ID   Y2766_MYCUA             Reviewed;         310 AA.
AC   A0PRV0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_2766;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_2766;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(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; CP000325; ABL05069.1; -; Genomic_DNA.
DR   RefSeq; WP_011740683.1; NC_008611.1.
DR   AlphaFoldDB; A0PRV0; -.
DR   SMR; A0PRV0; -.
DR   STRING; 362242.MUL_2766; -.
DR   EnsemblBacteria; ABL05069; ABL05069; MUL_2766.
DR   KEGG; mul:MUL_2766; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DFFTRWV; -.
DR   Proteomes; UP000000765; 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..310
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_2766"
FT                   /id="PRO_0000361245"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  33773 MW;  69EB55A6E0AC704E CRC64;
     MPRTDNDSWD LATSVGATAT MVAAARAIAT NADNPLIADR FAEPLVRAVG VDFFTRWVTG
     DLVVADVDDT ESGWQLAQMP DAMAVRARFF DAFFQDATRA GVRQAVILAS GLDARAYRLD
     WPAGMTVFEI DQPEVIAFKT TTLAGLGAVP RADLRTVAVD LRQDWPKALT EAGFDAGRPT
     AWIAEGLFGY LPPEAQDRLL DNITALSATG SRLACEAIPN RPQQDAEKAR ELMRKATARW
     REHGFELEFG DLGYEGDRAD VELYLQNLGW QSVGTQMSQL LADNGAAPIP HNNDSVTMAD
     TIYYSSVLTA