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RsmI C-terminal HTH domain
This entry represents a small helical domain at the C-terminus of RsmI that folds into a typical three helical DNA/RNA binding bundle containing HTH motif. This domain is found in Ribosomal RNA small subunit methyltransferase I (RsmI) and related proteins. RsmI is an S-adenosyl-L-methionine-dependent methyltransferase that catalyses the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. It may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity. In vitro, active on the assembled 30S subunit, but not naked 16S rRNA or 70S ribosomes. Paper describing PDB structure 5hw4. [1]. 27711192. Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI. Zhao M, Zhang H, Liu G, Wang L, Wang J, Gao Z, Dong Y, Zhang L, Gong Y;. PLoS One. 2016;11:e0163816. (from Pfam)
SAM-dependent methyltransferase
This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function, including Swiss:P45528. This family includes the methylase Dipthine synthase. (from Pfam)
16S rRNA (cytidine(1402)-2'-O)-methyltransferase
16S rRNA (cytidine(1402)-2'-O)-methyltransferase uses assembled 30S subunit as a substrate and catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA
This protein, previously known as YraL, is RsmI, one of a pair of genes involved in a unique dimethyl modification of a cytidine in 16S rRNA. See Pfam model PF00590 (tetrapyrrole methylase), which demonstrates homology between this family and other members, including several methylases for the tetrapyrrole class of compound, as well as the enzyme diphthine synthase.
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