ID   Y1068_MYCMM             Reviewed;         302 AA.
AC   B2HCV2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1068;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_1068;
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; ACC39524.1; -; Genomic_DNA.
DR   RefSeq; WP_012392963.1; NC_010612.1.
DR   AlphaFoldDB; B2HCV2; -.
DR   SMR; B2HCV2; -.
DR   STRING; 216594.MMAR_1068; -.
DR   EnsemblBacteria; ACC39524; ACC39524; MMAR_1068.
DR   KEGG; mmi:MMAR_1068; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; QDSWDLA; -.
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..302
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_1068"
FT                   /id="PRO_0000361163"
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   302 AA;  33243 MW;  7D037CD7FFC01DB8 CRC64;
     MTRTDQDSWD LASSVGATAT MVAAARALAS AEANPIIDDP FAAPLVRAVG LDFFTRLAEG
     EIDHDEQAQR DRQLVADSIA VRTRFFDDFF LDAARRGVRQ SVILAAGLDA RAYRLPWPSG
     SVVYEVDQPD VIDFKDTTMS ALGAVPTATR RTVRVDLRDD WPAALRHNGF DTTQPTAWSA
     EGLLMYLPPD AQDRLFDAIS GLSAPGSRLA TEYHPDPGST MAERAQQFNQ RWVRLGCDID
     LSGLFYEGER SNVVDYLTEH GWHVAARPRQ DLFTDYGRVF PDADTSQLRS IVAVTATFGE
     AG