ID   RLMG_SHEFN              Reviewed;         392 AA.
AC   Q07YH6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Sfri_3101;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
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   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI72938.1; -; Genomic_DNA.
DR   RefSeq; WP_011638544.1; NC_008345.1.
DR   AlphaFoldDB; Q07YH6; -.
DR   SMR; Q07YH6; -.
DR   STRING; 318167.Sfri_3101; -.
DR   DNASU; 4280004; -.
DR   EnsemblBacteria; ABI72938; ABI72938; Sfri_3101.
DR   KEGG; sfr:Sfri_3101; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_040288_4_0_6; -.
DR   OMA; DFLAWRM; -.
DR   OrthoDB; 1027015at2; -.
DR   Proteomes; UP000000684; Chromosome.
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; 2.
DR   PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..392
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000366509"
SQ   SEQUENCE   392 AA;  43460 MW;  EC646F5979966691 CRC64;
     MTTQFACSGI ELELFRYPSQ QASNLQAWDA ADEHLVKYLI DTEITATTTA ILNDNFGALT
     CALTMQYPHS ELLVETDAKT SLLGYQQNLL HNKLASTNIH WLNSRETLPQ NIQLVLMKLP
     KNLHYFGQQL ARLSTVLPAG TQILIGAKAK SINPALLASI EKNLGPASAS LAWKKTRVIS
     CISDGKKRSL AKAVSWNVDE LKLTISNLAN VFAANKLDIG ARIMLDNMPK GEFKHIIDLG
     CGNGILGLHA KQCYPNAQIH FVDDSDMAIA SAKHNWQANE LDTPSQDLQS QDPQTEQMPQ
     AFFHWDDCLS NLPADVEPDL VICNPPFHQG EAITDHIAWQ MFVDAHKRLK KGGLLHIVGN
     RHLAYHVKIN RIFKNCTTVA SNGKFVILQA IK