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Database: UniProt
Entry: A0A117E4L6_ASPNG
LinkDB: A0A117E4L6_ASPNG
Original site: A0A117E4L6_ASPNG 
ID   A0A117E4L6_ASPNG        Unreviewed;       426 AA.
AC   A0A117E4L6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Aspartic endopeptidase {ECO:0000313|EMBL:GAQ47301.1};
GN   ORFNames=ABL_09962 {ECO:0000313|EMBL:GAQ47301.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ47301.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAQ47301.1}.
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DR   EMBL; BCMY01000027; GAQ47301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117E4L6; -.
DR   PaxDb; 5061-CADANGAP00000033; -.
DR   VEuPathDB; FungiDB:An01g00370; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1116628; -.
DR   VEuPathDB; FungiDB:ATCC64974_23160; -.
DR   VEuPathDB; FungiDB:M747DRAFT_296174; -.
DR   OMA; WYGGVQS; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
FT   DOMAIN          90..414
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   426 AA;  46685 MW;  2C55F76BC868B183 CRC64;
     MATKIKLIPN LNYKRSGTKS YVHLIRKYRF HPTKPGPYTL SSSIQQTGRP YTDKPIGGRA
     HIRQLVRKKS TTSDEVGEVP AEDVQNDSMY LATVGIGTPA QNLKLDFDTG SADLWVWSNK
     LPSTLLSENK THAIFDSSKS STFKTLEGES WQISYGDGSS ASGSVGTDDV NIGGVVVKNQ
     AVELAEKMST TFAQGEGDGL LGLAFSNINT VQPTSVKTPV ENMILQDDIP KSAELFTAKL
     DTWRDTDDES FYTFGFIDQD LVKTAGEEVY YTPVDNSQGF WLFNSTSATV NGKTINRSGN
     TAIADTGTTL ALVDDDTCEA IYSAIDGAYY DQEVQGWIYP TDTAQDKLPT VSFAVGEKQF
     VVQKEDLAFS EAKTGYVYGG IQSRGDMTMD ILGDTFLKSI YAIFDVGNLR FGAVQREELR
     QSLKSE
//
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