GenomeNet

Database: UniProt
Entry: D0SI96_ACIJU
LinkDB: D0SI96_ACIJU
Original site: D0SI96_ACIJU 
ID   D0SI96_ACIJU            Unreviewed;       210 AA.
AC   D0SI96;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 63.
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   Synonyms=gidB {ECO:0000313|EMBL:EEY93568.1};
GN   ORFNames=HMPREF0026_00844 {ECO:0000313|EMBL:EEY93568.1};
OS   Acinetobacter junii SH205.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575587 {ECO:0000313|EMBL:EEY93568.1, ECO:0000313|Proteomes:UP000018442};
RN   [1] {ECO:0000313|Proteomes:UP000018442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH205 {ECO:0000313|Proteomes:UP000018442};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG705011; EEY93568.1; -; Genomic_DNA.
DR   RefSeq; WP_005402532.1; NZ_GG705011.1.
DR   AlphaFoldDB; D0SI96; -.
DR   HOGENOM; CLU_065341_2_0_6; -.
DR   Proteomes; UP000018442; 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   ECO:0000313|EMBL:EEY93568.1};
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:EEY93568.1}.
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
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         127..128
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   210 AA;  23678 MW;  1AF4576F35994911 CRC64;
     MHHFFQELKQ GSQALGLNLS EEALTLLLKY QDALVLWNKA YNLTAIRDPK EMLVKHLLDS
     LSILNDLPKG RLLDVGTGGG MPGMIIALCQ PERDCVLLDS NGKKIRFLKQ FIADLNLKNV
     IAVQTRVENE DSINELGQFD VITSRAFASL TDFVDAAQPY MHEKSIIAAM KGLIPTDELD
     QLKGQYQSQI VELKVPRLDE QRHLLLLQRI
//
DBGET integrated database retrieval system