Y1931_MYCBO
ID Y1931_MYCBO Reviewed; 303 AA.
AC Q7TZC0; A0A1R3Y1S6; X2BJ91;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb1931c;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB1931C;
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; SIU00534.1; -; Genomic_DNA.
DR RefSeq; NP_855582.1; NC_002945.3.
DR RefSeq; WP_003409526.1; NC_002945.4.
DR AlphaFoldDB; Q7TZC0; -.
DR SMR; Q7TZC0; -.
DR EnsemblBacteria; SIU00534; SIU00534; BQ2027_MB1931C.
DR PATRIC; fig|233413.5.peg.2118; -.
DR OMA; GSAASMW; -.
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..303
FT /note="Putative S-adenosyl-L-methionine-dependent
FT methyltransferase Mb1931c"
FT /id="PRO_0000361133"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 33267 MW; 7480EB8065C70DA8 CRC64;
MTTPEYGSLR SDDDHWDIVS NVGYTALLVA GWRALHTTGP KPLVQDEYAK HFITASADPY
LEGLLANPRT SEDGTAFPRL YGVQTRFFDD FFNCADEAGI RQAVIVAAGL DCRAYRLDWQ
PGTTVFEIDV PKVLEFKARV LSERGAVPKA HRVAVPADLR TDWPTPLTAA GFDPQRPSAW
SVEGLLPYLT GDAQYALFAR IDELCAPGSR VALGALGSRL DHEQLAALET AHPGVNMSGD
VNFSALTYDD KTDPVEWLVE HGWAVDPVRS TLELQVGYGL TPPDVDVKID SFMRSQYITA
VRA