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Y3826_MYCBP
ID   Y3826_MYCBP             Reviewed;         314 AA.
AC   A1KQ98;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_3826c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_3826c;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL73816.1; -; Genomic_DNA.
DR   RefSeq; WP_003420557.1; NC_008769.1.
DR   AlphaFoldDB; A1KQ98; -.
DR   SMR; A1KQ98; -.
DR   KEGG; mbb:BCG_3826c; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DSMPPTL; -.
DR   Proteomes; UP000001472; 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..314
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_3826c"
FT                   /id="PRO_0000361147"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34755 MW;  BACD884305460F6E CRC64;
     MPRTDNDSWA ITESVGATAL GVAAARAAET ESDNPLINDP FARIFVDAAG DGIWSMYTNR
     TLLAGATDLD PDLRAPIQQM IDFMAARTAF FDEYFLATAD AGVRQVVILA SGLDSRAWRL
     PWPDGTVVYE LDQPKVLEFK SATLRQHGAQ PASQLVNVPI DLRQDWPKAL QKAGFDPSKP
     CAWLAEGLVR YLPARAQDLL FERIDALSRP GSWLASNVPG AGFLDPERMR RQRADMRRMR
     AAAAKLVETE ISDVDDLWYA EQRTAVAEWL RERGWDVSTA TLPELLARYG RSIPHSGEDS
     IPPNLFVSAQ RATS
 
 
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