EC number:2.1.1.204

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.204
Description:tRNA (cytosine(38)-C(5))-methyltransferase.
Prosite: PDOC00089;
PDB:
PDBScop
Cath: 3.90.120.10; 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.204
BRENDA Enzyme Link: BRENDA 2.1.1.204
KEGG Enzyme Link: KEGG2.1.1.204
BioCyc Enzyme Link: BioCyc 2.1.1.204
ExPASy Enzyme Link: ExPASy2.1.1.204
EC2PDB Enzyme Link: EC2PDB 2.1.1.204
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.204
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.204
IntEnz Enzyme Link: IntEnz 2.1.1.204
MEDLINE Enzyme Link: MEDLINE 2.1.1.204

EC number:2.1.1.204

MSA:

2.1.1.204;
Phylogenetic Tree:

2.1.1.204;
Uniprot:
M-CSA:
RHEA:42956 cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism.Jurkowski TP, Meusburger M, Phalke S, Helm M, Nellen W, Reuter G, Jeltsch A2008 Aug18567810
Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2.Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH2006 Jan 2016424344