ID D1J7E5_METH1 Unreviewed; 257 AA. AC D1J7E5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607}; DE EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethylase {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607}; GN Name=rsmA {ECO:0000256|HAMAP-Rule:MF_00607}; GN Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607, GN ECO:0000313|EMBL:CAX37142.1}; GN OrderedLocusNames=MHO_0080 {ECO:0000313|EMBL:CAX37142.1}; OS Metamycoplasma hominis (strain ATCC 23114 / DSM 25592 / NBRC 14850 / OS NCTC 10111 / PG21) (Mycoplasma hominis). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae; OC Metamycoplasma. OX NCBI_TaxID=347256 {ECO:0000313|EMBL:CAX37142.1, ECO:0000313|Proteomes:UP000002631}; RN [1] {ECO:0000313|EMBL:CAX37142.1, ECO:0000313|Proteomes:UP000002631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23114 / NBRC 14850 / NCTC 10111 / PG21 RC {ECO:0000313|Proteomes:UP000002631}; RX PubMed=19816563; DOI=10.1371/journal.pgen.1000677; RA Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A., RA Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A., RA Bebear C.; RT "Life on arginine for Mycoplasma hominis: clues from its minimal genome and RT comparison with other human urogenital mycoplasmas."; RL PLoS Genet. 5:E1000677-E1000677(2009). CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and CC A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA CC in the 30S particle. May play a critical role in biogenesis of 30S CC subunits. {ECO:0000256|HAMAP-Rule:MF_00607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L- CC methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)- CC dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00607}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. rRNA adenine N(6)-methyltransferase family. RsmA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00607}. 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; FP236530; CAX37142.1; -; Genomic_DNA. DR AlphaFoldDB; D1J7E5; -. DR STRING; 347256.MHO_0080; -. DR PaxDb; 347256-MHO_0080; -. DR KEGG; mho:MHO_0080; -. DR eggNOG; COG0030; Bacteria. DR HOGENOM; CLU_041220_0_0_14; -. DR Proteomes; UP000002631; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR023165; rRNA_Ade_diMease-like_C. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00755; ksgA; 1. DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1. DR PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00607}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_00607}; Reference proteome {ECO:0000313|Proteomes:UP000002631}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00607}. FT DOMAIN 18..184 FT /note="Ribosomal RNA adenine methylase transferase N- FT terminal" FT /evidence="ECO:0000259|SMART:SM00650" FT BINDING 11 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 13 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 37 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 58 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 82 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 99 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" SQ SEQUENCE 257 AA; 29513 MW; BD6EDED4667893CA CRC64; MIKALKSLGQ NFLSNKNIQK EIVKAANVVG KNIIEIGPGM GAITDQMADV VNRLVCIEFD KRLYEFLLQK NYSSNVEILN QDFLQTDLLK YTDFEVIGNI PYNITSDIIF KLLDNAKNIN KITLMVQKEV ADRICCGAGN SQYSKLAASI QLLYEPKYLF TVKAKEFNPA PKVDSAVIQL NLIKNNDFIW NNQVEILKFI KQMFQYKRKT LLNNFPSNLK QKISDFLKSN ELDLNIRAEK ITKEISINLF KFINNKN //