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Database: UniProt
Entry: A0A135TL96_9PEZI
LinkDB: A0A135TL96_9PEZI
Original site: A0A135TL96_9PEZI 
ID   A0A135TL96_9PEZI        Unreviewed;       399 AA.
AC   A0A135TL96;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KXH48877.1};
GN   ORFNames=CSAL01_09006 {ECO:0000313|EMBL:KXH48877.1};
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:KXH48877.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH48877.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH48877.1,
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:KXH48877.1}.
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DR   EMBL; JFFI01001940; KXH48877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135TL96; -.
DR   STRING; 1209931.A0A135TL96; -.
DR   OrthoDB; 615305at2759; -.
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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF51; NAPSIN-A; 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, ECO:0000313|EMBL:KXH48877.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..399
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007803801"
FT   DOMAIN          85..395
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        116..121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   399 AA;  43570 MW;  7CA90E52B72DC973 CRC64;
     MKSTLLTAAV LLGAAQAEVH KLKLKKVPIE EQLNSVPIEH QVRQLGQKYM GARPDSHADA
     MFNQKPFTST GEHPVPVSNF MNAQYFSEIE IGTPPQTFKV VLDTGSSNLW VPSQQCGSIA
     CYLHSKYDSS SSSTYKSNGS EFEIHYGSGS LTGFVSQDDV SIGDLKIKKQ DFAEATSEPG
     LAFAFGRFDG ILGLGYDTIS VNKIVPPFYN LVNQKAIDEP VFAFYLGDTN EEGDESEATF
     GGIDDSHYEG KITYIPLRRK AYWEVDLDAI TLGDETADLE GHGAILDTGT SLNVLPSALA
     ELLNKEIGAK KGYNGQYSVE CSKRDELPDI TFTLSGYNFS ISAYDYVLEV SGSCISTFQG
     MDFPEPVGPL VILGDAFLRR WYSVYDLGKN AVGLAKAKK
//
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