ID   Y539_MYCMM              Reviewed;         301 AA.
AC   B2HNW1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_0539;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_0539;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC39003.1; -; Genomic_DNA.
DR   RefSeq; WP_012392506.1; NC_010612.1.
DR   AlphaFoldDB; B2HNW1; -.
DR   SMR; B2HNW1; -.
DR   STRING; 216594.MMAR_0539; -.
DR   EnsemblBacteria; ACC39003; ACC39003; MMAR_0539.
DR   KEGG; mmi:MMAR_0539; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; NEQCAPA; -.
DR   OrthoDB; 847145at2; -.
DR   Proteomes; UP000001190; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..301
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_0539"
FT                   /id="PRO_0000361174"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  32802 MW;  381EE36D661D25DF CRC64;
     MRSEGDSWDI TTSVGSTALF VATARALEAL KPDPLAVDPY AELFCRAVGG SWADVLDGNA
     ADHELQSDDF GKHFVNFQGA RTKYFDAYFR RAVEAGVRQV VVLAAGLDSR AYRLSWPDGT
     TIFELDRPQV LDFKREVLGG HGVRPRTERR EIAVDLRDDW PQALRDSGFD AEAPSAWIAE
     GLLIYLPAAA QEQLFTGIDS LACLGSHVAV EDGAPLPDAE FAAKLEEERA AVAAGGERPF
     FQLLYNERCA PAADWFSEHG WTALGTPLNN YLREVGRPVP GPGSEVAAMF ARNTLMSATK
     P