2.1.1.202: multisite-specific tRNA:(cytosine-C5)-methyltransferase
This is an abbreviated version!
For detailed information about multisite-specific tRNA:(cytosine-C5)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.202
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2.1.1.202
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methyltransferases
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mtases
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methylome
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williams-beuren
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anticodon
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transcriptome-wide
- 2.1.1.202
- methyltransferases
- mtases
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methylome
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williams-beuren
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anticodon
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transcriptome-wide
Reaction
Synonyms
5-methylcytosine RNA methyltransferase, broad-spectrum methyltransferase, cytosine-5 RNA methyltransferase, EC 2.1.1.29, HNSun6, M5C RNA methyltransferase, MJ0026, multisite-specific tRNA:m5C-methyltransferase, Ncl1p, NOP2/Sun RNA methyltransferase 2, NSUN2, NSUN6, PhNSUN6, RNA (cytosine-5)-methyltransferase, RNA:m5C methyltransferase, RNA:m5C MTase, TRDMT1, TRM4, TRM4A, TRM4B, Trm4p, tRNA (cytosine72-C5)-methyltransferase, tRNA-specific methyltransferase 4B, tRNA:m5C-methyltransferase, tRNA:m5C72 MTase
ECTree
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Cofactor
Cofactor on EC 2.1.1.202 - multisite-specific tRNA:(cytosine-C5)-methyltransferase
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additional information
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the S-adenosyl-L-methionine analigue sinefungin is bound in a negatively charged pocket near helix alpha8, binding structure, detailed overview
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S-adenosyl-L-methionine
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helix alpha8 can adopt two different conformations, thereby controlling the entry of S-adenosyl-L-methionine into the active site
S-adenosyl-L-methionine
cofactor interacting residues in hNSun6 are mainly composed of conserved residues Leu241, Cys242, Pro325 and Leu354. In addition, the side chain of residue Asp293 recognizes the N6 of the adenine ring. Asp293 is conserved as Asp or Glu in the RNA:m5C MTase family