ID RLMN_FRATW Reviewed; 370 AA. AC A4IY03; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=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=FTW_0968; OS Francisella tularensis subsp. tularensis (strain WY96-3418). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=418136; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WY96-3418; RX PubMed=17895988; DOI=10.1371/journal.pone.0000947; RA Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V., RA Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D., RA Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J., RA Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.; RT "Complete genomic characterization of a pathogenic A.II strain of RT Francisella tularensis subspecies tularensis."; RL PLoS ONE 2:E947-E947(2007). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S CC rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems CC to play a crucial role in the proofreading step occurring at the CC peptidyl transferase center and thus would serve to optimize ribosomal CC fidelity. {ECO:0000255|HAMAP-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; CP000608; ABO46804.1; -; Genomic_DNA. DR RefSeq; WP_003028042.1; NC_009257.1. DR AlphaFoldDB; A4IY03; -. DR SMR; A4IY03; -. DR KEGG; ftw:FTW_0968; -. DR HOGENOM; CLU_029101_0_0_6; -. 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(2503)-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0002935; F:tRNA (adenine(37)-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 GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 1.10.150.530; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR040072; Methyltransferase_A. DR InterPro; IPR048641; RlmN_N. DR InterPro; IPR027492; RNA_MTrfase_RlmN. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR00048; rRNA_mod_RlmN; 1. DR PANTHER; PTHR30544; 23S RRNA METHYLTRANSFERASE; 1. DR PANTHER; PTHR30544:SF5; RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF21016; RlmN_N; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1. DR SFLD; SFLDG01082; B12-binding_domain_containing; 1. DR SFLD; SFLDG01062; methyltransferase_(Class_A); 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 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..370 FT /note="Dual-specificity RNA methyltransferase RlmN" FT /id="PRO_0000350187" FT DOMAIN 99..337 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT ACT_SITE 93 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT ACT_SITE 343 FT /note="S-methylcysteine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 113 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 117 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 120 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 167..168 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 199 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 221..223 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT BINDING 300 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" FT DISULFID 106..343 FT /note="(transient)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01849" SQ SEQUENCE 370 AA; 41478 MW; 4988A14166735EC7 CRC64; MQQDKVNLLG LNQKAIEDFF ISIGEKKFHA RQVFKWIHKK GVIDFDAMTD LGKNLRHKLK EKAQITIPKV VFSKASKDGT HKWLIDVGGS AVETVFILEE GRGTLCVSSQ VGCTLNCSFC STGKQGFNRN LSAAEVIAQL WIAARTLSKT DGEHDFTVTN IVMMGMGEPL MNFENVVPAM DIMMDDLAYG LSRRKVTLST SGVVPRIYDL LEQSGVSLAV SLHAPNDMLR NEIVPINKKY NIDELLEACK LYAQKGPHKH ITFEYTLMEE VNDNLSDAEE LVALLKSREV PAKINLIPFN PYPGTPYKKP SNNRIHRFKE FLQHNGFVTT VRKTRGDDID AACGQLAGDV MDKTNRKQRY LKKLGDTNAN //