ID RSMG_ACTPJ Reviewed; 205 AA. AC B0BRY0; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074}; DE EC=2.1.1.170 {ECO:0000255|HAMAP-Rule:MF_00074}; DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; GN OrderedLocusNames=APJL_1687; OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=434271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JL03; RX PubMed=18197260; DOI=10.1371/journal.pone.0001450; RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W., RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T., RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S., RA Zhao G.-P., Chen H.; RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of RT serotype 3 prevalent in China."; RL PLoS ONE 3:E1450-E1450(2008). CC -!- FUNCTION: Specifically methylates the N7 position of guanine in CC position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)- CC methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74480; EC=2.1.1.170; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00074}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}. 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; CP000687; ABY70239.1; -; Genomic_DNA. DR RefSeq; WP_005605652.1; NC_010278.1. DR AlphaFoldDB; B0BRY0; -. DR SMR; B0BRY0; -. DR KEGG; apj:APJL_1687; -. DR HOGENOM; CLU_065341_2_2_6; -. DR Proteomes; UP000008547; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1. DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00138; rsmG_gidB; 1. DR PANTHER; PTHR31760; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1. DR PANTHER; PTHR31760:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1. DR Pfam; PF02527; GidB; 1. DR PIRSF; PIRSF003078; GidB; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 3: Inferred from homology; KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1..205 FT /note="Ribosomal RNA small subunit methyltransferase G" FT /id="PRO_0000342902" FT BINDING 73 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074" FT BINDING 78 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074" FT BINDING 124..125 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074" FT BINDING 138 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074" SQ SEQUENCE 205 AA; 23267 MW; 1DBBF4608DA3F3A0 CRC64; MRQKLDRLLE QAQINLTDQQ KEQLVGFVRL LDKWNKAYNL TSVRNPDEML VKHILDSLVV SEHLQGNNFI DVGTGPGLPG IPLAIANPDK QFVLLDSLGK RITFIKNALR ELGITNVTPV LSRVEEYKEQ TFDGVLSRAF ASLNDMVDWC YHLPNPQGKF YALKGIYAES EVQEIKNPIW LEKVIPLSVP ELVGERHLVL LNKPN //