ID   RLMG_ALIFM              Reviewed;         382 AA.
AC   B5FBH8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_01859};
DE            EC=2.1.1.174 {ECO:0000255|HAMAP-Rule:MF_01859};
DE   AltName: Full=23S rRNA m2G1835 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01859};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmG {ECO:0000255|HAMAP-Rule:MF_01859};
GN   Name=rlmG {ECO:0000255|HAMAP-Rule:MF_01859}; OrderedLocusNames=VFMJ11_0743;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the guanine in position 1835
CC       (m2G1835) of 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01859}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42744, Rhea:RHEA-COMP:10217, Rhea:RHEA-COMP:10218,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.174;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01859};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01859}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.
CC       {ECO:0000255|HAMAP-Rule:MF_01859}.
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DR   EMBL; CP001139; ACH66233.1; -; Genomic_DNA.
DR   RefSeq; WP_012533587.1; NC_011184.1.
DR   AlphaFoldDB; B5FBH8; -.
DR   SMR; B5FBH8; -.
DR   EnsemblBacteria; ACH66233; ACH66233; VFMJ11_0743.
DR   KEGG; vfm:VFMJ11_0743; -.
DR   HOGENOM; CLU_040288_4_0_6; -.
DR   OMA; DFLAWRM; -.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052916; F:23S rRNA (guanine(1835)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR   InterPro; IPR017237; rRNA_m2G-MeTrfase_RsmD.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47816:SF5; PTHR47816:SF5; 1.
DR   Pfam; PF05175; MTS; 1.
DR   PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..382
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000366533"
SQ   SEQUENCE   382 AA;  43463 MW;  3D29638AA882E1CE CRC64;
     MKTELSLLDR SLNLQRYPKR AQELLQAWDA GDEYIIKYVE EELNLEDGKN ILILNDNFGA
     LSCWFSDKHN VTMMTDSFVS QRGTLKNLQR NQCNRVQLIT STEEMPQGFD LVLMQIPKNN
     RMLTWQLQQL RQSMDSSCPI IAVNKAKEIH SSTLELFEDY LGETKTSLAW KKHRLVFSNA
     NASNPKTIAE AVCWSVDNED IDLLNYPNVY SGEKLDQGAR FMLEHIPSDP ELRHIIDLGC
     GNGVLSVKAG QLNPEARITC VDESFMAVES ARRNLEVNLG KERQFQFIAN NCLDGFKKHS
     SYLVLCNPPF HQGQAITDHI AWQMFCDAKH ILCKDGKLLV IGNRHLDYDG KLCRLFGEEN
     VTTVASNSKF VILEAVKAEK SK