BRENDA - Enzyme Database show
show all sequences of 2.1.1.204

Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase

Jurkowski, T.P.; Shanmugam, R.; Helm, M.; Jeltsch, A.; Biochemistry 51, 4438-4444 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
phylogenetic analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
C79A
site-directed mutagenesis, inactive mutant
Homo sapiens
E119A
site-directed mutagenesis, inactive mutant
Homo sapiens
K122A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
K168A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K196A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K241A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
K251A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
K254A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K271A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K295A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
K346A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K363A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K367A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
K387A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
R160A
site-directed mutagenesis, inactive mutant
Homo sapiens
R162A
site-directed mutagenesis, inactive mutant
Homo sapiens
R240A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
R275A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R288A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
R289A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R369A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
R371A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R84A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R95A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
Homo sapiens
-
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli to over 90% purity, except for mutant R84A, which is about 75% pure
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
DNMT2 induces a conformational change in the tRNA of the DNMT2-tRNA complex
718931
Homo sapiens
?
-
-
-
-
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
718931
Homo sapiens
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
mapping of the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants. tRNA specificity determinants and tRNA binding pocket structure in the DNMT2, overview
718931
Homo sapiens
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
structural modeling of DNMT2, overview
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
phylogenetic analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C79A
site-directed mutagenesis, inactive mutant
Homo sapiens
E119A
site-directed mutagenesis, inactive mutant
Homo sapiens
K122A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
K168A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K196A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K241A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
K251A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
K254A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K271A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K295A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
K346A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K363A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
K367A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
K387A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
R160A
site-directed mutagenesis, inactive mutant
Homo sapiens
R162A
site-directed mutagenesis, inactive mutant
Homo sapiens
R240A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
Homo sapiens
R275A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R288A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
R289A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R369A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
Homo sapiens
R371A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R84A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
R95A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
Homo sapiens
-
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli to over 90% purity, except for mutant R84A, which is about 75% pure
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
DNMT2 induces a conformational change in the tRNA of the DNMT2-tRNA complex
718931
Homo sapiens
?
-
-
-
-
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
718931
Homo sapiens
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
mapping of the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants. tRNA specificity determinants and tRNA binding pocket structure in the DNMT2, overview
718931
Homo sapiens
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
structural modeling of DNMT2, overview
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
evolution
DNMT2 methylates RNA by employing a DNA methyltransferase-like catalytic mechanism, which is clearly different from the mechanism of other RNA MTases. DNMT2 has changed its substrate specificity from DNA to RNA in the course of its evolution
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
evolution
DNMT2 methylates RNA by employing a DNA methyltransferase-like catalytic mechanism, which is clearly different from the mechanism of other RNA MTases. DNMT2 has changed its substrate specificity from DNA to RNA in the course of its evolution
Homo sapiens
Other publictions for EC 2.1.1.204
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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1
-
1
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1
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1
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1
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1
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1
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1
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1
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1
1
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13
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1
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1
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1
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1
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1
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1
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1
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103-113
2015
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1
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-
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3
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6
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3
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9
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6
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3
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1
3
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3
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6
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9
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6
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9
9
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735864
Burgess
Conservation of tRNA and rRNA ...
Arabidopsis thaliana
BMC Plant Biol.
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199
2015
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1
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2
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14
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2
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2
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3
3
-
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736018
Tuorto
The tRNA methyltransferase Dnm ...
Mus musculus, Mus musculus C57BL/6
EMBO J.
34
2350-2362
2015
-
-
-
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1
-
-
-
-
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8
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2
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8
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10
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1
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1
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1
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8
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8
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10
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2
2
-
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-
736905
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Dictyostelium discoideum, Schizosaccharomyces pombe
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43
10952-10962
2015
2
-
1
-
2
-
-
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2
-
4
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2
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7
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2
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2
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2
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2
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1
2
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2
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2
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4
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7
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2
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2
-
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3
2
2
3
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736775
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193
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2014
-
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1
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736856
Khoddami
Identification of direct targe ...
Homo sapiens
Nat. Biotechnol.
31
458-464
2013
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2
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4
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1
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1
1
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718931
Jurkowski
Mapping the tRNA binding site ...
Homo sapiens
Biochemistry
51
4438-4444
2012
-
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1
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24
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1
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1
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2
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1
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3
1
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1
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1
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24
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1
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3
1
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1
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1
1
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708588
Schaefer
RNA methylation by Dnmt2 prote ...
Drosophila melanogaster
Genes Dev.
24
1590-1595
2010
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1
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1
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1
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5
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2
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1
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2
2
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710349
Schaefer
The Drosophila cytosine-5 meth ...
Drosophila melanogaster
PLoS One
3
e1414
2008
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2
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710547
Jurkowski
Human DNMT2 methylates tRNA(As ...
Drosophila melanogaster, Homo sapiens
RNA
14
1663-1670
2008
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1
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5
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1
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708586
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Dnmt2 functions in the cytopla ...
Danio rerio
Genes Dev.
21
261-266
2007
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710560
Goll
Methylation of tRNAAsp by the ...
Homo sapiens
Science
311
395-398
2006
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