ID   A0A166TH53_9PEZI        Unreviewed;       403 AA.
AC   A0A166TH53;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Vacuolar protease a {ECO:0000313|EMBL:KZL72073.1};
DE   Flags: Fragment;
GN   ORFNames=CI238_00879 {ECO:0000313|EMBL:KZL72073.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL72073.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL72073.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL72073.1,
RC   ECO:0000313|Proteomes:UP000076584};
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:KZL72073.1}.
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DR   EMBL; LFIW01002391; KZL72073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166TH53; -.
DR   STRING; 1573173.A0A166TH53; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05488; Proteinase_A_fungi; 1.
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   InterPro; IPR033819; Saccharopepsin.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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:KZL72073.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..403
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007880120"
FT   DOMAIN          89..399
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        120..125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL72073.1"
SQ   SEQUENCE   403 AA;  43901 MW;  B8046D0ACC3B9216 CRC64;
     LTATMKSTLL TAAVLLGAAQ AEVHKLKLKK VPLEEQLNSV PIEHQVRQLG QKYMGARPDN
     HADAMFNQKP VQSNGEHPVP VSNFMNAQYF SEIEIGTPPQ TFKVVLDTGS SNLWVPSQQC
     GSIACYLHSK YDSSASSTYK SNGSSFEIHY GSGSLTGFVS QDDVSIGDLK IKKQDFAEAT
     SEPGLAFAFG RFDGILGLGY DTISVNKIVP PFYNLVNQKA IDEPVFAFYL GDTNEEGDES
     EATFGGLDDS HYEGKITYIP LRRKAYWEVD LDAISLGDET AELEGHGAIL DTGTSLNVLP
     SALAELLNKE IGAKKGYNGQ YSVECSKRDE LPDITFTLAG YNFSISAYDY VLEVSGSCIS
     TFQGMDFPEP VGPLVILGDA FLRRWYSVYD LGKNAVGLAK AKK
//