ID   Y1059_MYCMM             Reviewed;         324 AA.
AC   B2HCU5;
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_1059;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_1059;
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; ACC39517.1; -; Genomic_DNA.
DR   RefSeq; WP_012392957.1; NC_010612.1.
DR   AlphaFoldDB; B2HCU5; -.
DR   SMR; B2HCU5; -.
DR   STRING; 216594.MMAR_1059; -.
DR   PRIDE; B2HCU5; -.
DR   EnsemblBacteria; ACC39517; ACC39517; MMAR_1059.
DR   KEGG; mmi:MMAR_1059; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; RMADNMA; -.
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..324
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_1059"
FT                   /id="PRO_0000361162"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35047 MW;  C385F0D03D9B44C5 CRC64;
     MTSTGSTRYD GDSWDLASSV GVTATMVAAA RAMATRAENP LINDPYAEPL VRAVGVDLLT
     RLATGEFNVA DLDDDPQRPL GPLGDVADNM AVRTRFFDDF FLDATRAGLE QVVILASGLD
     ARAYRLPWPP QTVVYEIDLP QVIEFKSRTL ADLGAAPTAD RRVVAVDLRE DWPAALRAAG
     FDPNQPTAWS AEGLLGYLPP EAQDRLLDTV TELSAPGSRL AAECLSSVDP GEEEQIKERM
     QEVSARWRAH GFDVDMVGLV YFGDRNEAVP YLSDRGWLLT STPLPELRAA NGLAPAAVDD
     DGPSVDMLYV SGTLYTTPRP DPAP