ID   Y358_MYCMM              Reviewed;         311 AA.
AC   B2HLS6;
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_0358;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_0358;
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; ACC38825.1; -; Genomic_DNA.
DR   RefSeq; WP_012392340.1; NC_010612.1.
DR   AlphaFoldDB; B2HLS6; -.
DR   SMR; B2HLS6; -.
DR   STRING; 216594.MMAR_0358; -.
DR   EnsemblBacteria; ACC38825; ACC38825; MMAR_0358.
DR   GeneID; 64259123; -.
DR   KEGG; mmi:MMAR_0358; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DLWFDDE; -.
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..311
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_0358"
FT                   /id="PRO_0000361170"
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   311 AA;  34107 MW;  3717D511378895FF CRC64;
     MPRTADDSWD IATSVGATAV MVALARAAET ASETPLIRDQ FAEPLVSTPE LAAVREQVAA
     WWAQTDDDDD PDFTVDSQQM TDYLAVRTHF FDSYFIDAVA AGIRQVVILA AGLDSRAYRL
     DWPGGTTVYE IDLPKVLDYK EHTLARHGAA PVAALRAVPV DLRHDWPQAL RDAGFQTSLP
     TAWLAEGLLP FLPAAAQHAL FTAIDANSAT GSRVAVEMFG VDEDARRAAE ERAQRWARQR
     AKRQARGQDT SFDPFDLWFD DEGQPDPADW FAAHGWTTDS VQAGAEALRL GRTAHSQEGP
     FVNRFVTAGK P