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
//