ID   A0A0F4ZH60_9PEZI        Unreviewed;       474 AA.
AC   A0A0F4ZH60;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE   Flags: Fragment;
GN   ORFNames=TD95_005147 {ECO:0000313|EMBL:KKA29949.1};
OS   Thielaviopsis punctulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX   NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29949.1, ECO:0000313|Proteomes:UP000033483};
RN   [1] {ECO:0000313|EMBL:KKA29949.1, ECO:0000313|Proteomes:UP000033483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29949.1};
RA   Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA29949.1}.
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DR   EMBL; LAEV01000627; KKA29949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4ZH60; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000033483; 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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033483}.
FT   DOMAIN          74..388
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          409..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        322..353
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKA29949.1"
FT   NON_TER         474
FT                   /evidence="ECO:0000313|EMBL:KKA29949.1"
SQ   SEQUENCE   474 AA;  50757 MW;  F6CF6AC0C13F0B0B CRC64;
     AFAPHVIGAP PANNQPVPVP VALVSSPSAG SQLSSKPVSY NLSRKSVQVP SNRVLRRRSD
     DIDVSVYNFS AVSYNMALEI GTPAQEVRVI IDTGSSELWV NPNCEKAQSV PQKQQCLGSG
     HYNASDSSTS KTSALQSQIQ YGIGAVAIRY VSDHISLPGS DIAVEDVIFG QAIDSHDMNQ
     GIMGLSFGNG YNLGYSTFVD ELVRQNVSHI HGFGMALGSK EEEHGGVLTF GGVDTKKFSG
     RLHTEPIIAP TNDHDLYRYW VRLGSVGVTT DQGSRTFPNS SAVVFFDSGA TLSYLPRRVV
     NNMVSALDAK FDSTWGLYRT SCNANATIDF EFGDFVIQVP LSEFLWDMGI GACFLGVEAS
     DDVFLLGDSF LRSVYAVYDM DTPAIHFAQY VNCGSNARMI PAGANKTADF EGECKPQDSN
     TQGSSNSSNS DNSNSLNSQT SQGSDRNTDS GADRPIQSAL MAAVVAVGVV SILF
//