ID   Y3534_MYCMM             Reviewed;         310 AA.
AC   B2HK09;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_3534;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_3534;
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; ACC41951.1; -; Genomic_DNA.
DR   RefSeq; WP_012395162.1; NC_010612.1.
DR   AlphaFoldDB; B2HK09; -.
DR   SMR; B2HK09; -.
DR   STRING; 216594.MMAR_3534; -.
DR   EnsemblBacteria; ACC41951; ACC41951; MMAR_3534.
DR   KEGG; mmi:MMAR_3534; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DFFTRWV; -.
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..310
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_3534"
FT                   /id="PRO_0000361167"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  33604 MW;  B991533C4DEBBA5C CRC64;
     MPRTDNDSWD LATSVGATAT MVAAARAIAT NADNPLIADR FAEPLVRAVG VDFFTRWVTG
     DLVVADVDDT ESGWQLAQMP DAMAVRTRFF DAFFQDATRA GVRQAVILAS GLDARAYRLD
     WPAGMTVFEI DQPEVIAFKT TTLAGLGAVP RADLRTVAVD LRQDWPKALT DAGFDAGSPT
     AWIAEGLFGY LPPEAQDRLL DNITALSAAG SRLACEAIPN RPQQDAEKAR ELMRKATARW
     REHGFELEFG DLGYEGDRAD VALYLQDLGW QSVGTQMGQL LADNGAAPIP HNDDSVTMAD
     TIYYSSVLTA