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Database: UniProt
Entry: B6EIC1
LinkDB: B6EIC1
Original site: B6EIC1 
ID   RLMG_ALISL              Reviewed;         382 AA.
AC   B6EIC1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=VSAL_I0947;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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; FM178379; CAQ78632.1; -; Genomic_DNA.
DR   RefSeq; WP_012549717.1; NC_011312.1.
DR   AlphaFoldDB; B6EIC1; -.
DR   SMR; B6EIC1; -.
DR   KEGG; vsa:VSAL_I0947; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_040288_4_0_6; -.
DR   Proteomes; UP000001730; Chromosome 1.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR   InterPro; IPR017237; rRNA_m2G-MeTrfase_RlmG.
DR   InterPro; IPR046977; RsmC/RlmG.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47816:SF5; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE G; 1.
DR   PANTHER; PTHR47816; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR   Pfam; PF05175; MTS; 1.
DR   PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 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..382
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000366447"
SQ   SEQUENCE   382 AA;  43624 MW;  0F5D26FADE64B112 CRC64;
     MKTELCLFDR TLNLQRYPKR AQELLQAWDA GDEFIIKHVE EELNLEDNKN ILILNDNFGA
     LSCWFSEKHN VTMMTDSFVS QRGTLKNLQR NQCNRVQLIS STEEMPEGFD LVIMQIPKNN
     RMLAWQLQQL RQSMTAECPI IAVNKAKEIH SSTLEVFEDY LGETKTSLAW KKHRLVFSNA
     NATNPLTIAE AVCWSVDNED IDLLNYPNVY SGERLDQGAR FMLEHIPVDA ELRHIIDLGC
     GNGVLSVKAA QLNPEARITC IDESFMAVES ARRNLEVNLG KERQFQFIAN NCLDGFKKHS
     SYLVLCNPPF HQGQAVTDHI AWQMFCDAKH ILCKEGKLLV IGNRHLDYDD KLCRLFGEEN
     VTTIASNSKF VILEAVKAEK SK
//
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