RLMG_PSEMY
ID RLMG_PSEMY Reviewed; 374 AA.
AC A4XQA3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=Pmen_0751;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABP83519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000680; ABP83519.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041772801.1; NC_009439.1.
DR AlphaFoldDB; A4XQA3; -.
DR SMR; A4XQA3; -.
DR STRING; 399739.Pmen_0751; -.
DR PRIDE; A4XQA3; -.
DR EnsemblBacteria; ABP83519; ABP83519; Pmen_0751.
DR KEGG; pmy:Pmen_0751; -.
DR PATRIC; fig|399739.8.peg.762; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_040288_4_0_6; -.
DR OrthoDB; 1027015at2; -.
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..374
FT /note="Ribosomal RNA large subunit methyltransferase G"
FT /id="PRO_0000366478"
SQ SEQUENCE 374 AA; 40592 MW; EAC2DE5495969F09 CRC64;
MPIFTTPFAS LELLRQPHQP NEPLQAFDAA DEYLLNHLHE QGLRAEDSLL LLNDSFGALA
CSLAGRCQVT SSSDSHLGFI ALENNLAGNG LNRDAVRFLP SSETPQGPFD WVLIRVPKTL
ALLEEQLIRL HGQLAPGARV VAAAMVKHLP RAAGDLLEKY IGPVQASLAV KKARLLLATP
EAKAAPHSPY PTRYRLDKPA LELINHANVF CRDGLDIGTR AFLPHLPRHL DARRVADLGC
GNGVLGIAYA LGSPQAQLTL VDESYMAVQS ARENWAAALG ERPATIRAGD GLAEQPAGSL
DLVLCNPPFH QQQVVGDFLA WRMFQQARAA LVTGGELWIV GNRHLGYHAK LARLFRGVEQ
VAANPKFVVL KASK