ID   Y150_MYCBO              Reviewed;         311 AA.
AC   Q7U2R3; A0A1R3XUM9; X2BE73;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb0150;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BQ2027_MB0150;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIT98586.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIT98586.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q7U2R3; -.
DR   SMR; Q7U2R3; -.
DR   PATRIC; fig|233413.5.peg.171; -.
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..311
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Mb0150"
FT                   /id="PRO_0000361130"
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   311 AA;  33709 MW;  BD0ACB7D30CF10CD CRC64;
     MSSLPSSRRT AGDTWAITES VGATALGVAA ARAVETAATN PLIRDEFAKV LVSSAGTAWA
     RLADADLAWL DGDQLGRRVH RVACDYQAVR THFFDEYFGA AVDAGVRQVV ILAAGLDARA
     YRLNWPAGTV VYEIDQPSVL EYKAGILQSH GAVPTARRHA VAVDLRDDWP AALIAAGFDG
     TQPTAWLAEG LLPYLPGDAA DRLFDMVTAL SAPGSQVAVE AFTMNTKGNT QRWNRMRERL
     GLDIDVQALT YHEPDRSDAA QWLATHGWQV HSVSNREEMA RLGRAIPQDL VDETVRTTLL
     RGRLVTPAQP A