RLMG_VIBA3
ID RLMG_VIBA3 Reviewed; 383 AA.
AC B7VKD0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=VS_0691;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) 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; FM954972; CAV17685.1; -; Genomic_DNA.
DR RefSeq; WP_012603366.1; NC_011753.2.
DR AlphaFoldDB; B7VKD0; -.
DR SMR; B7VKD0; -.
DR STRING; 575788.VS_0691; -.
DR EnsemblBacteria; CAV17685; CAV17685; VS_0691.
DR KEGG; vsp:VS_0691; -.
DR PATRIC; fig|575788.5.peg.2039; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_040288_4_0_6; -.
DR OMA; DFLAWRM; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000009100; 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 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; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..383
FT /note="Ribosomal RNA large subunit methyltransferase G"
FT /id="PRO_1000188701"
SQ SEQUENCE 383 AA; 43474 MW; A56851E640FADACE CRC64;
MKTELTLLDR TLTLHRFPNR SNETLQAWDA GDEYIISHVE EMNLEPGKHI LIMNDSFGAL
SAWFSKDHDV TMMSDSFISH RGALKNLQRN QSNRVNFLNT MDDIPHGIDL VIMQLPKTNR
HLVWQLSQLR QALPEGCQVI GVNKVKDIHT STLNIFEKYL GETKTSLAKK KHRLVFSSPN
CQPIQTVEPF VEWDVDGEDI RLKNLPNVYS GEALDQGARY MLEHIPQDPE LRHIIDLGCG
NGVLSVKAGQ LNPQARITCV DESFMAVESA RQNIKDNLGE EGNFQFIANN CLDGFKKNST
YLVMCNPPFH QQQAITDHIA WQMFCDAKHV LSNGGKLIVI GNRHLGYDVK LARLFGEANV
ETLELNQKFE ILQATREPAN FNK