ID   Y818_MYCUA              Reviewed;         324 AA.
AC   A0PM89;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_0818;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_0818;
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; ABL03458.1; -; Genomic_DNA.
DR   RefSeq; WP_011739083.1; NC_008611.1.
DR   AlphaFoldDB; A0PM89; -.
DR   SMR; A0PM89; -.
DR   STRING; 362242.MUL_0818; -.
DR   EnsemblBacteria; ABL03458; ABL03458; MUL_0818.
DR   KEGG; mul:MUL_0818; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; RMADNMA; -.
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..324
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_0818"
FT                   /id="PRO_0000361256"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35016 MW;  B2873411C78E59FD CRC64;
     MTSTGSTRYD GDSWDLASSV GVTATMVAAA RAMATRAENP LINDPYAEPL VRAVGVDLLT
     RLATGEFNVA DLDDDPQRPL GPIGDVADNM AVRTRFFDDF FLAATRAGLE QVVILASGRD
     ARAYRLPWPP QTVVYEIDLP QVIDFKSRTL ADLGAAPTAD RRVVAVDLRE DWPAALRAAG
     FDPNQPTAWS AEGLLGYLPP EAQDRLLDTV TELSAPGSRL AAECLSGVDP AEEEQIKERM
     QEVSARWRAH GFDVDMVGLV YFGDRNEAVP YLSDRGWLLT STPLPELRAA NGLAPAAVDD
     DGPSVDMLYV SGTLYTTPRP DPAP