2.1.1.204	C292A	about 3fold reduction in RNA binding affinity. Significant residual activity	710547	
2.1.1.204	C79A	about 3fold reduction in RNA binding affinity. No detectable in vitro methylation activity	710547	
2.1.1.204	C79A	site-directed mutagenesis, inactive mutant	718931	
2.1.1.204	D217H	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	D226Y	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	D255Y	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	E119A	mutant binds stronger to RNA than wild-type. No detectable in vitro methylation activity	710547	
2.1.1.204	E119A	site-directed mutagenesis, inactive mutant	718931	
2.1.1.204	E185K	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	E202Q	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	E317G	site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	E63K	site-directed mutagenesis, the mutation causes a twofold increase in activity compared to the wild-type enzyme	735726	
2.1.1.204	G155S	site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme	735726	
2.1.1.204	G155V	site-directed mutagenesis, almost inactive mutant	735726	
2.1.1.204	K122A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K168A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K196A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K241A	site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K251A	site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K254A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K271A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K295A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K346A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K363A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K367A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	K387A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	L257V	site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme	735726	
2.1.1.204	M72I	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	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	756078	
2.1.1.204	additional information	generation of a DnmA-deletion mutant	736905	
2.1.1.204	additional information	generation of a Prmt1-deletion mutant	736905	
2.1.1.204	additional information	generation of Dnmt2 knockout (KO) cells	756387	
2.1.1.204	additional information	generation of Dnmt2 knockout mice	758319	
2.1.1.204	additional information	generation of Dnmt2 knockout murine embryonic fibroblast cells	756387	
2.1.1.204	additional information	generation of Dnmt2/- knockout mice	-, 736018	
2.1.1.204	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	756399	
2.1.1.204	N264S	site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme	735726	
2.1.1.204	R160A	no detectable in vitro methylation activity	710547	
2.1.1.204	R160A	site-directed mutagenesis, inactive mutant	718931	
2.1.1.204	R162A	no detectable in vitro methylation activity	710547	
2.1.1.204	R162A	site-directed mutagenesis, inactive mutant	718931	
2.1.1.204	R240A	site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R275A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R288A	site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R289A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R369A	site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R371A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R371H	site-directed mutagenesis, almost inactive mutant	735726	
2.1.1.204	R84A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931	
2.1.1.204	R95A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	718931