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Database: UniProt
Entry: A0A0F8B272_CERFI
LinkDB: A0A0F8B272_CERFI
Original site: A0A0F8B272_CERFI 
ID   A0A0F8B272_CERFI        Unreviewed;       401 AA.
AC   A0A0F8B272;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   SubName: Full=Gastricsin {ECO:0000313|EMBL:KKF95441.1};
DE            EC=3.4.23.3 {ECO:0000313|EMBL:KKF95441.1};
GN   Name=Pgc {ECO:0000313|EMBL:KKF95441.1};
GN   ORFNames=CFO_g2206 {ECO:0000313|EMBL:KKF95441.1};
OS   Ceratocystis fimbriata f. sp. platani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF95441.1, ECO:0000313|Proteomes:UP000034841};
RN   [1] {ECO:0000313|EMBL:KKF95441.1, ECO:0000313|Proteomes:UP000034841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFO {ECO:0000313|EMBL:KKF95441.1,
RC   ECO:0000313|Proteomes:UP000034841};
RA   Belbahri L.;
RT   "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT   trees.";
RL   Submitted (APR-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:KKF95441.1}.
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DR   EMBL; LBBL01000095; KKF95441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8B272; -.
DR   Proteomes; UP000034841; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF68; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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   Hydrolase {ECO:0000313|EMBL:KKF95441.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..401
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002527481"
FT   DOMAIN          34..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        307..345
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   401 AA;  43409 MW;  3D0C411D15651F90 CRC64;
     MHHSLSSILA ASAMVGVGSA AVLNLPIIRD DGYNLVDVQI GSPPTTHRLR FDTGSATTWV
     VDQVCGNGGC AIHSSSQRPY SPYDASASTS HVATGVYSEI QYLGGKTTGF TYHDNFDVDG
     TVWQQSFMAA NSSSWTQMPA DGFLGLAFST IADGQTTTLV ETLLWDGKLD KPRFGIFYND
     MGNLNSNNGG VLTIGDSCES TYGKDVVATI PTQLSGGELQ LWRVDVYAMT GTYKGWVSNA
     VAEGSNVNTD PIPVPVSQRL PLVAGSYTVF DTGGSAASVP TSMLVPLYRS INMDWESIKS
     GAHIPLCSEF TSDWHVEFEF ANGQNVTIYG DQLALPGFAN RDDACWPPFD DSGANEQFFL
     FGPRFLRNFY TTFDFGSDKP ENYAPTVSFA PLKDEYKSKF V
//
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