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Database: UniProt
Entry: A0A100ITK2_ASPNG
LinkDB: A0A100ITK2_ASPNG
Original site: A0A100ITK2_ASPNG 
ID   A0A100ITK2_ASPNG        Unreviewed;       451 AA.
AC   A0A100ITK2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=PEPAc {ECO:0000313|EMBL:GAQ47067.1};
GN   ORFNames=ABL_09728 {ECO:0000313|EMBL:GAQ47067.1};
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:GAQ47067.1, 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, ECO:0000256|RuleBase:RU000454}.
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:GAQ47067.1}.
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DR   EMBL; BCMY01000024; GAQ47067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100ITK2; -.
DR   PaxDb; 5061-CADANGAP00009589; -.
DR   VEuPathDB; FungiDB:An12g03300; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1118349; -.
DR   VEuPathDB; FungiDB:ATCC64974_41680; -.
DR   VEuPathDB; FungiDB:M747DRAFT_266360; -.
DR   OMA; YTINIDA; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..451
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007087733"
FT   DOMAIN          99..440
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   451 AA;  47931 MW;  F88764A9D498392A CRC64;
     MYIPIGTLAT ASLLAGAALA APTPSPLKAR NIVRRSGSHT IYKPTPFTAP SQHKAASKYL
     ELSKTKSKGN VNPRSAAYVT RSTSSGSSTL ISLFEGEEFA TAITIGGDSF DVIVDTGSSD
     TWVVKTGFTC IDLDTGRETS ESSCDFGSTW TVESSFVEIE GEEFAIEYGD GEYLYGVMGN
     ETVTLADITV DQTIGVVTEA AWEGDGTTSG LTGLAYPALT SAYSTKTDEQ VVYSNIITTM
     WEEGLIEPYF SLAIERDVSG AAGYLALGGL PPVDFVEDFT NTSILVTNIE GYSKAYDFYT
     INIDAVTLNG KSLTSAGGDD IQYIVDSGTT LNYLPTSISQ EINAAFSPAA TYSDDEGAYI
     VDCDATPPTH GITINGKTFY INPLDMILDA GTDDEGNAVC ITGIVDGGSD TSEDLYILGD
     TFQKNVVTVF DIGATELRFA ARENYTSNDT Y
//
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