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Database: UniProt
Entry: A0A0G2DUE8_9EURO
LinkDB: A0A0G2DUE8_9EURO
Original site: A0A0G2DUE8_9EURO 
ID   A0A0G2DUE8_9EURO        Unreviewed;       493 AA.
AC   A0A0G2DUE8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   10-MAY-2017, entry version 10.
DE   SubName: Full=Putative aspartyl aminopeptidase {ECO:0000313|EMBL:KKY14284.1};
GN   ORFNames=UCRPC4_g06817 {ECO:0000313|EMBL:KKY14284.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales;
OC   Phaeomoniellales incertae sedis; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY14284.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY14284.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY14284.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell
RT   wall degradation and secondary metabolism in the genomes of grapevine
RT   trunk pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY14284.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY14284.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY14284.1}.
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DR   EMBL; LCWF01000233; KKY14284.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY14284; KKY14284; UCRPC4_g06817.
DR   Proteomes; UP000053317; 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:KKY14284.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053317};
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:UP000053317};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   493 AA;  53970 MW;  E982D356F2B9DDA8 CRC64;
     MSRIIQTAAA EGFLEYVNAS PTPFHAEKEP WSSTCKPGGK YVLTRNGSTI VAFAVGKKWR
     PGNPVSMIGA HTDSPTLRLK PVSKKEGSGF LQVGVETYGG GLWHTWFDRD LGLAGRVMVK
     DGKGSIIQKL VHINKPILRI PTLAIHFERQ EKFEFNKQDQ LFPIAGLIAA ELKRQDEIKA
     TNGNKETTTP TSTEDFAPLK AVTQRHHSHI VELIAKDADA SPDDVVDFEV ILFDTQKSCL
     GGLQDEFIFS ARLDNLNSTY CATIGMIESV SDPAALEEDS TIRLIACFDN EEIGSTTTQG
     ADSHMLPAII RRLSVLPSSH FEDGESEKSY DKTVEADVST AFEQTLASSF LVSADMAHSV
     NPNYAGKYEP DHRPEMNKGP VIKINANARY TTNSPGIALI QEVAKKAAPL TKDDERGVPL
     QLFVIRNDSL CGSTIGPMIS AKLGVRALDL GNPQLSMHSI RETGGTEDVG YAIRLFKSFF
     QHYGALEKTI FVD
//
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