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Database: UniProt
Entry: A0A1U7GD08_9BACT
LinkDB: A0A1U7GD08_9BACT
Original site: A0A1U7GD08_9BACT 
ID   A0A1U7GD08_9BACT        Unreviewed;       483 AA.
AC   A0A1U7GD08;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BGO49_08200 {ECO:0000313|EMBL:OJW08804.1};
OS   Planctomycetales bacterium 71-10.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX   NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW08804.1, ECO:0000313|Proteomes:UP000185848};
RN   [1] {ECO:0000313|EMBL:OJW08804.1, ECO:0000313|Proteomes:UP000185848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71-10 {ECO:0000313|EMBL:OJW08804.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJW08804.1}.
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DR   EMBL; MKTT01000129; OJW08804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7GD08; -.
DR   STRING; 1895807.BGO49_08200; -.
DR   Proteomes; UP000185848; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd18095; SpoU-like_rRNA-MTase; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
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   Pfam; PF00588; SpoU_methylase; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 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:OJW08804.1};
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:OJW08804.1}.
FT   DOMAIN          348..475
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         82
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   483 AA;  52428 MW;  E0CD1DE830FB6ACD CRC64;
     MRPGRAGLEA ILRDCGVELA SNQYDALWTY HQMLRAANAS LNMTRIHNFE NMVLKHYVDS
     LLVLDFLDLP SPIIDMGSGP GLPGVPLKIA RPDVRMILCE PRSARVEFLS QVCEKLGFEG
     AEVYGHKLGP DYPGRVKGVV TRAVASIAET FERVAACIEP GGRMIFMKGP GCDPEVDEAR
     RDWTIWFRLE ADHPYTIPGT THDRRLVVYE RTDADPPLIE KDASARVARS FAGTVREITS
     ESNATYRLLS DLLTGRGVRK HGLAILSGPR ITAEVAEKFP GRVEGWITDA EGPPPADPSW
     TWHRLASPLF KALDVAGTHA PLLLARAPVI DAWSDSSPWP AGCTLFVPFQ DPENVGAVIR
     SAAAFGVPRV VLLQEAAHPF HPRASRAAGP ALFQVELMTG PSIRELSSSS HPLIALDASG
     EPLDAEPFPE TFGLVVGVEG PGLPEHLRRG PKRRVPIVEG VESLNAATAT AVALYAWSRL
     APG
//
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