as Topic; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000235:genetics; D008780:Methyltransferases / Q000235:genetics*; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D029968:Escherichia coli Proteins; C096452:FtsK protein, E coli; D008565:Membrane Proteins; D008780:Methyltransferases; C035181:rRNA (adenosine-O-2'-)methyltransferase