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methyltransferase domain-containing protein
This family appears to have methyltransferase activity. (from Pfam)
This family appears to be a methyltransferase domain. (from Pfam)
RNA cap guanine-N2 methyltransferase
RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyse methylation of the exocyclic N2 amine of 7-methylguanosine [1]. [1]. 17284461. Biochemical and Genetic Analysis of RNA Cap Guanine-N2 Methyltransferases from Giardia lamblia and Schizosaccharomyces pombe. Hausmann S, Ramirez A, Schneider S, Schwer B, Shuman S;. Nucleic Acids Res. 2007; [Epub ahead of print] (from Pfam)
50S ribosomal protein L11 methyltransferase
This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences. [1]. 8226664. Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12. Vanet A, Plumbridge JA, Alix JH;. J Bacteriol 1993;175:7178-7188. (from Pfam)
methyltransferase
This domain is found in ribosomal RNA small subunit methyltransferase C (eg Swiss:P44453) as well as other methyltransferases (eg Swiss:Q53742). (from Pfam)
ribosomal protein L3 N(5)-glutamine methyltransferase
ribosomal protein L3 N(5)-glutamine methyltransferase specifically methylates the 50S ribosomal protein L3 on Gln-150 using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; does not methylate the translation termination release factors RF1 and RF2; belongs to the class I SAM-dependent methyltransferase superfamily
50S ribosomal protein L3 N(5)-glutamine methyltransferase
Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors.
HemK family protein methyltransferase
The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase (Medline 95189105). Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain.
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