ID   Y776_MYCBP              Reviewed;         367 AA.
AC   A1KGK7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_0776c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_0776c;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; AM408590; CAL70762.1; -; Genomic_DNA.
DR   RefSeq; WP_003403691.1; NC_008769.1.
DR   AlphaFoldDB; A1KGK7; -.
DR   SMR; A1KGK7; -.
DR   GeneID; 45424691; -.
DR   KEGG; mbb:BCG_0776c; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; RMADNMA; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..367
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_0776c"
FT                   /id="PRO_0000361150"
FT   REGION          348..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..167
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  40876 MW;  5FF038903881804A CRC64;
     MTYTGSIRCE GDTWDLASSV GATATMVAAA RAMATRAANP LINDQFAEPL VRAVGVDVLT
     RLASGELTAS DIDDPERPNA SMVRMAEHHA VRTKFFDEFF MDATRAGIRQ VVILASGLDS
     RAYRLAWPAQ TVVYEIDQPQ VMEFKTRTLA ELGATPTADR RVVTADLRAD WPTALGAAGF
     DPTQPTAWSA EGLLRYLPPE AQDRLLDNVT ALSVPDSRFA TESIRNFKPH HEERMRERMT
     ILANRWRAYG FDLDMNELVY FGDRNEPASY LSDNGWLLTE IKSQDLLTAN GFQPFEDEEV
     PLPDFFYVSA RLQRKHRQYP AHRKPAPSWR HTACPVNELS KSAAYTMTRS DAHQASTTAP
     PPPGLTG