ID   Y2961_MYCUA             Reviewed;         302 AA.
AC   A0PSA4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_2961;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_2961;
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; ABL05223.1; -; Genomic_DNA.
DR   RefSeq; WP_011740835.1; NC_008611.1.
DR   AlphaFoldDB; A0PSA4; -.
DR   SMR; A0PSA4; -.
DR   STRING; 362242.MUL_2961; -.
DR   EnsemblBacteria; ABL05223; ABL05223; MUL_2961.
DR   KEGG; mul:MUL_2961; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; GSAASMW; -.
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..302
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_2961"
FT                   /id="PRO_0000361246"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  32913 MW;  B33D92D5925B69BF CRC64;
     MTTSEYGSRR SDDDQWDIVS GVGYTALLVA GWRALDTVGP QPLAPDEYAK YFIAASGDAY
     LNDQLAHPPT SVDETAFPRL YGVQTRFFDD FFRSAAAGTK QAVIVAAGLD SRAYRLEWPS
     GTTVFEIDLA QVLEFKARVL QRHGVEPKAR RNAVAADLRT DWPATLHAAG FEPGQPSAWS
     VEGLLPYLTA DAQDALFARI DDLCAPGSRI ATGALGSRLD HDQLVALEQT HPGVNLFGDV
     NFSALTYDDK TNPAQWLAAR GWVVEPVRNT LELEAGYGMT PPAVDVRLDA IMHSEYIVAT
     KP