ID A0A3C0CLJ0_9GAMM Unreviewed; 338 AA. AC A0A3C0CLJ0; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 08-MAY-2019, entry version 4. DE RecName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|SAAS:SAAS00536183}; DE EC=2.1.1.- {ECO:0000256|SAAS:SAAS00297775}; DE Flags: Fragment; GN Name=rlmN {ECO:0000313|EMBL:HAH79694.1}; GN ORFNames=DCL88_00605 {ECO:0000313|EMBL:HAH79694.1}; OS Gammaproteobacteria bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1913989 {ECO:0000313|EMBL:HAH79694.1}; RN [1] {ECO:0000313|EMBL:HAH79694.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA11652 {ECO:0000313|EMBL:HAH79694.1}; RX PubMed=30148503; DOI=10.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA. {ECO:0000256|SAAS:SAAS00536187}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]- CC [ferredoxin] + 2 S-adenosyl-L-methionine = 2- CC methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L- CC methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA-COMP:10000, CC Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA- CC COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; CC Evidence={ECO:0000256|SAAS:SAAS01114932}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|SAAS:SAAS00611820}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00297762}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000256|SAAS:SAAS00571858}. 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:HAH79694.1}. 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; DMGT01000025; HAH79694.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro. DR GO; GO:0070475; P:rRNA base methylation; IEA:InterPro. DR GO; GO:0030488; P:tRNA methylation; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR040072; Methyltransferase_A. 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 TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00297782}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00297764}; KW Iron {ECO:0000256|SAAS:SAAS00297790}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00297787}; KW Metal-binding {ECO:0000256|SAAS:SAAS00297793}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00297761, KW ECO:0000313|EMBL:HAH79694.1}; KW rRNA processing {ECO:0000256|SAAS:SAAS00536180}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00297766}; KW Transferase {ECO:0000256|SAAS:SAAS00297763, KW ECO:0000313|EMBL:HAH79694.1}. FT DOMAIN 108 272 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT NON_TER 338 338 {ECO:0000313|EMBL:HAH79694.1}. SQ SEQUENCE 338 AA; 37646 MW; 0574DB8E6300214E CRC64; MQNLQNLYGF DRTQLENLFV EQGLQAFRGR QLMKWVYHQE QTDFAAMTDL PLRMREWLAD NCHFAVPEVE RQLVSADGTI KWLLRVANGD LIEMVLIPEK GRNTLCVSSQ IGCVLDCSFC STGKQGFNGN LAPADIVGQM ILANQALRAR GESVTNVVLM GMGEPLLNFD AVVAATNVMK DDHAFGLSKR RVTVSTAGVV PGIDKLREVS DVALAISLHA PTDALRNELV PINRKYSIEQ LLRACRDYVE DLGPARKLVI EYTLMRGVND QPEHAGQLAE LLQSLRCKIN LIPFNPFPGS GYERPLDADI EHFQTILIQQ GFTTMLRTTR GEDIDAAC //