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Database: UniProt
Entry: A0A0D2CBE9_9EURO
LinkDB: A0A0D2CBE9_9EURO
Original site: A0A0D2CBE9_9EURO 
ID   A0A0D2CBE9_9EURO        Unreviewed;       529 AA.
AC   A0A0D2CBE9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   07-JUN-2017, entry version 13.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KIW47212.1};
GN   ORFNames=PV06_02804 {ECO:0000313|EMBL:KIW47212.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47212.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW47212.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47212.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KN847333; KIW47212.1; -; Genomic_DNA.
DR   RefSeq; XP_016267428.1; XM_016403531.1.
DR   EnsemblFungi; KIW47212; KIW47212; PV06_02804.
DR   GeneID; 27354878; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:KIW47212.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053342};
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:UP000053342};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   529 AA;  58037 MW;  3EBC67D3183EDA0C CRC64;
     MFLRLFLRGP STIKSYSTMT RAHIKVAAND FLDFVNASPT PFHAVKSVKE RLSKVGFKEI
     KEKESWSSTC QPGGKYFLTR NGSTVVAFAI GKKWKPGNPI SMIGAHTDSP CLRIKPVSKK
     QGDGFIQVGV ETYGGGLWHT WFDRDLGIAG RAMVRGRDGN VVQKLVRVDR PILRVPTLAV
     HLDRQETFNF NKETQLFPIA GLVAAELKRQ DDKKGQGKVE NNDQEEYGQS KPFTPLKAIT
     TRHHSHIVEL IAADAGVSPE DVVDFEVVLY DTQKACLGGL SEEFIFSARL DNLNQTYCAT
     MGLINSVESA SALDDESSIR LIACFDHEEI GSMTAQGAFS TMLPAIIRRI SVLPSSSFVD
     GSEQSYDHAV DPDVSTAYEQ TLSSSFLLSA DMAHSVNPNY GAKYEPDHKP EMNQGPVIKI
     NANARYATNS PGIVLLQEVA RKAPKIIDSD AEGVPLQLFV VRNDSSCGST IGPMLSAHLG
     TRTLDLGNPQ LSMHSCRETG GADDVHHAIR LFSSFFQHYS SLEKSILVD
//
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