ID   Y3816_MYCBO             Reviewed;         308 AA.
AC   Q7TVN7; A0A1R3Y6R3; X2BPK3;
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 Mb3816c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BQ2027_MB3816C;
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; SIU02445.1; -; Genomic_DNA.
DR   RefSeq; NP_857453.1; NC_002945.3.
DR   RefSeq; WP_003420620.1; NC_002945.4.
DR   AlphaFoldDB; Q7TVN7; -.
DR   SMR; Q7TVN7; -.
DR   EnsemblBacteria; SIU02445; SIU02445; BQ2027_MB3816C.
DR   PATRIC; fig|233413.5.peg.4173; -.
DR   OMA; RMAMETF; -.
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..308
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Mb3816c"
FT                   /id="PRO_0000361136"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  33390 MW;  5865CF059D44E304 CRC64;
     MARTDDDSWD LATGVGATAT LVAAGRARAA RAAQPLIDDP FAEPLVRAVG VEFLTRWATG
     ELDAADVDDP DAAWGLQRMT TELVVRTRYF DQFFLDAAAA GVRQAVILAS GLDARGYRLP
     WPADTTVFEV DQPRVLEFKA QTLAGLGAQP TADLRMVPAD LRHDWPDALR RGGFDAAEPA
     AWIAEGLFGY LPPDAQNRLL DHVTDLSAPG SRLALEAFLG SADRDSARVE EMIRTATRGW
     REHGFHLDIW ALNYAGPRHE VSGYLDNHGW RSVGTTTAQL LAAHDLPAAP ALPAGLADRP
     NYWTCVLG