ID W0GK93_9MOLU Unreviewed; 232 AA.
AC W0GK93;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00074};
DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
DE Short=16S rRNA m7G methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
GN Name=rsmG {ECO:0000256|HAMAP-Rule:MF_00074};
GN ORFNames=P344_01245 {ECO:0000313|EMBL:AHI57614.1};
OS Spiroplasma mirum ATCC 29335.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=838561 {ECO:0000313|EMBL:AHI57614.1, ECO:0000313|Proteomes:UP000019260};
RN [1] {ECO:0000313|EMBL:AHI57614.1, ECO:0000313|Proteomes:UP000019260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMCA {ECO:0000313|EMBL:AHI57614.1,
RC ECO:0000313|Proteomes:UP000019260};
RA Landry C.A., Bastian F.O., Thune R.L.;
RT "Complete genome sequence of Spiroplasma mirum suckling mouse cataract
RT agent.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC rRNA. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00074}.
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DR EMBL; CP006720; AHI57614.1; -; Genomic_DNA.
DR RefSeq; WP_025317020.1; NZ_CP006720.1.
DR AlphaFoldDB; W0GK93; -.
DR STRING; 838561.P344_01245; -.
DR KEGG; smia:P344_01245; -.
DR KEGG; smir:SMM_0198; -.
DR PATRIC; fig|838561.3.peg.232; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_0_1_14; -.
DR OrthoDB; 9808773at2; -.
DR Proteomes; UP000019260; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00138; rsmG_gidB; 1.
DR PANTHER; PTHR31760; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR31760:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF02527; GidB; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00074};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
KW Reference proteome {ECO:0000313|Proteomes:UP000019260};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00074}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00074}.
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 125..126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 232 AA; 26656 MW; BD9E149A6B8B2B3A CRC64;
MIEIITNVFP NLIITEYQQN QLKIYYEYLI AQNKVMNLTA ITDEQEVYYK HFLDSLLLLK
HYQISENSNI CDVGSGAGFP GIVLKIINPN FKLTIIEALE KRCKFLTNLV AKLNLTNITI
IHARAEEYSY NHSETFDIIL SRAVANLGML LELTVRLAKV GGLLICYKGA NIKIELTASQ
KTIEVLGLEL INLQYENIDH LGERNICFFK KRQPTNNKYP RNFSQIKKWP IG
//
