ID K9GLG6_9PROT Unreviewed; 421 AA. AC K9GLG6; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 01-OCT-2014, entry version 10. 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=C882_2073 {ECO:0000313|EMBL:EKV26850.1}; OS Caenispirillum salinarum AK4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Caenispirillum. OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV26850.1}; RN [1] {ECO:0000313|EMBL:EKV26850.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AK4 {ECO:0000313|EMBL:EKV26850.1}; RX PubMed=23409257; RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.; RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum RT salinarum AK4(T), Isolated from a Solar Saltern."; RL Genome Announc. 1:E00199-12(2013). 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 = S-adenosyl-L-homocysteine + L-methionine + 5'- CC deoxyadenosine + 2-methyladenine(2503) in 23S rRNA. CC {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00004752}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in CC tRNA = S-adenosyl-L-homocysteine + L-methionine + 5'- CC deoxyadenosine + 2-methyladenine(37) in tRNA. {ECO:0000256|HAMAP- CC Rule:MF_01849, ECO:0000256|SAAS:SAAS00004893}. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with CC 3 cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00004784}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS00004912}. 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:EKV26850.1}. 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; ANHY01000022; EKV26850.1; -; Genomic_DNA. DR EnsemblBacteria; EKV26850; EKV26850; C882_2073. 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:SAAS00004905}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004803}; 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:SAAS00004804}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004908}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004830}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004867, ECO:0000313|EMBL:EKV26850.1}; 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:SAAS00004753}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004805, ECO:0000313|EMBL:EKV26850.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004932}. FT REGION 220 221 S-adenosyl-L-methionine binding. {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT REGION 274 276 S-adenosyl-L-methionine binding. {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 142 142 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 394 394 S-methylcysteine intermediate. {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT METAL 164 164 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT METAL 168 168 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT METAL 171 171 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT BINDING 252 252 S-adenosyl-L-methionine. {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT BINDING 351 351 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. {ECO: FT 0000256|HAMAP-Rule:MF_01849}. FT DISULFID 157 394 (transient). {ECO:0000256|HAMAP-Rule: FT MF_01849}. SQ SEQUENCE 421 AA; 46767 MW; 8666DDBA638840CE CRC64; MTTDTTAADA VAREDAAVSD AQANAVSDDG IEKLPLQASD TAARAAVAAD HGKRDLVGLS REELGAAMAE LGEKPFRVKQ VWQWIYNKGV TDFDSMTNLS KPLREKLDAH FVIRRPSLPV EQTSEDGTRK WLMRFADGKE AETVYIPDVD EPRGSVCISS QVGCTLTCKF CHTGTQLLVR NLSAAEIVSQ FMVARDSYGE WPSPTDESRR LSNIVMMGMG EPLYNYDNVV KALKILVDGD GIALSRRRIT LSTSGVVPEM YRLGNDINVN LAVSLHAATD EIRNRIMPIN KKYPLAELMK ACREYPNVSN ARRITFEYVM LKDVNDSDAD ARALAKLVEG IPCKFNLIPF NPWPGSQFEC SSWNRIRKFS DLLYDLGFSA PIRMPRGRDI LAACGQLKSE SERERKSLMK ARLAAGIPDE H //