ID A0A073IMR2_9BACT Unreviewed; 553 AA. AC A0A073IMR2; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 04-MAR-2015, entry version 6. 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=EH55_08130 {ECO:0000313|EMBL:KEJ91633.1}; OS Synergistes jonesii. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Synergistes. OX NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ91633.1}; RN [1] {ECO:0000313|EMBL:KEJ91633.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=78-1 {ECO:0000313|EMBL:KEJ91633.1}; RA Coil D.A., Eisen J.A., Holland-Moritz H.E.; RT "Draft Genome Sequence of Synergistes jonesii."; RL Submitted (APR-2014) 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|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: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|SAAS:SAAS00165613}; 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|SAAS:SAAS00165613}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01849}; 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:KEJ91633.1}. 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; JMKI01000038; KEJ91633.1; -; Genomic_DNA. DR EnsemblBacteria; KEJ91633; KEJ91633; EH55_08130. 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 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}; 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}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00004932}. FT REGION 161 162 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT REGION 216 218 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 94 94 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 334 334 S-methylcysteine intermediate. 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 METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 121 121 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 193 193 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 292 292 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT DISULFID 107 334 (transient). {ECO:0000256|HAMAP-Rule: FT MF_01849}. SQ SEQUENCE 553 AA; 61058 MW; 5D01DDCF3FB9F424 CRC64; MAEKKYALDF DFGEWEKYIT ESLGEPKFRA GQICGWLWQK RVCDPAEMTN LSKELRAELA EKLDFACPAL VREQRSRDGT KKFLWRLRDG ETVESVLIKE GDRLTLCVST QVGCPLHCSF CATGLSGFAR NLSAGEIAGQ LLAAEKQIGR EINNVVYMGM GEPLLNVDSV LKSVRMLNDP KMRNLGRRHI TISTSGVIPG IEELAASGLG VRLAVSLHAA DDELRSLLMP VNQTYPASEL RDAMQKYQAA TGDRITIEYA LFGGVNDGVE RARELVRYLK GIHVFVNLIP ANDVAGRCEK PKAEDVLRFR SVLESAGFEC EIRSERGADI DAACGQLRRK AHGGEAAPEG GARTLAKAAV PPRVDKSDEW KEKSAARVKG AKKDFPALRA NEKKKAFSPS GGFVAYPGKR VRAQRPAGEK SYGAPNFGEK RGGRGNARDF ETPLGARSRD EHAELRRGGK TDEARQDHRT RREEENHFER GVAAKHGYAE ARAEKFDTRR PRKSGSCAPE KDSSRQRPRG KAKNGAGRGA ADADSAFWKF YLRPKKSARG KKP //