Y747_MYCBO
ID Y747_MYCBO Reviewed; 367 AA.
AC Q7U1E6; A0A1R3XW74; X2BFT7;
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 Mb0747c;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB0747C;
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; SIT99346.1; -; Genomic_DNA.
DR RefSeq; NP_854405.1; NC_002945.3.
DR RefSeq; WP_003403691.1; NC_002945.4.
DR AlphaFoldDB; Q7U1E6; -.
DR SMR; Q7U1E6; -.
DR EnsemblBacteria; SIT99346; SIT99346; BQ2027_MB0747C.
DR GeneID; 45424691; -.
DR PATRIC; fig|233413.5.peg.814; -.
DR OMA; RMADNMA; -.
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..367
FT /note="Putative S-adenosyl-L-methionine-dependent
FT methyltransferase Mb0747c"
FT /id="PRO_0000361138"
FT REGION 348..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 40876 MW; 5FF038903881804A CRC64;
MTYTGSIRCE GDTWDLASSV GATATMVAAA RAMATRAANP LINDQFAEPL VRAVGVDVLT
RLASGELTAS DIDDPERPNA SMVRMAEHHA VRTKFFDEFF MDATRAGIRQ VVILASGLDS
RAYRLAWPAQ TVVYEIDQPQ VMEFKTRTLA ELGATPTADR RVVTADLRAD WPTALGAAGF
DPTQPTAWSA EGLLRYLPPE AQDRLLDNVT ALSVPDSRFA TESIRNFKPH HEERMRERMT
ILANRWRAYG FDLDMNELVY FGDRNEPASY LSDNGWLLTE IKSQDLLTAN GFQPFEDEEV
PLPDFFYVSA RLQRKHRQYP AHRKPAPSWR HTACPVNELS KSAAYTMTRS DAHQASTTAP
PPPGLTG
