ID A0A0F9XR78_TRIHA Unreviewed; 454 AA.
AC A0A0F9XR78;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KKP06980.1};
GN ORFNames=THAR02_00859 {ECO:0000313|EMBL:KKP06980.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP06980.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP06980.1}.
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DR EMBL; JOKZ01000014; KKP06980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9XR78; -.
DR OMA; WYGGVQS; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000034112; 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: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 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KKP06980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112}.
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; 49246 MW; 0460453561CF2693 CRC64;
MEAIFQAQAK FRLDRGLHKI TAIRNKNYKR HGTKSYVYLL NRFGFEPTKP GPYFQEHRVH
QRGLVHPDYN APVGGRVHIT KALHKKKNHH GALDANGTEK GEVGAEDQQN DSEYLCEVTI
GTPGQKLLLD FDTGSSDLWV FSTELSKSLQ KNHTIFNPSE SSTFKKLSGQ TWQISYGDGS
SASGDCGSDN VTIGGLTIKN QTVELASKLA AQFAQGTGDG LLGLAWPSIN TVTTNGRSTP
ANTPVANMIT QDDVPSNAEL FTAAFYSERD ANAESFYTFG YIDQDLVTAS GQDIAWTDVD
NSQGFWMFPS TSSSVNGQAI SQSGNSAIAD TGTTLALVSD EVCDALYKAI PGATYDDQQQ
GYVFPMSTDV SSLPEFKVSV GDTQFVIQPE DLAFAPADDN NWYGGVQSRG SNPFDILGDV
FLKSVYAIFD QGNQRFGAVP KIQATQNLNS SSAQ
//
