2.1.1.171: 16S rRNA (guanine966-N2)-methyltransferase
This is an abbreviated version!
For detailed information about 16S rRNA (guanine966-N2)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.171
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2.1.1.171
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tuberculosis
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mycobacterial
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non-canonical
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chromatin
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histone
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non-cpg
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cytosines
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epigenome
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minimalist
- 2.1.1.171
- tuberculosis
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mycobacterial
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non-canonical
- chromatin
- histone
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non-cpg
- cytosines
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epigenome
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minimalist
Reaction
Synonyms
16S rRNA-specific methyltransferases m2GMT, EC 2.1.1.51, EC 2.1.1.52, m2G966 methyltransferase, RNA:(guanine-N2) methyltransferase RsmD, RsmD, RsmD-like methyltransferase, Rv2966c, Rv2966c protein, small rRNA methyltransferase, yhhF
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Subunits
Subunits on EC 2.1.1.171 - 16S rRNA (guanine966-N2)-methyltransferase
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dimer
based on a comprehensive bioinformatic analysis of m2G methyltransferases it is inferred that the prokaryotic RsmC and RsmD methyltransferases are pseudodimers. The C-terminal catalytic domain is closely related to the structurally characterized Mj0882 protein, while the N-terminal domain lacks the cofactor-binding and catalytic side-chains
additional information
protein Rv2966c shows a two-domain structure with a short hairpin domain at the N-terminus and a C-terminal domain with the S-adenosylmethionine-methyltransferase-fold. The N-terminal hairpin is a minimalist functional domain that helps Rv2966c in target recognition. In contrast to the variable substrate binding domain, the C-terminal domain is a highly conserved structure consisting of the classical S-adenosyl-L-methionine-methyltransferase-fold found in several S-adenosyl-L-methionine-dependent methyltransferases. It consists of a central eight-stranded beta-sheet flanked by alpha-helices on both sides, the first five strands of the beta-sheet are parallel to each other and encompass the S-adenosyl-L-methionine binding site toward their C terminus end, whereas the remaining strands of the beta-sheet are antiparallel. The N-terminus of Rv2966c is the target recognition region that helps in binding to nucleic acids
additional information
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protein Rv2966c shows a two-domain structure with a short hairpin domain at the N-terminus and a C-terminal domain with the S-adenosylmethionine-methyltransferase-fold. The N-terminal hairpin is a minimalist functional domain that helps Rv2966c in target recognition. In contrast to the variable substrate binding domain, the C-terminal domain is a highly conserved structure consisting of the classical S-adenosyl-L-methionine-methyltransferase-fold found in several S-adenosyl-L-methionine-dependent methyltransferases. It consists of a central eight-stranded beta-sheet flanked by alpha-helices on both sides, the first five strands of the beta-sheet are parallel to each other and encompass the S-adenosyl-L-methionine binding site toward their C terminus end, whereas the remaining strands of the beta-sheet are antiparallel. The N-terminus of Rv2966c is the target recognition region that helps in binding to nucleic acids