RLMG_PSESH
ID RLMG_PSESH Reviewed; 374 AA.
AC Q0EDR2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
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}; ORFNames=PHA56;
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MAFF 302282;
RX PubMed=16927007; DOI=10.1007/s00239-005-0271-4;
RA Genka H., Baba T., Tsuda M., Kanaya S., Mori H., Yoshida T., Noguchi M.T.,
RA Tsuchiya K., Sawada H.;
RT "Comparative analysis of argK-tox clusters and their flanking regions in
RT phaseolotoxin-producing Pseudomonas syringae pathovars.";
RL J. Mol. Evol. 63:401-414(2006).
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; AB237164; BAF32922.1; -; Genomic_DNA.
DR RefSeq; WP_041924638.1; NZ_RBUR01000216.1.
DR AlphaFoldDB; Q0EDR2; -.
DR SMR; Q0EDR2; -.
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_0000366484"
SQ SEQUENCE 374 AA; 40697 MW; DB5EDA67617EF282 CRC64;
MPLLISPFAE LDLIRQPEQQ DEPLQAFDAA DEYLLNHVAE TGLSLQSRVL VLNDSFGALA
ASLASHATVV SSTDSFLAAQ GLEKNLARNG MSYDAVPHIP ASEPLSGPFD WVLIRVPKTL
ALLEEQLIRL QGQLAPGARV VAAAMVKHLP RSAGDLLEEY VGPVQASLAV KKARLLFATP
QPMEVRTSPY PTRYRLDEPA IELLNHANVF CRDGLDIGTR AFLPYLPKNL GTARVADLGC
GNGVLAIASA LDNPQAHYTL VDESFMAVQS AAENWRATLG ERVVEVRAAD GLDTQEPDSL
DVVLCNPPFH QQQVVGDFLA WRMFLQARAA LVNGGALYIV GNRHLGYHTK LSRLFRGVEQ
VAATPKFVIL KARK