|Function||23S rRNA m2A2503 methyltransferase|
|Domain Trusted Cutoff||236.95|
|Domain Noise Cutoff||176.50|
|Mainrole Category||Unknown function|
|Subrole Category||Enzymes of unknown specificity|
|Author||Richardson DL, Haft DH|
|Entry Date||Apr 20 1999 2:04PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||A Staphylococcus sciuri plasmid-borne member of this family, Cfr, has been identified as essential to transferrable resistance to chloramphenicol and florfenicol by an unknown mechanism. A 14-15 residue cluster with four perfectly conserved Cys residues suggests this protein may be an enzyme with an iron-sulfur cluster. The Cys cluster is part of the radical SAM domain, suggested to provide a general mechanism by which the Fe-S center cleaves S-adenosylmethionine to initiate radical-based catalysis. Members of this family lack apparent transmembrane domains.|
|References||DR PFAM; PF04055; Radical SAM superfamily
RT The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA.
RA Toh SM, Xiong L, Bae T, Mankin AS
RL RNA. 2008 Jan;14(1):98-106. Epub 2007 Nov 19.
RT Identification of a plasmid-borne chloramphenicol-florfenicol resistance gene in Staphylococcus sciuri.
RA Schwarz S, Werckenthin C, Kehrenberg C.
RL Antimicrob Agents Chemother 2000 Sep;44(9):2530-3
RT Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.
RA Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE.
RL Nucleic Acids Res 2001 Mar 1;29(5):1097-106
DR HAMAP; MF_01849; 521 of 570|
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