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Database: UniProt
Entry: A0A135UQW9_9PEZI
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ID   A0A135UQW9_9PEZI        Unreviewed;       478 AA.
AC   A0A135UQW9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Endothiapepsin {ECO:0000313|EMBL:KXH62795.1};
GN   ORFNames=CSAL01_02700 {ECO:0000313|EMBL:KXH62795.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH62795.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH62795.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH62795.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH62795.1}.
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DR   EMBL; JFFI01001150; KXH62795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135UQW9; -.
DR   STRING; 1209931.A0A135UQW9; -.
DR   OrthoDB; 2900143at2759; -.
DR   Proteomes; UP000070121; 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; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 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; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT   DOMAIN          158..474
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          91..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        398..437
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   478 AA;  49515 MW;  6FC9663271DF63C1 CRC64;
     MRFTKPAAVA AFIPFASHLV DAAPRKIEIS TLGGAAFRIE QAPNPDFYYG NRRGPIALAR
     AYSKFGQQIP DDLLGLIDQI LGELGLLNGG KGKSGRKGGK GGGKGKGKGG KGGNAGAGGS
     KGNGTTTAPG GGGNKGNGTK TPPGGEVAAI PAEFDSQYLC PVQIGIPPQT IPLNFDTGSS
     DLWVFSSETP ITQVAGQALY NINASTSAKV LQGASWSISY GDGSSSQGNV YMDTVTIGGV
     TVESQAVESA TQVSSSFSRN KNQSGLVGLA FGNINTVQPT KQKTFFENAM TNLAMPLFTA
     NLKKAAAGNY NFGFLDSTEY TGDITFVPAN TTQGFWQFTA QGFAVGSNGS APTSAPHAAI
     ADTGTTLMLL PDAIVSAYYQ RIASAKYDAT NGGFVFNCKD QIPSFTVDMG TYQAVVPGDF
     MKFAPVDGQT IETSTTCFGG IQSSAALPFA IYGDVFLKSQ FVVFHGGNKE LGFANKPL
//
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