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Database: UniProt
Entry: A0A0M9UBP6_9CHLR
LinkDB: A0A0M9UBP6_9CHLR
Original site: A0A0M9UBP6_9CHLR 
ID   A0A0M9UBP6_9CHLR        Unreviewed;       233 AA.
AC   A0A0M9UBP6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=gidB {ECO:0000313|EMBL:GAP62098.1};
GN   Synonyms=rsmG {ECO:0000256|HAMAP-Rule:MF_00074};
GN   ORFNames=ARMA_0521 {ECO:0000313|EMBL:GAP62098.1};
OS   Ardenticatena maritima.
OC   Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC   Ardenticatenaceae; Ardenticatena.
OX   NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP62098.1, ECO:0000313|Proteomes:UP000037784};
RN   [1] {ECO:0000313|EMBL:GAP62098.1, ECO:0000313|Proteomes:UP000037784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|EMBL:GAP62098.1,
RC   ECO:0000313|Proteomes:UP000037784};
RA   Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT   "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT   Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL   Genome Announc. 3:e01145-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000037784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA   Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT   "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT   Ardenticatena maritima Strain 110S.";
RL   Submitted (AUG-2015) 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:GAP62098.1}.
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DR   EMBL; BBZA01000031; GAP62098.1; -; Genomic_DNA.
DR   RefSeq; WP_054492023.1; NZ_LGKN01000006.1.
DR   AlphaFoldDB; A0A0M9UBP6; -.
DR   STRING; 872965.SE16_12715; -.
DR   InParanoid; A0A0M9UBP6; -.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000037784; 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:GAP62098.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037784};
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:GAP62098.1}.
FT   BINDING         72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         95..97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         123..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   233 AA;  25422 MW;  35BD084325F955CF CRC64;
     MPIPPPPIAL TPEQMRLLDA YADALQDGNR RINLTAITDR DAIFIKHFWD TLAITPHLDA
     LLPPDAHLID VGTGGGIPGL VLAIARPTWR ITLLDATRKK VHFVEETART LGLNNVRAVW
     GRAEEVARES DHREQYDAAV ARAVAPLRVL AELCLPFVRV GGWWCAMKGP AVAEEAAEAH
     AAIALLGGEP PHIEMVEVPG ADAQRAVVLV RKHAPTPERY PRRAGVPHKR PLG
//
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