ID   Y706_MYCUA              Reviewed;         313 AA.
AC   A0PLZ1;
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_0706;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_0706;
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; ABL03360.1; -; Genomic_DNA.
DR   RefSeq; WP_011738985.1; NC_008611.1.
DR   AlphaFoldDB; A0PLZ1; -.
DR   SMR; A0PLZ1; -.
DR   STRING; 362242.MUL_0706; -.
DR   EnsemblBacteria; ABL03360; ABL03360; MUL_0706.
DR   KEGG; mul:MUL_0706; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; NDTWEIT; -.
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..313
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_0706"
FT                   /id="PRO_0000361253"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  34639 MW;  2764DB72981FDAE2 CRC64;
     MARTEDDSWE ITESVGATAL GVASARAAET RSQHPLISDP FAQVFLDAVG DGVWNWHSAP
     QLPAELLEIE PDLPLQMEAM VSYMASRTAF FDEFFLDATR AGIGQAVILA AGLDSRAWRL
     PWPAGTTVFE LDQPRVLEFK AATLAEHGAE PACGRVAVAV DLRQDWPTAL RQAGFDPSVS
     SVWSAEGLMP YLPAVAQDLL FERVQGLTVR ASRIAVEALG PKFLDPQVRA NRSARIERIR
     AVMAHVEPQR EIPRTDELWY FEEREDVGDW FRRHDWDVTV TPSGELMAGY GRAAAAQVED
     RVPTNLFVAA QRN