ID A0A1G9S032_9ACTN Unreviewed; 386 AA.
AC A0A1G9S032;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_01859};
DE EC=2.1.1.174 {ECO:0000256|HAMAP-Rule:MF_01859};
DE AltName: Full=23S rRNA m2G1835 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01859};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmG {ECO:0000256|HAMAP-Rule:MF_01859};
GN Name=rlmG {ECO:0000256|HAMAP-Rule:MF_01859};
GN ORFNames=SAMN05444921_10693 {ECO:0000313|EMBL:SDM28833.1};
OS Streptomyces wuyuanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM28833.1, ECO:0000313|Proteomes:UP000199063};
RN [1] {ECO:0000313|Proteomes:UP000199063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the guanine in position 1835
CC (m2G1835) of 23S rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01859};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01859}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.
CC {ECO:0000256|HAMAP-Rule:MF_01859}.
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DR EMBL; FNHI01000006; SDM28833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9S032; -.
DR STRING; 1196353.SAMN05444921_10693; -.
DR OrthoDB; 29650at2; -.
DR Proteomes; UP000199063; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR017237; rRNA_m2G-MeTrfase_RlmG.
DR InterPro; IPR046977; RsmC/RlmG.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR47816:SF5; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE G; 1.
DR PANTHER; PTHR47816; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01859};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01859,
KW ECO:0000313|EMBL:SDM28833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199063};
KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01859};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01859};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01859}.
FT DOMAIN 211..381
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 386 AA; 41858 MW; CCE55E35C7811E90 CRC64;
MNTFTTPWGD LGLTRFPEDP RDPLRAWDAS DEYLLRRLEG ETLDGTVVVV GDRWGALATA
LAALRPVQIS DSHLTQQATR ANLARNRTAA EAGGVRLLST QDTPPERVDV LLVRVPKSLA
LLEDQLQRLA PRLTADTLVV GTGMVTEIHT STLKLFERIV GPTRTSLAVK KARLIHCTPA
PDRIGPAAVA EGPWPHSYAL PAGVGVMSGR QVTNHAGIFC ADRLDIGTRF FLEHLPDRRG
PLRVVDLGCG NGVVGTAVAV ANPEAEVVFT DESFQAVASA EATFRANTGP SAKAAFVVGD
ALSGTERESA DLVLNNPPFH THRALTDSTS WRMFTGARRA LRPGGELWVI GNRHLGYHVR
LRRIFGNCET VASNPKFVVL RAVKRR
//