ID A0A0C3MK69_9PORP Unreviewed; 207 AA.
AC A0A0C3MK69;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=BA92_01135 {ECO:0000313|EMBL:KIO47083.1}, DMB45_14210
GN {ECO:0000313|EMBL:PXZ42736.1};
OS Sanguibacteroides justesenii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Sanguibacteroides.
OX NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO47083.1, ECO:0000313|Proteomes:UP000031980};
RN [1] {ECO:0000313|EMBL:KIO47083.1, ECO:0000313|Proteomes:UP000031980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO47083.1,
RC ECO:0000313|Proteomes:UP000031980};
RA Sydenham T.V., Hasman H., Justensen U.S.;
RT "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT genome.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PXZ42736.1, ECO:0000313|Proteomes:UP000248308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ42736.1,
RC ECO:0000313|Proteomes:UP000248308};
RX PubMed=25814588;
RA Sydenham T.V., Hasman H., Justesen U.S.;
RT "Draft Genome Sequences of Sanguibacteroides justesenii, gen. nov., sp.
RT nov., Strains OUH 308042T (= ATCC BAA-2681T) and OUH 334697 (= ATCC BAA-
RT 2682), Isolated from Blood Cultures from Two Different Patients.";
RL Genome Announc. 3:e00005-15(2015).
RN [3] {ECO:0000313|EMBL:PXZ42736.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ42736.1};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) 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:KIO47083.1}.
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DR EMBL; JPIU01000024; KIO47083.1; -; Genomic_DNA.
DR EMBL; QJPL01000012; PXZ42736.1; -; Genomic_DNA.
DR RefSeq; WP_041503009.1; NZ_QJPL01000012.1.
DR AlphaFoldDB; A0A0C3MK69; -.
DR OrthoDB; 9808773at2; -.
DR Proteomes; UP000031980; Unassembled WGS sequence.
DR Proteomes; UP000248308; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00074};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074,
KW ECO:0000313|EMBL:KIO47083.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031980};
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:KIO47083.1}.
FT COILED 12..39
FT /evidence="ECO:0000256|SAM:Coils"
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 122..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 207 AA; 23848 MW; B942BA197427793B CRC64;
MEFIQKYFAG LSDLQKKRLE QLEGLYREWN EKINVISRKD IGELEIHHVL HSMAIAKVIS
FKPGTRVMDV GTGGGFPGIP LAILFPETDF FLVDSIGKKI KVVREIVTAL GLKNVRAEQL
RVEEVKEKFD FIVSRAVTAF PTFMSWTRNR IRKGGNNELP NGILYIKGGD FDEEIKPYRD
KVRVYGIPDF FEEEFFATKK IIYMPLL
//
