ID   Y1935_MYCBP             Reviewed;         303 AA.
AC   A1KJW1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_1935c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_1935c;
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}.
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; AM408590; CAL71922.1; -; Genomic_DNA.
DR   RefSeq; WP_003409526.1; NC_008769.1.
DR   AlphaFoldDB; A1KJW1; -.
DR   SMR; A1KJW1; -.
DR   PRIDE; A1KJW1; -.
DR   KEGG; mbb:BCG_1935c; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; GSAASMW; -.
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..303
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_1935c"
FT                   /id="PRO_0000361144"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  33267 MW;  7480EB8065C70DA8 CRC64;
     MTTPEYGSLR SDDDHWDIVS NVGYTALLVA GWRALHTTGP KPLVQDEYAK HFITASADPY
     LEGLLANPRT SEDGTAFPRL YGVQTRFFDD FFNCADEAGI RQAVIVAAGL DCRAYRLDWQ
     PGTTVFEIDV PKVLEFKARV LSERGAVPKA HRVAVPADLR TDWPTPLTAA GFDPQRPSAW
     SVEGLLPYLT GDAQYALFAR IDELCAPGSR VALGALGSRL DHEQLAALET AHPGVNMSGD
     VNFSALTYDD KTDPVEWLVE HGWAVDPVRS TLELQVGYGL TPPDVDVKID SFMRSQYITA
     VRA