RLMG_ALISL
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 03-AUG-2022, entry version 68.
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; Proteobacteria; 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 STRING; 316275.VSAL_I0947; -.
DR EnsemblBacteria; CAQ78632; CAQ78632; VSAL_I0947.
DR KEGG; vsa:VSAL_I0947; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_040288_4_0_6; -.
DR OMA; DFLAWRM; -.
DR OrthoDB; 1027015at2; -.
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 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; 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
