RLMG_ALIF1
ID RLMG_ALIF1 Reviewed; 382 AA.
AC Q5E6X8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=VF_0723;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85218.1; -; Genomic_DNA.
DR RefSeq; WP_011261441.1; NC_006840.2.
DR RefSeq; YP_204106.1; NC_006840.2.
DR AlphaFoldDB; Q5E6X8; -.
DR SMR; Q5E6X8; -.
DR STRING; 312309.VF_0723; -.
DR EnsemblBacteria; AAW85218; AAW85218; VF_0723.
DR KEGG; vfi:VF_0723; -.
DR PATRIC; fig|312309.11.peg.717; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_040288_4_0_6; -.
DR OMA; DFLAWRM; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000000537; Chromosome I.
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..382
FT /note="Ribosomal RNA large subunit methyltransferase G"
FT /id="PRO_0000366532"
SQ SEQUENCE 382 AA; 43458 MW; 53EF7373E34B5DF6 CRC64;
MKTELSLLDR SLNLQRYPKR AQELLQAWDA GDEYIIKYVE EELNLEDGKN ILILNDNFGA
LSCWFSDKHN VTMMTDSFVS QRGTLKNLQR NQCNRVQLIT STEEMPQGFD LVLMQIPKNN
RMLTWQLQQL RQSMDSSCPI IAVNKAKEIH SSTLELFEDY LGETKTSLAW KKHRLVFSNA
NVSNPKTIAE AVCWSVDNED IDLLNYPNVY SGEKLDQGAR FMLDHIPSDP ELRHIIDLGC
GNGVLSVKAG QLNPEARITC VDESFMAVES AHRNLEVNLG KERQFQFIAN NCLDGFKKHS
SYLVLCNPPF HQGQAITDHI AWQMFCDAKH ILCKDGKLLV IGNRHLDYDG KLCRLFGEEN
VTTVASNSKF VILEAVKAEK SK
