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Database: UniProt
Entry: V4PW46_9CAUL
LinkDB: V4PW46_9CAUL
Original site: V4PW46_9CAUL 
ID   V4PW46_9CAUL            Unreviewed;       215 AA.
AC   V4PW46;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ORFNames=ABENE_09825 {ECO:0000313|EMBL:ESQ91624.1};
OS   Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ91624.1, ECO:0000313|Proteomes:UP000017837};
RN   [1] {ECO:0000313|EMBL:ESQ91624.1, ECO:0000313|Proteomes:UP000017837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ91624.1,
RC   ECO:0000313|Proteomes:UP000017837};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESQ91624.1}.
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DR   EMBL; AWGB01000016; ESQ91624.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4PW46; -.
DR   STRING; 1121022.GCA_000376105_01040; -.
DR   PATRIC; fig|1121022.4.peg.1986; -.
DR   eggNOG; COG0357; Bacteria.
DR   Proteomes; UP000017837; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
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   Reference proteome {ECO:0000313|Proteomes:UP000017837};
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         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         134..135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   215 AA;  23959 MW;  F8B956D7A2A51D24 CRC64;
     MNHMTPEEMS ARLMFHVKHE AIADLQKFYQ VLADGNEVMN LVGPATLPDY WSRHVLDSAQ
     LLDCRPDART WADLGAGAGF PGIVLSILLK HSTTLADGPA PHVYLVESLT KRCRFLQTVV
     DDLNLPATVI NDRAENVSVK VDVVTARAVA PMIKLLGFAE GFIRKGADAW FLKGENVESE
     LVDAGKVWKF DVEQSESMSD PRGRVIHIRR LRRAR
//
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