ID   Y817_MYCUA              Reviewed;         300 AA.
AC   A0PM88;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_0817;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_0817;
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; ABL03457.1; -; Genomic_DNA.
DR   RefSeq; WP_011739082.1; NC_008611.1.
DR   AlphaFoldDB; A0PM88; -.
DR   SMR; A0PM88; -.
DR   STRING; 362242.MUL_0817; -.
DR   EnsemblBacteria; ABL03457; ABL03457; MUL_0817.
DR   KEGG; mul:MUL_0817; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TEHVPDP; -.
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..300
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_0817"
FT                   /id="PRO_0000361255"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33338 MW;  AE4FB2150F6C8387 CRC64;
     MNRRTDADSW DPASSVGATA TMVAASRARA SRGPDALLDD RLAGPLVRAV GLQPLVRMID
     GDTAVDDPPS SPRSLNEQIA VRTRYFDDFF TAAGAGGIRQ AVILASGLDT RAYRLNWPSG
     MTVYEIDQPQ VIEFKTRTLA EFGALPCPDH RPIGIDLRED WPSALRQRGF DAGQPTAWIA
     EGLLVYLPPE AQDRLFDNIA ELSTPRSQVA TEHFPDPNGF SGPRAQRLSE RWHRMGMDLD
     MAELIYHGDR NTVIDYLADH GWRVRARTFE EMHAHNGFEP PDDEMMALFG GMSYVTGIRK