ID   A0A166PZW6_9PEZI        Unreviewed;       570 AA.
AC   A0A166PZW6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KZL67362.1};
GN   ORFNames=CT0861_12459 {ECO:0000313|EMBL:KZL67362.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL67362.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL67362.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL67362.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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:KZL67362.1}.
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DR   EMBL; LFIV01000147; KZL67362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166PZW6; -.
DR   STRING; 708197.A0A166PZW6; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000076552; 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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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; 1.
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:KZL67362.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   DOMAIN          64..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          106..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        320..358
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   570 AA;  58890 MW;  FAA0F68E54D67437 CRC64;
     MKSGVFVAVA GGVVNSVTAL SLPRTTTEGK GYIAMPVRQV RPDLGHLTKR EAIEVVLKNR
     EFYYSTDIII GTPGQQVTVL LDTGSSELWV NPDCSTAPSA AQAKQCSAAG QYNPRNSRTP
     PTGPIGTRRL NYGDPSDPNT QTSAEIAYYS DSITMGGGVL SNQTFGIVTK SDGIATGIMG
     LAPDLKAGFE HGKPYSLILN SLAEQGVIGS RIFSLDLRHA SADSGALIYG GVDRGKFIGE
     LLRVPMVNGA KGEPRLAVEL TGIGMNIANS AKTYALAPED KNVMLDSGTT LTRLHPSIAR
     PILADLKATT DSDGYWTAAC SLRNSGSDSY VTFTFGRKTI RVPLSDFILD LGPRDGQCYI
     GLVTTNDQQI LGDSMMRAGY FVFDWDNQVI HMAQASTCGK DEIVAVGKGS DAVPSGVVGL
     CDGPAAPDGD GNPTTSAVSP PASSTPYTPT VSPTGDTVTI TKTVDNGPAP TPTYVTLSGC
     IALTLCPQSS STNGASPPSS SPAGESQNGG SSPAPSKNTG VSAPTAASTG GPSSSTSSDS
     HSAASSLVDE RFLGLLLGSL MTLAAAFWNI
//