Y853_MYCBO
ID Y853_MYCBO Reviewed; 301 AA.
AC Q7U163; A0A1R3XYN1; X2BG66;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb0853;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB0853;
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; SIT99452.1; -; Genomic_DNA.
DR RefSeq; NP_854511.1; NC_002945.3.
DR RefSeq; WP_003404349.1; NC_002945.4.
DR AlphaFoldDB; Q7U163; -.
DR SMR; Q7U163; -.
DR EnsemblBacteria; SIT99452; SIT99452; BQ2027_MB0853.
DR GeneID; 45424793; -.
DR PATRIC; fig|233413.5.peg.926; -.
DR OMA; TRFYDQF; -.
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 Mb0853"
FT /id="PRO_0000361140"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 156..157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 33416 MW; 5F6C68208D1E6199 CRC64;
MVRADRDRWD LATSVGATAT MVAAQRALAA DPRYALIDDP YAAPLVRAVG MDVYTRLVDW
QIPVEGDSEF DPQRMATGMA CRTRFFDQFF LDATHSGIGQ FVILASGLDA RAYRLAWPVG
SIVYEVDMPE VIEFKTATLS DLGAEPATER RTVAVDLRDD WATALQTAGF DPKVPAAWSA
EGLLVYLPVE AQDALFDNIT ALSAPGSRLA FEFVPDTAIF ADERWRNYHN RMSELGFDID
LNELVYHGQR GHVLDYLTRD GWQTSALTVT QLYEANGFAY PDDELATAFA DLTYSSATLM
R