ID A0A1X1RIR3_MYCCE Unreviewed; 237 AA.
AC A0A1X1RIR3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AWB95_21270 {ECO:0000313|EMBL:ORV06929.1}, CQY23_22150
GN {ECO:0000313|EMBL:PIB74037.1};
OS Mycobacterium celatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV06929.1, ECO:0000313|Proteomes:UP000193907};
RN [1] {ECO:0000313|EMBL:ORV06929.1, ECO:0000313|Proteomes:UP000193907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV06929.1,
RC ECO:0000313|Proteomes:UP000193907};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PIB74037.1, ECO:0000313|Proteomes:UP000230971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12882 {ECO:0000313|EMBL:PIB74037.1,
RC ECO:0000313|Proteomes:UP000230971};
RX PubMed=29030295; DOI=10.1016/j.meegid.2017.10.013;
RA Tortoli E., Fedrizzi T., Meehan C.J., Trovato A., Grottola A.,
RA Giacobazzi E., Serpini G.F., Tagliazucchi S., Fabio A., Bettua C.,
RA Bertorelli R., Frascaro F., De Sanctis V., Pecorari M., Jousson O.,
RA Segata N., Cirillo D.M.;
RT "The new phylogeny of the genus Mycobacterium: The old and the news.";
RL Infect. Genet. Evol. 56:19-25(2017).
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:ORV06929.1}.
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DR EMBL; LQOM01000050; ORV06929.1; -; Genomic_DNA.
DR EMBL; PDKV01000043; PIB74037.1; -; Genomic_DNA.
DR RefSeq; WP_062539923.1; NZ_PDKV01000043.1.
DR STRING; 28045.AWB95_21270; -.
DR OrthoDB; 9808773at2; -.
DR Proteomes; UP000193907; Unassembled WGS sequence.
DR Proteomes; UP000230971; 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 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:ORV06929.1};
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:ORV06929.1}.
FT REGION 215..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 127..128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 237 AA; 25678 MW; 9D99CB3A5173BB01 CRC64;
MFHVKHVEVA TPPDAAAAIF GDRLGVAQRY AELLAGTGVE WGLLGPHEVD RVWDRHLLNS
AAVAELLQSG ARVADIGSGA GLPGLPLAIA RPDIRMVLVE SLLRRTEFLR DAVAELELDV
DVLRGRAEDR AVRERVGGSD VVVSRAVAPL DKLTRWSLAL LRPGGRMLAI KGERATEEVG
EHRRVMTELG AVNVRVVKCG VNYLSPPATV VVAQRGKPAP MGQRPRPRPC RPNRESL
//
