ID A0A293TT00_HELPX Unreviewed; 357 AA. AC A0A293TT00; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 13-NOV-2019, 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 ECO:0000313|EMBL:QEF45294.1}; GN ORFNames=BGL73_02360 {ECO:0000313|EMBL:OPG44421.1}, D2C71_06230 GN {ECO:0000313|EMBL:QEF45294.1}; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210 {ECO:0000313|EMBL:OPG44421.1, ECO:0000313|Proteomes:UP000220272}; RN [1] {ECO:0000313|EMBL:OPG44421.1, ECO:0000313|Proteomes:UP000220272} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGms167 {ECO:0000313|EMBL:OPG44421.1, RC ECO:0000313|Proteomes:UP000220272}; RX PubMed=28293542; DOI=.3389/fcimb.2017.00050; RA Munoz-Ramirez Z.Y., Mendez-Tenorio A., Kato I., Bravo M.M., RA Rizzato C., Thorell K., Torres R.C., Aviles-Jimenez F., Camorlinga M., RA Canzian F., Torres J.; RT "Whole Genome Sequence and Phylogenetic Analysis Show Helicobacter RT pylori Strains from Latin America Have Followed a Unique Evolution RT Pathway."; RL Front. Cell. Infect. Microbiol. 7:50-50(2017). RN [2] {ECO:0000313|EMBL:QEF45294.1, ECO:0000313|Proteomes:UP000321373} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G-Mx-2003-250 {ECO:0000313|EMBL:QEF45294.1, RC ECO:0000313|Proteomes:UP000321373}; RA Torres R.C., Torres J., Weimer B.C., Storey D.B., Becker M., RA Kong N.T., Huang C.B., Camorlinga M.; RT "Genome-Based Search for H. pylori Disease-Associated Genes in the RT Context of Different Populations."; RL Submitted (AUG-2018) 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: 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 EC=2.1.1.192; Evidence={ECO:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS01114928}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + CC 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'- CC deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162, CC Rhea:RHEA-COMP:10485, 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 EC=2.1.1.192; Evidence={ECO:0000256|HAMAP-Rule:MF_01849, CC ECO:0000256|SAAS:SAAS01114934}; 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:SAAS00297762}. 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 --------------------------------------------------------------------------- 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; MILK01000030; OPG44421.1; -; Genomic_DNA. DR EMBL; CP032048; QEF45294.1; -; Genomic_DNA. DR Proteomes; UP000220272; Unassembled WGS sequence. DR Proteomes; UP000321373; Chromosome. 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; 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 TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00297782}; KW Complete proteome {ECO:0000313|Proteomes:UP000220272, KW ECO:0000313|Proteomes:UP000321373}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00297764}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00721829}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00297790}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00297787}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00297793}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00297761, ECO:0000313|EMBL:OPG44421.1}; 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:SAAS00297766}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00297763, ECO:0000313|EMBL:OPG44421.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849, KW ECO:0000256|SAAS:SAAS00721837}. FT DOMAIN 119 278 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT REGION 173 174 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT REGION 226 228 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT ACT_SITE 89 89 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01849}. FT ACT_SITE 345 345 S-methylcysteine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 123 123 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 127 127 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT METAL 130 130 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 203 203 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01849}. FT BINDING 302 302 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01849}. SQ SEQUENCE 357 AA; 40759 MW; 037D84DB8ADDBD87 CRC64; MKASIYDFTL KELSQLLKPS FRAKQLYLWL YAKYKTSFKD MQNNFSKDFI AYLEQEFTLR TIEITHVRES VDGSKKYLFK SLRDNHTFEA VLLKMKDKKI DEETNAILEG EKYTVCVSCQ IGCQVGCAFC FTQKGGFVRN LKASEIIQQA LLIKEDNNLP IEKALNIVFM GMGEPLNNLD EVCKAVEIFN TGMQISPKRI TISTSGVADK IPILAGKNLG VQLAISLHAV DDKTRSSLMP LNKKYNIECV LNEVRKWPLE QRKRVMFEYL LIKDLNDSLD CAKKLLKLLN GIKSKVNLIL FNPHEGSKFE RPSLESARMF ADFLNSKGLL CTIRESKALD IEAACGQLRE KKLQQKI //