ID A0A1V6CTA9_9BACT Unreviewed; 357 AA. AC A0A1V6CTA9; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 25-OCT-2017, entry version 5. 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 ECO:0000313|EMBL:OQB80139.1}; GN ORFNames=BWX88_04647 {ECO:0000313|EMBL:OQB80139.1}; OS Planctomycetes bacterium ADurb.Bin126. OC Bacteria; Planctomycetes. OX NCBI_TaxID=1852903 {ECO:0000313|EMBL:OQB80139.1}; RN [1] {ECO:0000313|EMBL:OQB80139.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ADurb.Bin126 {ECO:0000313|EMBL:OQB80139.1}; RA Nobu M.K., Mei R., Narihiro T., Kuroda K., Liu W.-T.; RT "Delving into the versatile metabolic prowess of the omnipresent RT phylum Bacteroidetes."; RL Submitted (FEB-2017) 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:SAAS00536188}. 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:SAAS00536172}. 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:OQB80139.1}. 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; MWDR01000075; OQB80139.1; -; Genomic_DNA. 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; 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 SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 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 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:SAAS00919707}; 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:OQB80139.1}; 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:OQB80139.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00536152}. FT DOMAIN 97 313 Elp3. {ECO:0000259|SMART:SM00729}. FT REGION 154 155 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT REGION 209 211 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 87 87 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 335 335 S-methylcysteine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 107 107 Iron-sulfur (4Fe-4S-S-AdoMet). 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 114 114 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 186 186 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 285 285 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01849}. SQ SEQUENCE 357 AA; 38547 MW; 380C9B849E93DCBB CRC64; MTISVLDLSV DELKQALTDA GQPAYRAAQI ADWVYRKGAS DPARMTNLPP ALAGELVVMT SRVAQRADSS DGTIKLLLEL RDGERIETVL IPTPDRATAC LSTQAGCSMA CSFCASGLGG LRRGLTAGEM IEQILHLQQA AQRKVTHVVF MGTGEPLANY EPTVAAVRAI VDPARLNISA RRVTVSTVGL PRQIRRLAGE DLPITLAISL HAPNDALRRQ IMPKAATASI DQILAAAEEF FHSRNREITI EYVVLAGVND TNVCAEALAR IAHRLRCNVN LIQYNPLPEG VGERLPARYR RPSAESMRGF AQRLRARGAN VQVRRSRGLD AAAACGQLRA QAGEDGRKGA EEQGETE //