ID   Y1057_MYCMM             Reviewed;         304 AA.
AC   B2HCU3;
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_1057;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_1057;
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; ACC39515.1; -; Genomic_DNA.
DR   RefSeq; WP_012392955.1; NC_010612.1.
DR   AlphaFoldDB; B2HCU3; -.
DR   SMR; B2HCU3; -.
DR   STRING; 216594.MMAR_1057; -.
DR   EnsemblBacteria; ACC39515; ACC39515; MMAR_1057.
DR   KEGG; mmi:MMAR_1057; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; FFIKMMD; -.
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..304
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_1057"
FT                   /id="PRO_0000361160"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  32951 MW;  D386CD62AF02F60F CRC64;
     MARTHDDKWD LASSVGATAT MVAAGRAMAS RDPRGLIDDP FAEPLVRAVG VDFFIKMMDG
     EFDLSVLQNV SSAKAQAMVD GMAVRTKYFD DYFGDAIKSG IRQAVILASG LDARAYRLPW
     PADTVVYELD QPQVIEFKTN VLADLGAEPR ATRRAIPIDL RGDWPVALRA AGLDTTAPTA
     WLAEGLLIYL PPEAQDRLFD NITALSAPGS TVATEFVPGI VDFDVDRARQ MSGPFRDHGL
     DIDMSSLVYT GARNHVVDYL RAKGWDAEGV TRSELFERNG MAVPAPSDDD PLGEIIFISA
     ALTG