RLMG_SHIDS
ID RLMG_SHIDS Reviewed; 378 AA.
AC Q32BN8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=SDY_3267;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB63267.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000034; ABB63267.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000018683.1; NC_007606.1.
DR RefSeq; YP_404758.1; NC_007606.1.
DR AlphaFoldDB; Q32BN8; -.
DR SMR; Q32BN8; -.
DR STRING; 300267.SDY_3267; -.
DR PRIDE; Q32BN8; -.
DR EnsemblBacteria; ABB63267; ABB63267; SDY_3267.
DR KEGG; sdy:SDY_3267; -.
DR PATRIC; fig|300267.13.peg.3907; -.
DR HOGENOM; CLU_040288_4_0_6; -.
DR Proteomes; UP000002716; Chromosome.
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; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..378
FT /note="Ribosomal RNA large subunit methyltransferase G"
FT /id="PRO_0000366523"
SQ SEQUENCE 378 AA; 42300 MW; 6F79DDBA969B4BD8 CRC64;
MSHLDNGFRS LTLQRFPATD DVNPLQAWEA ADEYLLQQLD DTEIRGPVLI LNDAFGALSC
ALAEHKPYSI GDSYISELAT RENLRLNGID ESSVKFLDST ADYPQQPGVV LIKVPKTLAL
LEQQLRALRK VVTSDTRIIA GAKARDIHTS TLELFEKVLG PTTTTLAWKK ARLINCTFNE
PPLADAPQTV SWKLEGTDWT IHNHANVFSR TGLDIGARFF MQHLPENLEG EIVDLGCGNG
VIGLTLLDKN PQAKVVFVDE SPMAVASSRL NVETNMPEAL DRCEFMINNA LSGVEPFRFN
AVLCNPPFHQ QHALTDNVAW EMFHHARRCL KINGELYIVA NRHLDYFHKL KKIFGNCTTI
ATNNKFVVLK AVKLGRRR