|PROSITE documentation PDOC00945 [for PROSITE entry PS01231]|
In Escherichia coli, the trmA protein is a tRNA (uracil-5-)-methyltransferase (EC 188.8.131.52) that catalyzes the S-adenosylmethionine dependent methylation of U54 in all tRNAs. Orthologs of trmA are found in many eubacterial species. A number of uncharacterized homologs of trmA have been found :
It is probable that ygcA/HI0333 and HI0958 are probably responsible for the methylation of U747 and U1939 in 23S rRNA. In trmA, a cysteine is known to participate in the catalytic mechanism by forming a covalent adduct to C6 of uracil.
We selected two conserved regions as signature patterns, the first includes the active site cysteine and the second one, located at the C-terminal end, contains a conserved histidine.Last update:
April 2006 / Patterns revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Gustafsson C. Reid R. Greene P.J. Santi D.V.|
|Title||Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes.|
|Source||Nucleic Acids Res. 24:3756-3762(1996).|