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Database: UniProt
Entry: G6EBI2_9SPHN
LinkDB: G6EBI2_9SPHN
Original site: G6EBI2_9SPHN 
ID   G6EBI2_9SPHN            Unreviewed;       213 AA.
AC   G6EBI2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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=NSU_1703 {ECO:0000313|EMBL:EHJ61264.1};
OS   Novosphingobium pentaromativorans US6-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ61264.1, ECO:0000313|Proteomes:UP000004030};
RN   [1] {ECO:0000313|EMBL:EHJ61264.1, ECO:0000313|Proteomes:UP000004030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=US6-1 {ECO:0000313|EMBL:EHJ61264.1,
RC   ECO:0000313|Proteomes:UP000004030};
RX   PubMed=22275104; DOI=10.1128/JB.06476-11;
RA   Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT   "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT   pentaromativorans US6-1.";
RL   J. Bacteriol. 194:907-907(2012).
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:EHJ61264.1}.
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DR   EMBL; AGFM01000024; EHJ61264.1; -; Genomic_DNA.
DR   RefSeq; WP_007012618.1; NZ_CP009291.1.
DR   AlphaFoldDB; G6EBI2; -.
DR   STRING; 1088721.JI59_11565; -.
DR   KEGG; npn:JI59_11565; -.
DR   PATRIC; fig|1088721.3.peg.1682; -.
DR   eggNOG; COG0357; Bacteria.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000004030; 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:UP000004030};
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         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         129..130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   213 AA;  24052 MW;  22F63D75C798F242 CRC64;
     MITTEDEARA WLRALPECDD AAMTRLERLV DLLVEENQRQ NLVSAGSLDQ VWLRHIVDSA
     QLLPHVPRET SLPWMDLGTG AGFPGLVIAA LRPELEVLMV ESRTRRIEWL DRARIAMGLE
     RSRIVGQRLE MVETCQVGVI SARAFAPLDR LLTLSARFST SDTIWLLPKG RSAQQELDDL
     RKWRHVFHVE QSLTDPQAGI IVGNLTGRKG KTK
//
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