ID   S0EHZ2_GIBF5            Unreviewed;       413 AA.
AC   S0EHZ2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Probable endothiapepsin {ECO:0000313|EMBL:CCT74409.1};
GN   ORFNames=FFUJ_10458 {ECO:0000313|EMBL:CCT74409.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT74409.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; HF679032; CCT74409.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EHZ2; -.
DR   STRING; 1279085.S0EHZ2; -.
DR   EnsemblFungi; CCT74409; CCT74409; FFUJ_10458.
DR   VEuPathDB; FungiDB:FFUJ_10458; -.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   OrthoDB; 2900143at2759; -.
DR   Proteomes; UP000016800; Chromosome 10.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..413
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004485281"
FT   DOMAIN          87..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   413 AA;  43991 MW;  828D623ACE2E71F1 CRC64;
     MKFSSVLTSG LASFTLVAGL PTVTSPSEHS VQQVRNPVYK RNGIAALDKI YRKYHIDLPE
     YLESSLLARR DSTGTVANKP IENNAEWLTP VQIGNPPRTF QMDLDTGSSD LWVYGSKVAT
     AGGSSNRYNA SNSKTCEEMA GAKWTIEYGD GSGASGHVVK DTVSIGGLSV EAQAVQVADK
     VHESFAQQEE LDGLLGLGFR SINTVTPKKQ KTFFDNAKTE HGAGVFTADL KHDAPGTYTF
     GVINKTAYEG DITYTTVNPS TGMWTFTSTG YAVGKGNVTK TPITAIADTG TSLMFLPEAV
     NKAYYAQIDG AKIDATAGGY VFPCDTKMPD FTFYVGETGI TVPGAYMNFA PLEGPVPGGK
     EGKREVGTCY GGLQSSAGDI NIFGDIALKA AFVVFDTEKT RIGFAKKTLV GVE
//