ID   Y816_MYCUA              Reviewed;         304 AA.
AC   A0PM87;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_0816;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_0816;
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}.
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; CP000325; ABL03456.1; -; Genomic_DNA.
DR   RefSeq; WP_011739081.1; NC_008611.1.
DR   AlphaFoldDB; A0PM87; -.
DR   SMR; A0PM87; -.
DR   STRING; 362242.MUL_0816; -.
DR   EnsemblBacteria; ABL03456; ABL03456; MUL_0816.
DR   KEGG; mul:MUL_0816; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; FFIKMMD; -.
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..304
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_0816"
FT                   /id="PRO_0000361254"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  32932 MW;  D0D85963AA52ACED CRC64;
     MARTHDDKWD LASSVGATAT IVAAGRAMAS RDPRGLIDDP FAEPLVRAVG VDFFIKMMDG
     EFDLSVLQNV SSAKAQAMVD GMAVRTKYFD DYFGDAIKSG IRQAVILASG LDARAYRLPW
     PADTVVYELD QPQVIEFKTN VLADLGAEPR ATRRAIPIDL RGDWPVALRA AGLDTTAPTA
     WLAEGLLIYL PPEAQDRLFD NITALSAPGS TVATEFVPGI VDFDVDRARQ MSGPFRDHGL
     DIDMSSLVYT GARNHVVDYL RAKGWDAEGV TRSKLFERNG MAVPAPSDDD PLGEIIFISA
     ALTG