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Database: UniProt
Entry: K0Z6D8_9ACTO
LinkDB: K0Z6D8_9ACTO
Original site: K0Z6D8_9ACTO 
ID   K0Z6D8_9ACTO            Unreviewed;       232 AA.
AC   K0Z6D8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE            EC=2.1.1.- {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=HMPREF9241_00382 {ECO:0000313|EMBL:EJZ87754.1};
OS   Schaalia turicensis ACS-279-V-Col4.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Schaalia.
OX   NCBI_TaxID=883077 {ECO:0000313|EMBL:EJZ87754.1, ECO:0000313|Proteomes:UP000003994};
RN   [1] {ECO:0000313|EMBL:EJZ87754.1, ECO:0000313|Proteomes:UP000003994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-279-V-Col4 {ECO:0000313|EMBL:EJZ87754.1,
RC   ECO:0000313|Proteomes:UP000003994};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinomyces turicensis ACS-279-V-COL4.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC       position 518 of 16S rRNA. {ECO:0000256|HAMAP-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:EJZ87754.1}.
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DR   EMBL; AGWQ01000003; EJZ87754.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0Z6D8; -.
DR   STRING; 883077.HMPREF9241_00382; -.
DR   PATRIC; fig|883077.3.peg.372; -.
DR   eggNOG; COG0357; Bacteria.
DR   HOGENOM; CLU_065341_5_0_11; -.
DR   Proteomes; UP000003994; 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   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   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:EJZ87754.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003994};
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:EJZ87754.1}.
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         146..147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   232 AA;  25847 MW;  E0CDC69479C92B48 CRC64;
     MSELDISADQ GEFHDPLKRK VGDPFIPEQP TDEVREFFGP AFSDVEEYVH MLEEEGEIRG
     LVGPREMPRL WSRHAVNAAA VLDFLPRSGQ ILDIGSGAGL PGIIIAICRP ELDVHLAEPM
     QRRCEWLSDV IDHLALDNVT LHQVRAEELR GKGQADVITA RAVANMSKLI RMTTKLIAPG
     GSLVALKGRR APIEIDEAAK ELKSHHLRAQ IHEVPSIMEE ESTYVVVCKR QK
//
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