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Database: UniProt
Entry: A0A101ARR4_9MYCO
LinkDB: A0A101ARR4_9MYCO
Original site: A0A101ARR4_9MYCO 
ID   A0A101ARR4_9MYCO        Unreviewed;       225 AA.
AC   A0A101ARR4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=AU194_21785 {ECO:0000313|EMBL:KUI27767.1};
OS   Mycobacterium sp. GA-2829.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI27767.1, ECO:0000313|Proteomes:UP000053444};
RN   [1] {ECO:0000313|EMBL:KUI27767.1, ECO:0000313|Proteomes:UP000053444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-2829 {ECO:0000313|EMBL:KUI27767.1,
RC   ECO:0000313|Proteomes:UP000053444};
RG   TB Trials Study Group;
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA   Grewal H.M.S.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC       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:KUI27767.1}.
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DR   EMBL; LQIT01000041; KUI27767.1; -; Genomic_DNA.
DR   RefSeq; WP_059091492.1; NZ_LQIT01000041.1.
DR   AlphaFoldDB; A0A101ARR4; -.
DR   STRING; 1772283.AU194_21785; -.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000053444; 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   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:KUI27767.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053444};
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:KUI27767.1}.
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
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         121..122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         139
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   225 AA;  24390 MW;  1163D27B1AF1895A CRC64;
     MKHGEPPPAA EAVFGERLPL ACRYTELLAT AGVERGLIGP RETDRLWDRH VLNSAAVGEL
     VEPDQWIADI GSGAGLPGIP LALARPDVHV TLIEPMLRRS EFLSEVVEEL GIDVRVIRGR
     AEDADVLGEV GEMDVVTSRA VAALDKLATW SMGLLRVGGE MLALKGARAE TEIEENRRVL
     TRAGAVDVRV LKCGAEYLEP PATVVAARRG APLKKRNRPM RSGRR
//
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