ID A0A0S2KH62_9GAMM Unreviewed; 222 AA.
AC A0A0S2KH62;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PS2015_3056 {ECO:0000313|EMBL:ALO47680.1};
OS Pseudohongiella spirulinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO47680.1, ECO:0000313|Proteomes:UP000065641};
RN [1] {ECO:0000313|EMBL:ALO47680.1, ECO:0000313|Proteomes:UP000065641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO47680.1,
RC ECO:0000313|Proteomes:UP000065641};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013189; ALO47680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2KH62; -.
DR STRING; 1249552.PS2015_3056; -.
DR KEGG; pspi:PS2015_3056; -.
DR PATRIC; fig|1249552.3.peg.3088; -.
DR OrthoDB; 9808773at2; -.
DR Proteomes; UP000065641; 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:ALO47680.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065641};
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:ALO47680.1}.
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 138..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 222 AA; 24857 MW; FAA086803A27B8E8 CRC64;
MAAQERLRAI LRQGLAKLDL TLSDAQQQTL LDYVALLDKW NKAYNLSAVR DPLQMISRHL
LDSLTVAPCL AEIQADTQHS LSVLDVGTGA GLPGIPLAIC YPDIKFILLD SNGKKTRFLF
QVKTMLSLDN IQVENTRIER YQCPEQIDIV VSRAFASLSD FVLGCEHLCQ PHTRLLAMKG
LYPEQELADL PSHWRLQQAS AVQVPDTEGE RHIIELKQTG KN
//
