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
//