2.1.1.204: tRNA (cytosine38-C5)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (cytosine38-C5)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.204
-
2.1.1.204
-
methyltransferases
-
n6-methyladenosine
-
5-methylcytosine
-
mtases
-
2'-o-methylation
-
epitranscriptomic
-
methyltransferase-like
-
2'-o-methyltransferase
-
piwi-interacting
-
mettl16
-
spout
- 2.1.1.204
- methyltransferases
- n6-methyladenosine
- 5-methylcytosine
- mtases
-
2'-o-methylation
-
epitranscriptomic
-
methyltransferase-like
-
2'-o-methyltransferase
-
piwi-interacting
- mettl16
-
spout
Reaction
Synonyms
(cytosine-5) RNA methyltransferase, cytosine-5 tRNA methyltransferase, dDnmt2, DNA methyltransferase 2, DnmA, Dnmt2, DNMT2 methyltransferase, EC 2.1.1.29, hDNMT2, Pf-DNMT2, PMT1, pombe methyltransferase 1, RCMT, RNA methyltransferase, spDnmt2, transfer RNA aspartic acid methyltransferase 1, TRDMT1, tRNA aspartic acid methyltransferase 1, tRNA-aspartic acid methyltransferase 1
ECTree
2.1.1.204 tRNA (cytosine38-C5)-methyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.1.1.204 - tRNA (cytosine38-C5)-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C292A
-
about 3fold reduction in RNA binding affinity. Significant residual activity
C79A
D217H
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D226Y
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D255Y
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E119A
E185K
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E202Q
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E317G
-
site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme
E63K
-
site-directed mutagenesis, the mutation causes a twofold increase in activity compared to the wild-type enzyme
G155S
-
site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme
K122A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K168A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K196A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K241A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
K251A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
K254A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K271A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K295A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K346A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K363A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K367A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K387A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
L257V
-
site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme
M72I
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
N264S
-
site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme
R160A
R162A
R240A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
R275A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R288A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
R289A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R369A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
R371A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R84A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R95A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
C79A
-
about 3fold reduction in RNA binding affinity. No detectable in vitro methylation activity
E119A
-
mutant binds stronger to RNA than wild-type. No detectable in vitro methylation activity
additional information
homozygous Dnmt2-null mutations are viable and fertile, long-term cultivation of Dnmt2 mutant animals might introduce genomic changes accounting for some of the observed phenotypes. Generation of Dnmt2 mutant allele (Dnmt2DELTA5.4), which shows loss of RNA methylation at known tRNA substrates. Catalytically mutant Dnmt2 rescues transposable element (TE) expression changes. Recombinant ectopic expression of the catalytically inactive mutant Dnmt2, which does not reconstitute tRNA methylation, also normalizes TE expression levels. RNAi-mediated knockdown of Dnmt2 in follicle cells. Spliced Gypsy mRNA is significantly elevated in Dnmt2 mutants after heat shock, but not in controls, functional Gypsy retroviral particles can be formed in Dnmt2 mutants. Specific eccDNAs accumulate in RCMT mutants. RCMT mutants display reduced tRNA stability and tRNA abundance
additional information
generation of Dnmt2 knockout murine embryonic fibroblast cells
additional information
-
generation of Dnmt2 knockout murine embryonic fibroblast cells
additional information
construction of enzyme mutant Pf-NDELTATRDMT1 lacking the N-terminus. The Pf-NDELTATRDMT1 protein consists of motifs specific for both DNA and tRNA methyltransferases, substrate specificity analysis reveals that no DNA methylation activity can be detected, but Pf-NDELTATRDMT1 methylates only tRNA-Asp and very weakly tRNA-Val
