Modomics - A Database of RNA Modifications

Full name: tRNA (cytosine(38)-C(5))-methyltransferase
GI: 4758184
COG: COG0270
UniProt: O14717
Structures: | 1G55 |
Enzyme type: methyltransferase
Position of modification - modification: t:38 - m5C


Dnmt2 is a methyltransferase with high sequence similarity to various enzymes from the eukaryotic DNA:methyltransferase family, which includes in particular Dnmt1 and Dnmt3 enzymes. Although it uses the same catalytic residues as other Dnmt enzymes, DNA methylation activity producing dm5C by Dnmt2 is weak, and both its existence and biological role are controversial. Instead, the enzmye displays robust tRNA Methylation activity to yield m5C at position 38 of tRNAs in vitro and in vivo. Mammalian substrates include tRNAs Asp, Gly, and Val. Dnmt2 homologues are widespread in eukaryotes, including certain single cellular eukaroytes, but only one bacterial homologue is known. Active enzymes have been confirmed in mammalia, Drosophila melanogaster, Saccharomyces pombe, and Entamoeba histolytica.

Protein sequence:


Enzymatic activities:

Reaction Substrate Type Position
C:m5C tRNA (t) Asp/8UC/unknown 38


Title Authors Journal Details PubMed Id DOI
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 TH... Science [details] 16424344 -
Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Dong A, Yoder JA, Zhang X, Zhou L, Bestor TH, Cheng X... Nucleic Acids Res [details] 11139614 -



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