GenomeNet

Database: UniProt
Entry: A0A433RM02_9BACL
LinkDB: A0A433RM02_9BACL
Original site: A0A433RM02_9BACL 
ID   A0A433RM02_9BACL        Unreviewed;       249 AA.
AC   A0A433RM02;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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   ECO:0000313|EMBL:RUS48787.1};
GN   ORFNames=ELR57_00085 {ECO:0000313|EMBL:RUS48787.1};
OS   Cohnella sp. AR92.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=648716 {ECO:0000313|EMBL:RUS48787.1, ECO:0000313|Proteomes:UP000267180};
RN   [1] {ECO:0000313|EMBL:RUS48787.1, ECO:0000313|Proteomes:UP000267180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR92 {ECO:0000313|EMBL:RUS48787.1,
RC   ECO:0000313|Proteomes:UP000267180};
RX   PubMed=29166641; DOI=10.1159/000480541;
RA   Pisa J.H., Manfredi A.P., Perotti N.I., Romero H.G., Breccia J.D.,
RA   Martinez M.A.;
RT   "Agrowastes as Feedstock for the Production of Endo-?-Xylanase from
RT   Cohnella sp. Strain AR92.";
RL   J. Mol. Microbiol. Biotechnol. 27:277-288(2017).
CC   -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC       position 535 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:RUS48787.1}.
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; RZJR01000001; RUS48787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433RM02; -.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000267180; 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:RUS48787.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267180};
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:RUS48787.1}.
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         131..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   249 AA;  27568 MW;  114D2D12F3C2F765 CRC64;
     MDDPQKWLQQ QARELELELS DSQLSQFEQY YRLLVEWNEK MNLTGITERD AVYEKHFYDS
     LTVALAADLS IAGTSIADIG SGAGFPSIPL KIAFPELKVT IIDSLAKRIR FLEEVVARLG
     LANVACVHGR AEDIARLPEH RDQYDVVTAR AVARLAGLNE LCLPFAKTGG VFISMKGSDI
     QEELEESRFS LGKLGAKLAE VKRLELPIEK SERHLIMMTK ISATAKAYPR KAGVPLKSPL
     LASSSGVRL
//
DBGET integrated database retrieval system