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Database: UniProt
Entry: A0A0D1ZE83_9EURO
LinkDB: A0A0D1ZE83_9EURO
Original site: A0A0D1ZE83_9EURO 
ID   A0A0D1ZE83_9EURO        Unreviewed;       527 AA.
AC   A0A0D1ZE83;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   10-MAY-2017, entry version 13.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KIV85113.1};
GN   ORFNames=PV11_00848 {ECO:0000313|EMBL:KIV85113.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV85113.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV85113.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV85113.1,
RC   ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
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; KN846951; KIV85113.1; -; Genomic_DNA.
DR   EnsemblFungi; KIV85113; KIV85113; PV11_00848.
DR   Proteomes; UP000053599; 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:KIV85113.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053599};
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:UP000053599};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   527 AA;  57818 MW;  AD8153F43F8B2DEF CRC64;
     MPLRLVVSGL PRTRLYSTMA PVNIKVAAND FLDFVNASPT PYHAVKSIKE RLTGVGFKEI
     KEKDSWSSRC LPGGKYFLTR NASTIVAFAI GKKWKPGNPI SMIGAHTDSP CLRIKPVSKK
     QGDGFIQVGV ETYGGGLWHT WFDRDLGVAG RVMVRDTDGN VVQKLVHINK PILRIPTLAV
     HLDRQETFSF NKETQLFPIA GLVAAELKRQ DEKKSKTANE EEEDETRKPF SPLKAITTRH
     HPHIVELIAS NAGVSAEEVV DFEIVLYDTQ KACLGGLTDE FIFSARLDNL NQTYCATMGL
     INSLESPSAL DDESSIRLIA CFDHEEIGSM TAQGAFSMML PAIIRRLSVL PSASFVENDS
     EDSYDHASDP DVSTAYEQTL ASSFLVSADM AHSVNPNYGA KYESDHKPEM NQGPVIKINA
     NARYATNSPG IVLLQEVARK AAKIIDSDPE GVPLQLFVVR NDSSCGSTIG PMLSAHLGAR
     TLDLGNPQLS MHSCRETGGA DDVHHAIRLF SSFFQHYSAL EKTILVD
//
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