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 11-DEC-2019, entry version 106. 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=TTE1502; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM OS 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., Chen Y., RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., RA 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 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; AE008691; AAM24720.1; -; Genomic_DNA. DR RefSeq; WP_011025761.1; NC_003869.1. DR SMR; Q8R9T4; -. DR STRING; 273068.TTE1502; -. DR EnsemblBacteria; AAM24720; AAM24720; TTE1502. DR KEGG; tte:TTE1502; -. DR eggNOG; ENOG4105C55; Bacteria. DR eggNOG; COG0820; LUCA. DR HOGENOM; HOG000217991; -. DR KO; K06941; -. DR OMA; CGQLANK; -. DR OrthoDB; 1111428at2; -. DR BioCyc; TTEN273068:G1FZJ-1598-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-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. PE 3: Inferred from homology; KW 4Fe-4S; Cytoplasm; Disulfide bond; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; rRNA processing; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1..342 FT /note="Probable dual-specificity RNA methyltransferase FT RlmN" FT /id="PRO_0000350496" FT REGION 157..158 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT REGION 212..214 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT ACT_SITE 91 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT ACT_SITE 331 FT /note="S-methylcysteine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT METAL 111 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT METAL 115 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT METAL 118 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 189 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 288 FT /note="S-adenosyl-L-methionine; via amide nitrogen and FT carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT DISULFID 104..331 FT /note="(transient)" FT /evidence="ECO:0000255|HAMAP-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 //