ID   Y4763_MYCUA             Reviewed;         310 AA.
AC   A0PWG4;
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_4763;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_4763;
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; ABL06683.1; -; Genomic_DNA.
DR   RefSeq; WP_011742275.1; NC_008611.1.
DR   AlphaFoldDB; A0PWG4; -.
DR   SMR; A0PWG4; -.
DR   STRING; 362242.MUL_4763; -.
DR   EnsemblBacteria; ABL06683; ABL06683; MUL_4763.
DR   KEGG; mul:MUL_4763; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; QAVRTHY; -.
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_4763"
FT                   /id="PRO_0000361252"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..167
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34214 MW;  4A55904A417FCA94 CRC64;
     MTELDEVDSL RSDGDSWTVT ESVGATALGV AAARAVETAG ANPLIRDEFA PILVSSAGPA
     WARLADPDIG WLDDDPHGQR LHRLGCDYQA VRTHFSDEYF AAAAGAGIEQ AVILAAGLDC
     RAYRLNWPPE AVVFEIDQPK VLEYKAQILE SHGVTAAATR HGVAVDLRED WPAALLRAGF
     DRDRPTAWLA EGLLPYLPGD AQDRLFEMIT DLSAPRSRIA VESFTMNLTG NKQRWNRMRD
     RLGLDINVEA LTYREPGRTD AAEWLANHGW QVYSVSNREE MARLGRPVPE DLVDEAITTT
     LLRASLEILR