(data stored in ACNUC8465 zone)

SWISSPROT: B6HE88_PENRW

ID   B6HE88_PENRW            Unreviewed;       195 AA.
AC   B6HE88;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   30-AUG-2017, entry version 56.
DE   RecName: Full=D-tyrosyl-tRNA(Tyr) deacylase {ECO:0000256|RuleBase:RU003470};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU003470};
GN   ORFNames=Pc20g04800 {ECO:0000313|EMBL:CAP85809.1}, PCH_Pc20g04800
GN   {ECO:0000313|EMBL:CAP85809.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85809.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85809.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free
CC       tRNA(Tyr). Could be a defense mechanism against a harmful effect
CC       of D-tyrosine. {ECO:0000256|RuleBase:RU003470}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003470}.
CC   -!- SIMILARITY: Belongs to the DTD family.
CC       {ECO:0000256|RuleBase:RU003470}.
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DR   EMBL; AM920435; CAP85809.1; -; Genomic_DNA.
DR   RefSeq; XP_002563021.1; XM_002562975.1.
DR   STRING; 500485.XP_002563021.1; -.
DR   EnsemblFungi; CAP85809; CAP85809; PCH_Pc20g04800.
DR   GeneID; 8314577; -.
DR   KEGG; pcs:Pc20g04800; -.
DR   eggNOG; KOG3323; Eukaryota.
DR   eggNOG; COG1490; LUCA.
DR   HOGENOM; HOG000113981; -.
DR   KO; K07560; -.
DR   OMA; DGPVTIW; -.
DR   OrthoDB; EOG092C54JK; -.
DR   BioCyc; PCHR:PC20G04800-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR   Gene3D; 3.50.80.10; -; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_dom.
DR   PANTHER; PTHR10472; PTHR10472; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; SSF69500; 1.
DR   TIGRFAMs; TIGR00256; TIGR00256; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HE88.
DR   SWISS-2DPAGE; B6HE88.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Hydrolase {ECO:0000256|RuleBase:RU003470};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
SQ   SEQUENCE   195 AA;  21806 MW;  7C9570A1554EE6DD CRC64;
     MKLVIQRVKS ASVTVDSELI SSIGKGLLVF AGVGKEDTEK DAENLVNKVL KAKFWPDENG
     VQWKKNVKDI EGEVLCVSQF TLYAKMKKGN KPDFHDAAAP EPARKLYDFF YAKMGEGYTP
     DRVKNGVFQA MMDVELKNDG PVGVNYCSED AAVTIEINTN LPKKEPKEQQ NGDKKTDEQE
     IKGSFEFQIP PELLQ
//

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