ID RLMN_BACAA Reviewed; 362 AA. AC C3P635; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 12-AUG-2020, entry version 66. DE RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000255|HAMAP-Rule:MF_01849}; DE EC=2.1.1.192 {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA m2A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; GN Name=rlmN {ECO:0000255|HAMAP-Rule:MF_01849}; OrderedLocusNames=BAA_4026; OS Bacillus anthracis (strain A0248). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=592021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A0248; RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D., RA Brettin T.; RT "Genome sequence of Bacillus anthracis A0248."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S CC rRNA and position 2 of adenine 37 in tRNAs. {ECO:0000255|HAMAP- CC Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] CC + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + CC 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA- CC COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S- CC adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'- CC deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S- CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA-COMP:10000, CC Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10485, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01849}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving CC intermediate methylation of a conserved cysteine residue. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001598; ACQ49308.1; -; Genomic_DNA. DR RefSeq; WP_000450543.1; NC_012659.1. DR SMR; C3P635; -. DR EnsemblBacteria; ACQ49308; ACQ49308; BAA_4026. DR GeneID; 50401390; -. DR KEGG; bai:BAA_4026; -. DR HOGENOM; CLU_029101_0_1_9; -. DR KO; K06941; -. DR OMA; QVGCSLD; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR040072; Methyltransferase_A. DR InterPro; IPR027492; RNA_MTrfase_RlmN. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR30544; PTHR30544; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cytoplasm; Disulfide bond; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; rRNA processing; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1..362 FT /note="Probable dual-specificity RNA methyltransferase FT RlmN" FT /id="PRO_1000188545" FT DOMAIN 111..344 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT REGION 175..176 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT REGION 230..232 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT ACT_SITE 105 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT ACT_SITE 349 FT /note="S-methylcysteine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT METAL 125 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT METAL 129 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT METAL 132 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 207 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 306 FT /note="S-adenosyl-L-methionine; via amide nitrogen and FT carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT DISULFID 118..349 FT /note="(transient)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" SQ SEQUENCE 362 AA; 41553 MW; 5D1D0D3E937245BD CRC64; METTVRKQKK NLETKKPSIY SLQLHEMQDW LKEQGEPKFR AGQIFDWLYK KRVKNYEDMS NLSKGLREKL SNSFDITTLN TLVKQTSSDG TIKFLFQLYD GYSIETVLMR HEYGNSICVT TQVGCRIGCT FCASTLGGLK RNLEAGEIVA QVVEVQRALD ESEERVSSLV VMGIGEPFDN YDNLMGFLRI INHEKGLHIG ARHMTVSTSG IIPKIYKFAE EDLQINFAIS LHAPNSELRS KLMPINRAYK LPDLMEAIKY YVNRTGRRIT FEYGLFGGEN DQVEHAEELA ALLKGVKCHV NLIPVNYVPE RDYVRTPREQ IFLFEKTLKD RGVNVTIRRE QGHDIDAACG QLRAKERKEE TR //