Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q12383 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Trm13p belongs to the RFM superfamily of MTases despite the absence of a significant sequence similarity to previously characterized members of this superfamily. The model reveals residues potentially responsible for cofactor binding, tRNA binding, and catalysis of the 2'-O-methylation reaction. The model suggests a presence of one to three disulfide bonds and/or metal ion binding site next to the substrate binding pocket | Saccharomyces cerevisiae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Trm13p | - |
Saccharomyces cerevisiae |
tRNA:Xm4 modification enzyme | - |
Saccharomyces cerevisiae |