ID   Y945_MYCBP              Reviewed;         325 AA.
AC   A1KH25;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_0945c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_0945c;
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; CAL70931.1; -; Genomic_DNA.
DR   RefSeq; WP_003404654.1; NC_008769.1.
DR   AlphaFoldDB; A1KH25; -.
DR   SMR; A1KH25; -.
DR   PRIDE; A1KH25; -.
DR   KEGG; mbb:BCG_0945c; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; NWDINTS; -.
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..325
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_0945c"
FT                   /id="PRO_0000361153"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  36073 MW;  6280F61020906EDE CRC64;
     MRTEDDSWDV TTSVGSTGLL VAAARALETQ KADPLAIDPY AEVFCRAAGG EWADVLDGKL
     PDHYLTTGDF GEHFVNFQGA RTRYFDEYFS RATAAGMKQV VILAAGLDSR AFRLQWPIGT
     TIFELDRPQV LDFKNAVLAD YHIRPRAQRR SVAVDLRDEW QIALCNNGFD ANRPSAWIAE
     GLLVYLSAEA QQRLFIGIDT LASPGSHVAV EEATPLDPCE FAAKLERERA ANAQGDPRRF
     FQMVYNERWA RATEWFDERG WRATATPLAE YLRRVGRAVP EADTEAAPMV TAITFVSAVR
     TGLVADPART SPSSTSIGFK RFEAD