ID A0A059G7V9_9RHOB Unreviewed; 389 AA. AC A0A059G7V9; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 01-APR-2015, entry version 9. DE RecName: Full=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=HOC_08959 {ECO:0000313|EMBL:KDA02814.1}; OS Hyphomonas oceanitis SCH89. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=1280953 {ECO:0000313|EMBL:KDA02814.1}; RN [1] {ECO:0000313|EMBL:KDA02814.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCH89 {ECO:0000313|EMBL:KDA02814.1}; RX PubMed=25070064; DOI=10.1007/s10482-014-0236-y; RA Li C., Lai Q., Li G., Dong C., Wang J., Liao Y., Shao Z.; RT "Hyphomonas beringensis sp. nov. and Hyphomonas chukchiensis sp. nov., RT isolated from surface seawater of the Bering Sea and Chukchi Sea."; RL Antonie Van Leeuwenhoek 106:657-665(2014). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 CC modification seems to play a crucial role in the proofreading step CC occurring at the peptidyl transferase center and thus would serve CC to optimize ribosomal fidelity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00181435}. 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:SAAS00181420}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS00173519}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00173519}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine.; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS00090888}. 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}. 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:KDA02814.1}. 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; ARYL01000011; KDA02814.1; -; Genomic_DNA. DR EnsemblBacteria; KDA02814; KDA02814; HOC_08959. 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; TIGR00048; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00090918}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00090849}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004735}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00090861}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00090912}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00091014}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00090880}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004875}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00090866}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00091018}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004932}. FT REGION 187 188 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT REGION 241 243 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 110 110 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 361 361 S-methylcysteine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 132 132 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 136 136 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 139 139 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 219 219 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 318 318 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT DISULFID 125 361 (transient). {ECO:0000256|HAMAP-Rule: FT MF_01849}. SQ SEQUENCE 389 AA; 42516 MW; FD984BB05934370E CRC64; MTITLDLSRK PDQPQGQRSL AGMPLPALKA ELEAMGLDPK KASMRAKQIS RWSQYFGATS FEGMTDIGKE LRAELAARFT LDRPEIADHQ VSKDGTQKWL SRFQPGVEGE SVYIPSVGMD GGALCVSSQV GCTLNCTFCH TGTQALVRNL TAQEITAQVM IARDALNEWP SSIEARNLTN IVFMGMGEPL YNLDNVAAAI DTISDGDGIS IGRRRITVST AGVAPKIPEL GERTNAMLAI SLHATNDDLR NELVPINRKY DLQMLFEAIR AYPGSGNSRR VTFEYVMLKG INDTQAEARE LVRLLKGVPA KINLIPFNPW PGSPYECSDW ETIEAFAEIV NRAGYASPIR TPRGRDIDAA CGQLRSESVK KSAAEKRREA LEAAASPEA //