Y746_MYCBO
ID Y746_MYCBO Reviewed; 301 AA.
AC Q7U1E7; A0A1R3XWM4; X2BFZ0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb0746c;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB0746C;
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; SIT99345.1; -; Genomic_DNA.
DR RefSeq; NP_854404.1; NC_002945.3.
DR RefSeq; WP_003403687.1; NC_002945.4.
DR AlphaFoldDB; Q7U1E7; -.
DR SMR; Q7U1E7; -.
DR EnsemblBacteria; SIT99345; SIT99345; BQ2027_MB0746C.
DR PATRIC; fig|233413.5.peg.813; -.
DR OMA; FFIKMMD; -.
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..301
FT /note="Putative S-adenosyl-L-methionine-dependent
FT methyltransferase Mb0746c"
FT /id="PRO_0000361137"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 159..160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 32247 MW; EE44495196D2A279 CRC64;
MPRAHDDNWD LASSVGATAT MVAAGRALAT KDPRGLINDP FAEPLVRAVG LDFFTKLIDG
ELDIATTGNL SPGRAQAMID GIAVRTKYFD DYFRTATDGG VRQVVILAAG LDARAYRLPW
PAGTVVYEID QPQVIDFKTT TLAGIGAKPT AIRRTVYIDL RADWPAALQA AGLDSTAPTA
WLAEGMLIYL PPDPRTGCST TAPNSVLRAA RSLPNLSRAL WISTQAGYEK WRIRFASTAW
TSTWRRWCIP ANAATSSTTC APRAGTLRAQ CGPTYSGAMV CPFPPHTTTI RSAKSSSSAV
V