ID   Y4761_MYCUA             Reviewed;         311 AA.
AC   A0PWG2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_4761;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_4761;
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABL06681.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000325; ABL06681.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; A0PWG2; -.
DR   SMR; A0PWG2; -.
DR   STRING; 362242.MUL_4761; -.
DR   EnsemblBacteria; ABL06681; ABL06681; MUL_4761.
DR   KEGG; mul:MUL_4761; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
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..311
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_4761"
FT                   /id="PRO_0000361250"
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   311 AA;  34129 MW;  2D3F9B361FD0F2E6 CRC64;
     MPRTADDSWD IATSVGATAV MVALARAAET ASETPLIRDQ FAEPLVSTPE LAAVREQVAA
     WWAQTDDDDD PDFTVDSQQM TDYLAVRTHF FDSYFIDAVA AGIRQVVILA AGLDSRAYRL
     DWPGGTMVYE IDLPKVLDYK EHTLARHGAA PVAALRAVPV DLRHDWPQAL RDAGFQTSLP
     TAWLAEGLLP FLPAAAQHAL FTAIDANSAT GSRVAVEMFG VDEDARRAAE ERAQRWARQR
     AKRQARGQDT SFDPFDLWFD DEGQPDPADW FAAHGWTTDS VQVGAEALRL GRTATSQEGP
     FVNRFVTAGK P