ID K9BVR5_9GAMM Unreviewed; 410 AA. AC K9BVR5; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 27-MAY-2015, entry version 18. 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 ECO:0000313|EMBL:EKU57720.1}; GN ORFNames=ACINWC487_0529 {ECO:0000313|EMBL:EKU57720.1}; OS Acinetobacter sp. WC-487. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=903917 {ECO:0000313|EMBL:EKU57720.1}; RN [1] {ECO:0000313|EMBL:EKU57720.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WC-487 {ECO:0000313|EMBL:EKU57720.1}; RA Harkins D.M., Durkin A.S., Beck E., Fedorova N.B., Kim M., Onuska J., RA Radune D., DePew J., Koroleva G.I., Singh I., Chahine M.A., Cash D.M., RA Huang X.-Z., Nikolich M.P., Nierman W.C., Fouts D.E.; RL Submitted (SEP-2012) 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. 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:SAAS00201823}; 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:SAAS00201823}; 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:EKU57720.1}. 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; AMZR01000073; EKU57720.1; -; Genomic_DNA. DR RefSeq; WP_002053401.1; NZ_AMZR01000073.1. DR ProteinModelPortal; K9BVR5; -. DR EnsemblBacteria; EKU57720; EKU57720; ACINWC487_0529. 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; rRNA_mod_RlmN; 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 200 201 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT REGION 254 256 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 120 120 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 378 378 S-methylcysteine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 144 144 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 148 148 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 151 151 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 232 232 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 335 335 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT DISULFID 137 378 (transient). {ECO:0000256|HAMAP-Rule: FT MF_01849}. SQ SEQUENCE 410 AA; 45756 MW; 2E98CD9213296A88 CRC64; MSSAVVVSSE NLDGQQQSSS TPASPAAEKV NLLGMSRAQL EKFFEDIGEK KFRAGQVMKW IHQYFVTDFA EMTNISGKLR AKLEQICEIK APEVVHRHYS KDGTRKWVFR VGEGSGSLVE TVLIPAEDKT GSRKTLCISS QVGCALDCSF CSTGKQGFQR DLTPDEIIGQ LWMANYSYME EVPVAERERS VTNVVMMGMG EPLLNYDAVL SSMHIMLDDF AYGMSKRRVT LSTSGVVPKI DQLAQDIDVA LAISLHAPND ELRNELVPIN KKYPLAQLIA ACQRYIAKDG NESARKHVTI EYVMLEGVND QPEHAQQLLK LLKNLPSKIN LIPFNPFPHA PYGRSSRNRI ISFQKTLSDA GFVCTIRQTR GDDIDAACGQ LVGQVADRTR RAEQWQKKVA QRQEILRTQG //