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RLMG_SHESA
ID   RLMG_SHESA              Reviewed;         377 AA.
AC   A0KTP8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Shewana3_0932;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
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   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-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; CP000469; ABK47167.1; -; Genomic_DNA.
DR   RefSeq; WP_011716061.1; NC_008577.1.
DR   AlphaFoldDB; A0KTP8; -.
DR   SMR; A0KTP8; -.
DR   STRING; 94122.Shewana3_0932; -.
DR   EnsemblBacteria; ABK47167; ABK47167; Shewana3_0932.
DR   KEGG; shn:Shewana3_0932; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_040288_4_0_6; -.
DR   OMA; DFLAWRM; -.
DR   OrthoDB; 1027015at2; -.
DR   Proteomes; UP000002589; 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; 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..377
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000366516"
SQ   SEQUENCE   377 AA;  41565 MW;  1924115ADFB2EDBD CRC64;
     MTTQFSVAGI ELELFRYPAS QESNLQAWDA ADEHLINTLV EGGQTAVPTA IINDSFGALS
     CALSRLNPDW PLNVETDART SFLGAEQNHH RNQLPMDNLT RFTSRDALPC DLALVLMKLP
     KNLTYFAHQL MRLSQVLPAG CKVLVGAKAK SINASLLEVF ATHLGPASAS LAWKKTRVIT
     CISDGKPRAL PKEVTWDIPE FNLHISNLSN VFAANKLDIG ARIMLDNLPQ GDFKTIVDLG
     CGNGVLGLRA AQLYPNADIH FIDDSEMAVA SAKANWANNQ LPAEKGHFHW DDCMTHLPDG
     VEPDLVLCNP PFHQGEAITD HIAWQMFLDA RRRLKNGGIL HIVGNRHLAY HVKLQRLFKN
     CTTVASNGKF VILQAQK
 
 
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