ID   Y4402_MYCUA             Reviewed;         314 AA.
AC   A0PVM7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_4402;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_4402;
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; ABL06396.1; -; Genomic_DNA.
DR   RefSeq; WP_011741997.1; NC_008611.1.
DR   AlphaFoldDB; A0PVM7; -.
DR   SMR; A0PVM7; -.
DR   STRING; 362242.MUL_4402; -.
DR   EnsemblBacteria; ABL06396; ABL06396; MUL_4402.
DR   KEGG; mul:MUL_4402; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DSMPPTL; -.
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..314
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_4402"
FT                   /id="PRO_0000361247"
FT   REGION          291..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   314 AA;  34424 MW;  C406988258995264 CRC64;
     MPRTDNDSWT ITESVGATAL GVAAARAAET ESENPLIEDP FARVFVDAAG DGMWSMFANP
     ALLAGAPEIE SQVGARVRQM IDFMATRTAF FDEFFLGAAD AGVRQVVILA SGLDSRAWRL
     PWPDGTVVYE LDQPRVLEFK SATLRQHGAR PTAQLMNIPI DLRQDWPAAL LDSGFDASKP
     TAWSAEGLVR YLPARAQDLL FERIDTLSPA GSWLATNVPQ GGFLDPDLVR RQHEEMQRMR
     AAAGRLVEIQ MPAVEDLWYA EERTPVADWL GEHGWRASAT TSAELLTRYG RPVPDDAEGP
     VPPTLFVSAH RPAA