2.1.1.268: tRNAThr (cytosine32-N3)-methyltransferase
This is an abbreviated version!
For detailed information about tRNAThr (cytosine32-N3)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.268
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2.1.1.268
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actin
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3-methylcytidine
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latrunculin
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filament-binding
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s-adenosylmethionine
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fission
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decoding
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cables
- 2.1.1.268
- actin
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3-methylcytidine
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latrunculin
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filament-binding
- s-adenosylmethionine
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fission
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decoding
- cables
Reaction
Synonyms
ABP140, METTL2B, Trm140
ECTree
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General Information
General Information on EC 2.1.1.268 - tRNAThr (cytosine32-N3)-methyltransferase
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evolution
malfunction
physiological function
additional information
in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
evolution
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in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
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knockout strains in the yeast Saccharomyces cerevisiae lack N3-methylcytosine32 in tRNA1Thr. Lack of the m3C modification does impair translation, albeit mildly
malfunction
N3-methylcytosine32 modification is absent in strains that lack the entire ABP140 gene
malfunction
specific reduction of N3-methylcytosine formation in HeLa cells by siRNA-mediated knock down of METTL2B
N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
physiological function
the 3-methylcytidine (m3C) modification is ubiquitous in eukaryotic tRNA, widely found at C32 in the anticodon loop of tRNAThr, tRNASer, and some tRNAArg species, as well as in the variable loop (V-loop) of certain tRNASer species. In the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species. Trm140 binding is a significant driving force for tRNA modification and suggest separate contributions from each recognition element for the modification
physiological function
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the 3-methylcytidine (m3C) modification is ubiquitous in eukaryotic tRNA, widely found at C32 in the anticodon loop of tRNAThr, tRNASer, and some tRNAArg species, as well as in the variable loop (V-loop) of certain tRNASer species. In the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species. Trm140 binding is a significant driving force for tRNA modification and suggest separate contributions from each recognition element for the modification
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enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
additional information
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enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
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