ID E6UXT0_VARPE Unreviewed; 213 AA.
AC E6UXT0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE EC=2.1.1.170 {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 OrderedLocusNames=Varpa_0051 {ECO:0000313|EMBL:ADU34274.1};
OS Variovorax paradoxus (strain EPS).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34274.1, ECO:0000313|Proteomes:UP000008917};
RN [1] {ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Orwin P., Han J.-I.G., Woyke T.;
RT "Complete sequence of Variovorax paradoxus EPS.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU34274.1, ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|EMBL:ADU34274.1,
RC ECO:0000313|Proteomes:UP000008917};
RX PubMed=24158554;
RA Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT "Genome of the Root-Associated Plant Growth-Promoting Bacterium Variovorax
RT paradoxus Strain EPS.";
RL Genome Announc. 1:e00843-e00813(2013).
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 527 of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.170; Evidence={ECO:0000256|HAMAP-
CC 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; CP002417; ADU34274.1; -; Genomic_DNA.
DR RefSeq; WP_013538521.1; NC_014931.1.
DR AlphaFoldDB; E6UXT0; -.
DR STRING; 595537.Varpa_0051; -.
DR KEGG; vpe:Varpa_0051; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_2_0_4; -.
DR OrthoDB; 9808773at2; -.
DR Proteomes; UP000008917; 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 PIRSF; PIRSF003078; 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 ECO:0000313|EMBL:ADU34274.1};
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, ECO:0000313|EMBL:ADU34274.1}.
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 132..133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 213 AA; 22839 MW; E9FB4692D8FA7B7B CRC64;
MSAPIDTLRA GAGALGVTLS DRQGEQLLAY GTLMLKWNKV YNLTAVRDPA GVMTHHLLDS
LAVIAPLQRQ YPEQGRLLDV GSGAGLPGVI IAIMRPDIDV SCLDAVAKKA AFVQQVAVEL
ELPNLRGLHA RVELLEGSYN VISSRAFASL PDFFNGSKHL LPADGVWLAM KGKMPGDELA
VLPPEVAVFH VEQLTVPGLD AERCIVWARK ASV
//
