ID RLMN_CALS4 Reviewed; 342 AA. AC Q8R9T4; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 29-APR-2015, entry version 86. 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}; GN OrderedLocusNames=TTE1502; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / OS JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=273068; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4; RX PubMed=11997336; DOI=10.1101/gr.219302; RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., RA Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., RA Tan H., Chen R., Wang J., Yu J., Yang H.; RT "A complete sequence of the T. tengcongensis genome."; RL Genome Res. 12:689-700(2002). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA and position 2 of adenine 37 in tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in CC 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L- CC homocysteine + L-methionine + 5'-deoxyadenosine + 2- CC methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in CC tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + CC L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 CC oxidized [2Fe-2S] ferredoxin. {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 CC involving intermediate methylation of a conserved cysteine CC residue. {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; AE008691; AAM24720.1; -; Genomic_DNA. DR RefSeq; NP_623116.1; NC_003869.1. DR ProteinModelPortal; Q8R9T4; -. DR STRING; 273068.TTE1502; -. DR EnsemblBacteria; AAM24720; AAM24720; TTE1502. DR KEGG; tte:TTE1502; -. DR PATRIC; 23897712; VBITheTen82880_1509. DR eggNOG; COG0820; -. DR HOGENOM; HOG000217991; -. DR KO; K06941; -. DR OMA; VNNRWSV; -. DR OrthoDB; EOG6DJZ2N; -. DR BioCyc; CSUB273068:GJEB-2719-MONOMER; -. DR Proteomes; UP000000555; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. 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 SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron; KW Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 342 Probable dual-specificity RNA FT methyltransferase RlmN. FT /FTId=PRO_0000350496. FT REGION 157 158 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT REGION 212 214 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT ACT_SITE 91 91 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01849}. FT ACT_SITE 331 331 S-methylcysteine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 111 111 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 189 189 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 288 288 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT DISULFID 104 331 (transient). {ECO:0000255|HAMAP- FT Rule:MF_01849}. SQ SEQUENCE 342 AA; 39453 MW; AFBC048AEDB24289 CRC64; MYNLKDMTLE EMEEFFVNLG ESKFRAKQLY KWIYDKRVTD FDLMTDISKN LRAKLKEIAY ISELKIIERR VSQIDDTVKY LFLLEDKNII EGVAIKYKFG NTACVSTQVG CNMKCKFCAS AIGGKVRDLK ASEMVDQVMA IDSDYGKISN IVLMGSGEPF DNYDEVMKFI KIVNNPYGLK IGKRHITIST VGIVPKIYQF ADEELQVNLS ISLHAPNNEL RNELMPINRA YPLEELMKAC RYYIEKTNRR ITFEYALIDG VNDKKEHAYQ LVDLLKGMLC HVNLIPINYV KEIGFRKSNN EKVMMFKKII ENAGITCTVR RELGSDIEAA CGQLRRKYLK EG //