ID   Y1058_MYCMM             Reviewed;         300 AA.
AC   B2HCU4;
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_1058;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_1058;
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; ACC39516.1; -; Genomic_DNA.
DR   RefSeq; WP_012392956.1; NC_010612.1.
DR   AlphaFoldDB; B2HCU4; -.
DR   SMR; B2HCU4; -.
DR   STRING; 216594.MMAR_1058; -.
DR   PRIDE; B2HCU4; -.
DR   EnsemblBacteria; ACC39516; ACC39516; MMAR_1058.
DR   KEGG; mmi:MMAR_1058; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TEHVPDP; -.
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..300
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_1058"
FT                   /id="PRO_0000361161"
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   300 AA;  33312 MW;  309F88DCE0168236 CRC64;
     MNRRTDADSW DPASSVGATA TMVAASRARA SRGPDALLDD RLAEPLVRAV GLQPLVRMID
     GDTAVDDPPS SPRSLNEQIA VRTRYFDDFF TAAGAGGIRQ AVILASGLDT RAYRLNWPSG
     MTVYEIDQPQ VIEFKTRTLA EFGALPCPDH RPIGIDLRED WPSALRQRGF DAGQPTAWIA
     EGLLVYLPPE AQDRLFDNIA ELSTPGSQVA TEHFPDPNGF SGPRAQRLSE RWRRMGLDLD
     MAELIYHGDR NTVIDYLADH GWRVRARTFE EMHAHNGFEP PDDEMMALFG GMSYVTGIRK