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UniProt functional annotation for Q5SM16 | ||
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| UniProt code: Q5SM16. |
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| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
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| Function: | |
Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type I methylase, which methylates all tRNAs. {ECO:0000269|PubMed:11918670, ECO:0000269|PubMed:15062082, ECO:0000269|PubMed:20053984, ECO:0000269|PubMed:23867454}. |
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| Catalytic activity: | |
Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O- methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-COMP:10192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.34; Evidence={ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000269|PubMed:11918670, ECO:0000269|PubMed:15062082, ECO:0000269|PubMed:20053984, ECO:0000269|PubMed:23867454}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=10 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15062082}; Vmax=10 umol/h/mg enzyme {ECO:0000269|PubMed:15062082}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:15062082}. |
| Domain: | |
Both N- and C-terminal regions function in tRNA binding, but the substrate tRNA is determined by the catalytic domain. {ECO:0000269|PubMed:23867454}. |
| Miscellaneous: | |
Binding of TrmH to tRNA is composed of at least three steps: the first is bi-molecular binding and the subsequent two are uni-molecular induced-fit processes. {ECO:0000269|PubMed:20053984}. |
| Similarity: | |
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. {ECO:0000255|HAMAP- Rule:MF_02060, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.