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Database: UniProt
Entry: A0A0F9WYS6_TRIHA
LinkDB: A0A0F9WYS6_TRIHA
Original site: A0A0F9WYS6_TRIHA 
ID   A0A0F9WYS6_TRIHA        Unreviewed;       475 AA.
AC   A0A0F9WYS6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Candidapepsin-3 {ECO:0000313|EMBL:KKO97564.1};
GN   ORFNames=THAR02_10335 {ECO:0000313|EMBL:KKO97564.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKO97564.1, 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}.
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:KKO97564.1}.
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DR   EMBL; JOKZ01000542; KKO97564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9WYS6; -.
DR   OrthoDB; 2322499at2759; -.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..475
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002529616"
FT   DOMAIN          69..395
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   475 AA;  50632 MW;  F468977BBBF0F78C CRC64;
     MHFSLLMALA TLASPFRGVA ALSMQLTGRE MPAVFSLPVD YRPVSQAKLH KRSPSSTVQA
     DTMLYDITPF VKLSVGTPPQ LIGMAVDLQN AFIAFLVPNT TDCVPQSSAT SAQYNCATDD
     YCVTMGYFCP ASSSTMKSIQ PSKSDPEGPV NADVVTVGSQ RVDGVHMWLN DISPGAYSRM
     GIAPGSPFLY LMVDQGFINS PSFSLWSYGI PNNQGQLLFG GVNKAMYKGT LQAFPLSGLN
     NNVNMPIAAI VVESGGNSTA GPTTTRHNLA DSTTAVLSTI DIFTFLPNKT VQQIYADLHI
     TPTFIPSFNA SMGIVDCART QSENRTVSLV FGNATISVPW SELFIPFEDD ICEFTIVPYR
     PDLTYGPGSE LQIGATVLQY MYLAVDYDNM FAAVAPLNPN PGPDNILEIG NGTRIPDADG
     DFPATITPYG APTLTTTTTG SPPTSTTASK AQAVTFIPRA MDIILGVSGA ILAVF
//
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