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| PROSITE documentation PDOC00945 |
RNA methyltransferase trmA family signatures
In Escherichia coli, the trmA protein is a tRNA (uracil-5-)-methyltransferase (EC 2.1.1.35) 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 [1]:
- Escherichia coli hypothetical protein ygcA and HI0333, the corresponding Haemophilus influenzae protein.
- Haemophilus influenzae hypothetical protein HI0958.
- Chlamydia trachomatis protein HOM1.
- Fission yeast hypothetical protein SpAC4G8.07c.
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.
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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). | |
| PubMed ID | 8871555 |
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