ID   Y289_MYCBO              Reviewed;         302 AA.
AC   Q7U2D4; A0A1R3XVY9; X2BEG3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb0289;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BQ2027_MB0289;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT98813.1; -; Genomic_DNA.
DR   RefSeq; NP_853953.1; NC_002945.3.
DR   RefSeq; WP_003401448.1; NC_002945.4.
DR   AlphaFoldDB; Q7U2D4; -.
DR   SMR; Q7U2D4; -.
DR   PATRIC; fig|233413.5.peg.317; -.
DR   OMA; NEQCAPA; -.
DR   Proteomes; UP000001419; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..302
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Mb0289"
FT                   /id="PRO_0000361134"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  32998 MW;  E61B7CC197AE2782 CRC64;
     MRTEGDSWDI TTSVGSTALF VATARALEAQ KSDPLVVDPY AEAFCRAVGG SWADVLDGKL
     PDHKLKSTDF GEHFVNFQGA RTKYFDEYFR RAAAAGARQV VILAAGLDSR AYRLPWPDGT
     TVFELDRPQV LDFKREVLAS HGAQPRALRR EIAVDLRDDW PQALRDSGFD AAAPSAWIAE
     GLLIYLPATA QERLFTGIDA LAGRRSHVAV EDGAPMGPDE YAAKVEEERA AIAEGAEEHP
     FFQLVYNERC APAAEWFGER GWTAVATLLN DYLEAVGRPV PGPESEAGPM FARNTLVSAA
     RV