ID   RLMG_SHEPC              Reviewed;         378 AA.
AC   A4Y3Y0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 76.
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};
GN   OrderedLocusNames=Sputcn32_0934;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP74663.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000681; ABP74663.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041420638.1; NC_009438.1.
DR   AlphaFoldDB; A4Y3Y0; -.
DR   SMR; A4Y3Y0; -.
DR   STRING; 319224.Sputcn32_0934; -.
DR   GeneID; 45041366; -.
DR   KEGG; spc:Sputcn32_0934; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_040288_4_0_6; -.
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   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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..378
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000366514"
SQ   SEQUENCE   378 AA;  41857 MW;  016A84D5FE06484F CRC64;
     MTTQFSVAGV ELELLRYPAQ QESNLQAWDA ADEHLLKSLI ESEQAAVPTA IVNDSFGALS
     CGLSKLHPSW PLFVETDART SFLGTEQNHG RNQLPMDNLQ RFTSRDTLPE NLALVLMKLP
     KNLSYFAHQL TRLSQVLPAG TRVLVAAKAK SINSALLDIF AKHLGPASAS LAWKNTRVIT
     CVSDGKPRPL AKEVTWAVPE YQLEISNLSN VFAANKLDIG ARIMLENLPK GNFKSIVDLG
     CGNGVLGLRT AQLSPEADIH FIDDSEMAVA SAKANWARNQ LPADKGHFYW DDCMTHLPEE
     VQPDLVLCNP PFHQGEAITD HIAWQMFLDA RRRLKEGGIL HIVGNRHLAY HVKLQRLFKN
     CTTVASNGKF VILQAQKK