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
//