ID A0A0F9Y0K1_TRIHA Unreviewed; 391 AA.
AC A0A0F9Y0K1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=THAR02_02329 {ECO:0000313|EMBL:KKP05603.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP05603.1, 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:KKP05603.1}.
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DR EMBL; JOKZ01000045; KKP05603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9Y0K1; -.
DR OMA; GTYGIPC; -.
DR OrthoDB; 2670782at2759; -.
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; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
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..391
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002530091"
FT DOMAIN 57..385
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 391 AA; 41467 MW; 490D195F55B412AC CRC64;
MRGALSAILL AMTLLPTGAL SQSGNSRFPA ILPLKARVRQ AESYQRRKRQ TPNISEPLSN
WHSGTDLQAS LGTVVFDTGS SDVVIPSTQC DANPGCTGLQ RRFAPEKSET FTSLNGSFRI
SYSTGTGVAA AGNVEIEGVI SRDVVAVAGL QVQDFQFGLI TNQSAALGVD PFDGIVGMGF
PSGLTTGPHT FLGGVYGSGQ IPQAVYGLYL TPQSVGNAEI SLGGVDSSKL VSEINYIPVF
PATGQFNGTF EKVYVDNTIT DVSFNYAIYD SGTANIVAPK NDAEEIYAMI SPDIKPVDTV
GTYGIPCSKL KDIKSSISFS IGGRNYTIPS QELSVGPISD QPGICQTLIN SSGDDQAKSL
WVIGGSLLKY YYTVWDIENV RFGLAQTLHS P
//
