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
//