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Database: UniProt
Entry: A3LQF5_PICST
LinkDB: A3LQF5_PICST
Original site: A3LQF5_PICST 
ID   A3LQF5_PICST            Unreviewed;       489 AA.
AC   A3LQF5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   07-JUN-2017, entry version 68.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ABN64672.2};
DE            EC=3.4.11.21 {ECO:0000313|EMBL:ABN64672.2};
GN   Name=DNP1 {ECO:0000313|EMBL:ABN64672.2};
GN   ORFNames=PICST_75911 {ECO:0000313|EMBL:ABN64672.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64672.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN64672.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP000496; ABN64672.2; -; Genomic_DNA.
DR   RefSeq; XP_001382701.2; XM_001382664.1.
DR   ProteinModelPortal; A3LQF5; -.
DR   STRING; 322104.XP_001382701.2; -.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; ABN64672; ABN64672; PICST_75911.
DR   GeneID; 4837340; -.
DR   KEGG; pic:PICST_75911; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; A3LQF5; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ABN64672.2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002258};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ABN64672.2};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   489 AA;  54224 MW;  CB4D3E43C09C5E3B CRC64;
     MSTERPLKYA QNFVDFVNAS PTPYHAVNSV KSHLVEAGFT ELSERANWNS KLEKGGKYFV
     TRNGSSLVGF TVGEQFKNGN GIAIVGAHTD SPCLRIKPIS KKTSEGFIQV GVEQYGGLIA
     HSWFDRDLSI AGRVYVQEND EFVPKLIKID KPLLRIPTLA IHLNREVNTK FEFNKETKLV
     PIAGQVALDK NEIASKKAEK KAHSCADDPD LQLTPEQFES VQNVISRHNQ SLIELIAKEV
     NVSPSQIEDF ELLLFDHQKS TIGGLNDEFI FSPRLDNLTS CFTATVGLIE STEFLANQKS
     ISLISLFDHE EIGSVSAQGA DSTFLPDIIQ RLTKTDFGGS SNRDYFHETM AKSFLLSSDM
     AHGVHPNYGE AYEAQNRPQV NLGPVIKINA NQRYATNSPG IVLLKKVADK ANVPLQLFVV
     RNDSPCGSTI GPILSAKLGI RTLDLGNPQL SMHSIRETGG TFDVVRLSDL FKSFFEHYYE
     LDDKIKCDL
//
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