ID   Y1069_MYCMM             Reviewed;         316 AA.
AC   B2HCV3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1069;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_1069;
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; ACC39525.1; -; Genomic_DNA.
DR   RefSeq; WP_012392964.1; NC_010612.1.
DR   AlphaFoldDB; B2HCV3; -.
DR   SMR; B2HCV3; -.
DR   STRING; 216594.MMAR_1069; -.
DR   EnsemblBacteria; ACC39525; ACC39525; MMAR_1069.
DR   KEGG; mmi:MMAR_1069; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; NAFNWEE; -.
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..316
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_1069"
FT                   /id="PRO_0000361164"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  34269 MW;  408A76BCCA6A583D CRC64;
     MSSARFDGDT WDLASSVGLT ATMVAAARAV AARDPEGAGA VATDRFAEPL VRAVGVDFFT
     RMATGELDAA ELDEETAIGM RHFGAAMAIR TRFFDDFFLD ATASGIRQAV ILASGLDSRA
     YRLPWPAGTT LFEVDQPKVI DFKIATLSEL GAQPTADRRA VAVDLREDWP AALRQAGFDP
     TERTAWIAEG LLGYLPAEAQ DRLLDQIAAQ SAAGSRFATE GLPDVNDVKQ EELRRRMQRQ
     NERWNRHGFD LDMAALVYFD DRTDAGTYLA AQGWQVTSAS NSELFTQHGL QPLNGDDAPF
     GEVLYLSAVK DTAAAA