ID A0A139PXE9_STROR Unreviewed; 361 AA. AC A0A139PXE9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000256|HAMAP-Rule:MF_01849}; DE EC=2.1.1.192 {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA m2A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; GN Name=rlmN {ECO:0000256|HAMAP-Rule:MF_01849}; GN ORFNames=BBP19_02045 {ECO:0000313|EMBL:OJG02681.1}, SORDD27_00908 GN {ECO:0000313|EMBL:KXT94936.1}, SORDD30_00386 GN {ECO:0000313|EMBL:KXU00023.1}; OS Streptococcus oralis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1303 {ECO:0000313|EMBL:KXT94936.1, ECO:0000313|Proteomes:UP000072363}; RN [1] {ECO:0000313|EMBL:KXT94936.1, ECO:0000313|Proteomes:UP000070220, ECO:0000313|Proteomes:UP000072363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD27 {ECO:0000313|EMBL:KXT94936.1, RC ECO:0000313|Proteomes:UP000072363}, and DD30 RC {ECO:0000313|EMBL:KXU00023.1, ECO:0000313|Proteomes:UP000070220}; RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I., RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.; RT "Highly variable Streptococcus oralis are common among viridans RT streptococci isolated from primates."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OJG02681.1, ECO:0000313|Proteomes:UP000183671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC15-3744 {ECO:0000313|EMBL:OJG02681.1, RC ECO:0000313|Proteomes:UP000183671}; RA Kanji J.N., Bharat A., Naidu P., Martin I., Mulvey M.R., Panaro C.D.; RT "A clinical isolate of carbapenem-resistant Streptococcus oralis with RT altered penicillin binding proteins."; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA and position 2 of adenine 37 in tRNAs. CC {ECO:0000256|SAAS:SAAS00721833}. 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:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00536154}. 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:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS00721810}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS00385725}. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism CC involving intermediate methylation of a conserved cysteine CC residue. {ECO:0000256|HAMAP-Rule:MF_01849}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00571858}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01849}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXT94936.1}. 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; LQNZ01000088; KXT94936.1; -; Genomic_DNA. DR EMBL; LQRP01000014; KXU00023.1; -; Genomic_DNA. DR EMBL; MBDM01000006; OJG02681.1; -; Genomic_DNA. DR RefSeq; WP_000804759.1; NZ_MBDM01000006.1. DR ProteinModelPortal; A0A139PXE9; -. DR Proteomes; UP000070220; Unassembled WGS sequence. DR Proteomes; UP000072363; Unassembled WGS sequence. DR Proteomes; UP000183671; Unassembled WGS sequence. 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; 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 TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00463035}; KW Complete proteome {ECO:0000313|Proteomes:UP000070220, KW ECO:0000313|Proteomes:UP000072363, ECO:0000313|Proteomes:UP000183671}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00462865}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00721829}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00462960}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00462907}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00462842}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00462825, ECO:0000313|EMBL:KXT94936.1}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00536180}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00462941}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00463018, ECO:0000313|EMBL:KXT94936.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00721837}. FT DOMAIN 105 276 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT REGION 163 164 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT REGION 218 220 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 91 91 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 340 340 S-methylcysteine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 111 111 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 195 195 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 296 296 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01849}. SQ SEQUENCE 361 AA; 41335 MW; 2FCF507FCD8770CB CRC64; MKPSIYSLTR QTMQEWVLEQ GEKKFRADQI WEWLYRKRVQ SFEEMTNLSK DLIAKLNDQF VVNPLKQRIV QESADGTVKY LFELPDGMLI ETVLMRQHYG LSVCVTTQVG CNIGCTFCAS GLIKKQRDLN NGEIVAQIML VQKYFDERGQ DERVSHIVVM GIGEPFDNYN NVLNFVRTIN DDKGMAIGAR HITVSTSGLA HKIRDFANEG VQVNLAVSLH APNNELRSSI MKINRAFPIE KLFAAIEYYI EKTNRRVTFE YIMLNEVNDG VEQALELAEL LKNIKKLSYV NLIPYNPVSE HDQYSRSPKE RVMAFYDTLK KKGVNCVVRQ EHGTDIDAAC GQLRSNTMKR DRQKAVAAVN P //