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Database: UniProt
Entry: I2JZN6_DEKBR
LinkDB: I2JZN6_DEKBR
Original site: I2JZN6_DEKBR 
ID   I2JZN6_DEKBR            Unreviewed;       352 AA.
AC   I2JZN6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   25-OCT-2017, entry version 14.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EIF48438.1};
GN   ORFNames=AWRI1499_1568 {ECO:0000313|EMBL:EIF48438.1};
OS   Brettanomyces bruxellensis AWRI1499.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF48438.1, ECO:0000313|Proteomes:UP000004997};
RN   [1] {ECO:0000313|EMBL:EIF48438.1, ECO:0000313|Proteomes:UP000004997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF48438.1,
RC   ECO:0000313|Proteomes:UP000004997};
RX   PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA   Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT   "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of
RT   the Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL   PLoS ONE 7:E33840-E33840(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIF48438.1}.
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DR   EMBL; AHIQ01000089; EIF48438.1; -; Genomic_DNA.
DR   MEROPS; M18.A01; -.
DR   EnsemblFungi; EIF48438; EIF48438; AWRI1499_1568.
DR   Proteomes; UP000004997; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EIF48438.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004997};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
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:UP000004997};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   UNSURE       80     80       E or Q. {ECO:0000313|EMBL:EIF48438.1}.
FT   UNSURE       81     81       D or N. {ECO:0000313|EMBL:EIF48438.1}.
SQ   SEQUENCE   352 AA;  39789 MW;  D6A94CAC9F8FEC6C CRC64;
     MVEEFWHTWF DRDLSLAGRV FIRNSTTGNY EYKLLKIDRP ILRIPTLAIH LDKERGKFEF
     NKETQLRPVL GTDSEXLSSE DAEENDKNFE VIKSVIQRHN KKLVKVISEE LXVKPEDIXD
     FELVLFDTQK SCLGGLENEF IFSPRLDNQV TCYSAIQGLI QSTENLQXET GIRLVSLFDH
     EEIGSQSAQG ADSSFLPDIL HRLTSLTFNP TSDLSSQLSP DHFFNSMSKS FVISSDMAHA
     VHPNYSENYE ALNRPKLNAG PVFKINANQR YVTNSPGIVL MKXIASIGKV PMQLFVIRND
     SPCGSTIGPM IAAKLGIRTL DIGNPQLSMH SIRETCGSKD IEQLXNLFRT YF
//
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