NametRNA (cytosine(38)-C(5))-methyltransferase
Synonyms
  • 2.1.1.204
  • DNA (cytosine-5)-methyltransferase-like protein 2
  • DNA methyltransferase homolog HsaIIP
  • DNA MTase homolog HsaIIP
  • DNMT2
  • M.HsaIIP
  • PuMet
Gene NameTRDMT1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0004943|tRNA (cytosine(38)-C(5))-methyltransferase
MEPLRVLELYSGVGGMHHALRESCIPAQVVAAIDVNTVANEVYKYNFPHTQLLAKTIEGI
TLEEFDRLSFDMILMSPPCQPFTRIGRQGDMTDSRTNSFLHILDILPRLQKLPKYILLEN
VKGFEVSSTRDLLIQTIENCGFQYQEFLLSPTSLGIPNSRLRYFLIAKLQSEPLPFQAPG
QVLMEFPKIESVHPQKYAMDVENKIQEKNVEPNISFDGSIQCSGKDAILFKLETAEEIHR
KNQQDSDLSVKMLKDFLEDDTDVNQYLLPPKSLLRYALLLDIVQPTCRRSVCFTKGYGSY
IEGTGSVLQTAEDVQVENIYKSLTNLSQEEQITKLLILKLRYFTPKEIANLLGFPPEFGF
PEKITVKQRYRLLGNSLNVHVVAKLIKILYE
Number of residues391
Molecular Weight44596.17
Theoretical pI5.95
GO Classification
Functions
  • DNA (cytosine-5-)-methyltransferase activity
  • RNA binding
  • tRNA methyltransferase activity
Processes
  • C-5 methylation of cytosine
  • tRNA modification
  • tRNA processing
  • gene expression
  • response to amphetamine
  • tRNA methylation
Components
  • cytoplasm
  • nucleoplasm
General FunctionTrna methyltransferase activity
Specific FunctionSpecifically methylates cytosine 38 in the anticodon loop of tRNA(Asp).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDO14717
UniProtKB Entry NameTRDMT_HUMAN
Cellular LocationNucleus
Gene sequence
>lcl|BSEQ0011795|tRNA (cytosine(38)-C(5))-methyltransferase (TRDMT1)
ATGGAGCCCCTGCGGGTGCTGGAGCTATACAGCGGCGTGGGCGGCATGCACCACGCGCTG
AGAGAAAGCTGTATACCTGCACAAGTGGTGGCTGCCATTGATGTCAACACTGTCGCTAAT
GAAGTATACAAGTATAATTTTCCTCACACACAGTTACTTGCCAAGACGATTGAAGGCATT
ACACTCGAAGAGTTTGACAGATTATCTTTTGATATGATTTTAATGAGCCCTCCCTGCCAG
CCATTCACAAGGATTGGCCGGCAGGGTGATATGACTGATTCAAGGACGAATAGCTTCTTA
CATATTCTAGATATTCTCCCAAGATTACAAAAATTACCAAAGTATATTCTTTTGGAAAAT
GTTAAAGGTTTTGAAGTATCTTCTACAAGAGACCTCTTGATACAAACAATAGAAAATTGT
GGCTTTCAGTACCAAGAGTTTCTATTATCTCCAACCTCTCTTGGCATTCCAAATTCAAGG
CTACGATATTTTCTTATTGCAAAGCTTCAGTCAGAGCCATTACCCTTTCAAGCCCCTGGT
CAGGTACTGATGGAGTTCCCCAAAATTGAATCTGTACATCCACAAAAATATGCAATGGAT
GTAGAAAATAAAATTCAAGAAAAGAACGTTGAACCAAATATTAGCTTTGATGGCAGCATA
CAGTGTTCTGGAAAAGATGCCATTCTTTTTAAGCTTGAAACTGCAGAAGAAATTCACAGG
AAAAATCAACAAGATAGTGATCTCTCTGTGAAAATGCTAAAAGATTTTCTTGAAGATGAC
ACTGACGTGAACCAGTATCTTTTACCACCAAAGTCATTGCTGCGATATGCTCTTCTGTTA
GACATTGTTCAGCCCACTTGTAGAAGGTCCGTGTGCTTTACCAAAGGATATGGAAGCTAC
ATAGAAGGGACAGGGTCTGTGTTACAGACTGCAGAGGATGTGCAGGTTGAGAATATCTAC
AAATCCCTTACCAATTTGTCACAAGAAGAACAGATAACAAAGCTGTTAATACTTAAACTG
CGATATTTCACTCCTAAAGAAATAGCAAATCTCCTTGGATTTCCTCCAGAGTTCGGATTT
CCTGAGAAGATAACAGTGAAACAGCGTTATCGCCTACTTGGAAATAGTCTCAACGTGCAT
GTAGTAGCTAAACTAATCAAAATCTTATATGAATAA
GenBank Gene IDAF012128
GeneCard IDNot Available
GenAtlas IDTRDMT1
HGNC IDHGNC:2977
Chromosome Location10
Locus10p15.1
References
  1. Yoder JA, Bestor TH: A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast. Hum Mol Genet. 1998 Feb;7(2):279-84. 9425235
  2. Van den Wyngaert I, Sprengel J, Kass SU, Luyten WH: Cloning and analysis of a novel human putative DNA methyltransferase. FEBS Lett. 1998 Apr 17;426(2):283-9. 9599025
  3. Okano M, Xie S, Li E: Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells. Nucleic Acids Res. 1998 Jun 1;26(11):2536-40. 9592134
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  6. Franchina M, Hooper J, Kay PH: Five novel alternatively spliced transcripts of DNA (cytosine-5) methyltransferase 2 in human peripheral blood leukocytes. Int J Biochem Cell Biol. 2001 Nov;33(11):1104-15. 11551826
  7. Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH: Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2. Science. 2006 Jan 20;311(5759):395-8. 16424344
  8. Dong A, Yoder JA, Zhang X, Zhou L, Bestor TH, Cheng X: Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Nucleic Acids Res. 2001 Jan 15;29(2):439-48. 11139614