ID   Y4850_MYCMM             Reviewed;         301 AA.
AC   B2HGZ9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_4850;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_4850;
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; ACC43254.1; -; Genomic_DNA.
DR   RefSeq; WP_012396384.1; NC_010612.1.
DR   AlphaFoldDB; B2HGZ9; -.
DR   SMR; B2HGZ9; -.
DR   STRING; 216594.MMAR_4850; -.
DR   EnsemblBacteria; ACC43254; ACC43254; MMAR_4850.
DR   KEGG; mmi:MMAR_4850; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TRFYDQF; -.
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_4850"
FT                   /id="PRO_0000361172"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33097 MW;  32BBC9372F8F59D0 CRC64;
     MVRTDRDRWD LATSVGATAT MVAAQRALAA DPQYALIDDP YAAPLVRAVG IDVYTRLVNG
     QIPVDVESGF DPARMAEAMA CRTRFYDQFF VEATRSGISQ VVILASGLDA RAYRLDWPAG
     TVVYEVDMPE VIEFKTLTLA DLGAEPTAER RTVAVDLRDD WAAALQAAGF DKDVPSAWSA
     EGLLVYLPDD AQDALFDNIT ALSATGSRLA FEFVPDTAVF NDERWRSHHA RMSELGFEID
     FNDLVYHGQR SHVIDHLARD GWQSASHTAK ELHAANGFDY PDDDIAAVFA DITYTSAVLG
     R