ID   Y4570_MYCMM             Reviewed;         307 AA.
AC   B2HEF0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_4570;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_4570;
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; ACC42975.1; -; Genomic_DNA.
DR   RefSeq; WP_012396118.1; NC_010612.1.
DR   AlphaFoldDB; B2HEF0; -.
DR   SMR; B2HEF0; -.
DR   STRING; 216594.MMAR_4570; -.
DR   EnsemblBacteria; ACC42975; ACC42975; MMAR_4570.
DR   KEGG; mmi:MMAR_4570; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TYPGEHT; -.
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..307
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_4570"
FT                   /id="PRO_0000361171"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  32549 MW;  D9AFC519893C78E0 CRC64;
     MARTEGDSWD LANSVGATAT MVAAARAAAT RRSRPIIADP FAEPLVRAVG LDLFTRAASG
     EVDLDEVAAG LGFARMVDTF AARALFFDKF FADAIAAGLR QVVIVASGLD ARPYRLPWPT
     GMRVYEIDQP EVIEFKTTTL ARLGASPTAD HHPVGIDLRD DWPSALRAAG FDAARPTAWL
     AEGVLIGFLP PEAETRLLDN VIELSAVGSR LAADYGTING SSAESQQLAQ QMTEGWRAHG
     LDMDIAGLTY PGEHTDVAAY LRSHGWETAT ADHGDVVLAA GLAELTAADR QSPASTIGFV
     TAVRSTD