ID   A0SZ74_TRIHA            Unreviewed;       454 AA.
AC   A0SZ74;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   22-FEB-2023, entry version 51.
DE   SubName: Full=Aspartyl proteinase {ECO:0000313|EMBL:ABK64118.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:ABK64118.1};
RN   [1] {ECO:0000313|EMBL:ABK64118.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yang Q., Liu Y.;
RT   "The RACE amplifying and sequence analyzing of aspartyl proteinase gene of
RT   Trichoderma harzianum.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF063643; ABK64118.1; -; mRNA.
DR   AlphaFoldDB; A0SZ74; -.
DR   MEROPS; A01.080; -.
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:SF1; ASPARTYL PROTEINASE; 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   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}.
FT   DOMAIN          114..439
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   454 AA;  49188 MW;  A641CA441B69039A CRC64;
     MEAIFQAQAK FRLDRGLHKI TAIRNKNYKR HGTKSYVYLL NRFGFEPTKP GPYFQEHRVH
     QRGLVHPDYN APVGGRVHIT KALHKKKNHH GALDANGSEK GEVGAEDQQN DSEYLCEVTI
     GTPGQKLLLD FDTGSSDLWV FSTELSKSLQ KNHTIFNPSE SSTFKKLSGQ TWQISYGDGS
     SASGDCGSDN VTVGGLTIKN QTVELASKLA AQFAQGTGDG LLGLAWPSIN TVATNGRSTP
     ANTPVANMIT QDDVPSNAEL FTAAFYSERD ANAESFYTFG YIDQDLVTAS GQDIAWTDVD
     NSQGFWMFPS TSSSVNGQAI SQSGNSAIAD TGTTLALVSD EVCDALYKAI PGATYDDQQQ
     GYVFPMSTDV SSLPEFKVSV GDTQFVIQPE DLAFAPADDN NWYGGVQSRG SNPFDILGDV
     FLKSVYAIFD QGNQRFGAVP KIQATQNLNS SSAQ
//