ID   Y5323_MYCMM             Reviewed;         314 AA.
AC   B2HLJ5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_5323;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_5323;
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; ACC43727.1; -; Genomic_DNA.
DR   RefSeq; WP_012396828.1; NC_010612.1.
DR   AlphaFoldDB; B2HLJ5; -.
DR   SMR; B2HLJ5; -.
DR   STRING; 216594.MMAR_5323; -.
DR   EnsemblBacteria; ACC43727; ACC43727; MMAR_5323.
DR   KEGG; mmi:MMAR_5323; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DSMPPTL; -.
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..314
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_5323"
FT                   /id="PRO_0000361173"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34468 MW;  6401ECD71220CF76 CRC64;
     MPRTDNDSWT ITESVGATAL GVAAARAAET ESENPLIEDP FARVFVDAAG DGMWSMFANP
     ALLAGAPEIE SQVGARVRQM IDFMATRTAF FDEFFLGAAD TGVRQVVILA SGLDSRAWRL
     PWPDGTVVYE LDQPRVLEFK SATLRQHGAR PTAQLVNIPI DLRQDWPAAL LDSGFDASKP
     TAWSAEGLVR YLPARAQDLL FERIDTLSPA GSWLATNVPQ EGFSDPDLVR RQHEEMQRMR
     AAAGRLVEIQ MPAVEDLWYA EERTPVADWL GEHGWRASAT TSAELLTRYG RPVPDDAEGP
     VPPTLFVSAH RPAA