RLMG_ECODH
ID RLMG_ECODH Reviewed; 378 AA.
AC B1XG88;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ECDH10B_3259;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(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; CP000948; ACB04168.1; -; Genomic_DNA.
DR RefSeq; WP_000018695.1; NC_010473.1.
DR AlphaFoldDB; B1XG88; -.
DR SMR; B1XG88; -.
DR PRIDE; B1XG88; -.
DR KEGG; ecd:ECDH10B_3259; -.
DR HOGENOM; CLU_040288_4_0_6; -.
DR OMA; DFLAWRM; -.
DR BioCyc; ECOL316385:ECDH10B_RS16575-MON; -.
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..378
FT /note="Ribosomal RNA large subunit methyltransferase G"
FT /id="PRO_0000366456"
SQ SEQUENCE 378 AA; 42331 MW; 0496E8BBD36FFB2C CRC64;
MSHLDNGFRS LTLQRFPATD DVNPLQAWEA ADEYLLQQLD DTEIRGPVLI LNDAFGALSC
ALAEHKPYSI GDSYISELAT RENLRLNGID ESSVKFLDST ADYPQQPGVV LIKVPKTLAL
LEQQLRALRK VVTSDTRIIA GAKARDIHTS TLELFEKVLG PTTTTLAWKK ARLINCTFNE
PQLADAPQTV SWKLEGTDWT IHNHANVFSR TGLDIGARFF MQHLPENLEG EIVDLGCGNG
VIGLTLLDKN PQAKVVFVDE SPMAVASSRL NVETNMPEAL DRCEFMINNA LSGVEPFRFN
AVLCNPPFHQ QHALTDNVAW EMFHHARRCL KINGELYIVA NRHLDYFHKL KKIFGNCTTI
ATNNKFVVLK AVKLGRRR
