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Database: UniProt
Entry: A0A0M8N2L7_9HYPO
LinkDB: A0A0M8N2L7_9HYPO
Original site: A0A0M8N2L7_9HYPO 
ID   A0A0M8N2L7_9HYPO        Unreviewed;       501 AA.
AC   A0A0M8N2L7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   12-APR-2017, entry version 8.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KOS19304.1};
GN   ORFNames=ESCO_000160 {ECO:0000313|EMBL:KOS19304.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS19304.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS19304.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease
RT   agent of ant agriculture.";
RL   Submitted (JUL-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:KOS19304.1}.
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DR   EMBL; LGSR01000020; KOS19304.1; -; Genomic_DNA.
DR   EnsemblFungi; KOS19304; KOS19304; ESCO_000160.
DR   Proteomes; UP000053831; 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:KOS19304.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053831};
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:UP000053831};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   501 AA;  54082 MW;  E0F6F9C9312DA350 CRC64;
     MAPPQAALDF VDFVNASPTP YHAVQSASVR LEKAGFQLIR ERDSWAATLQ PGGKYYLTRN
     GSSIVAFAIG RRWRPGNPVA IVGAHTDSPC LRVKPVSSKR NVGYLQVGVE TYGGGIWHSW
     FDRDLSLAGR VLVRDGAGAV VQRLVKVDKP LLRIPTLAIH LHRNDNFDPN KETELFPIVG
     LAAAELNKGS GGESKGQESE GGGAEPKEDF QPLQKMEVRH HPAVLDVVAE HAGVQVADIV
     DFELVLYDTQ KSCVGGLHDE FIFSPRLDNL NMTYCSIEGL IASVHRADAL HDDATIRMTV
     CFDHEEIGSQ SAQGAHSNLL PSVLRRLSVL PGNRDAASDG SYVAVASPAA HEGEDATAYE
     QTLARSFLVS ADMAHAVHPN YAHKYEPSHQ PAINGGVVVK VNANQRYATN SPGIVLLQEC
     ARQAGVPLQL FVVRNDSPCG STIGPGLAAR LGMRTLDLGN PQLSMHSIRE TGGTADVGSA
     VKLFDQFFES YGRIEPRILV D
//
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