ID   ASE1_ACRSP              Reviewed;          40 AA.
AC   P85156;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Subtilisin-like serine protease AS-E1;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Acremonium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium;
OC   unclassified Acremonium.
OX   NCBI_TaxID=2046025;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=F11177 {ECO:0000269|PubMed:17482570};
RX   PubMed=17482570; DOI=10.1016/j.bbrc.2007.04.133;
RA   Liu C., Matsushita Y., Shimizu K., Makimura K., Hasumi K.;
RT   "Activation of prothrombin by two subtilisin-like serine proteases from
RT   Acremonium sp.";
RL   Biochem. Biophys. Res. Commun. 358:356-362(2007).
CC   -!- FUNCTION: Subtilisin-like serine protease. Cleaves prothrombin at 155-
CC       Arg-|-Ser-156, 45-Thr-|-Ala-46 and 316-Tyr-|-Ile-317 to produces
CC       meizothrombin(desF1)-like molecules. Degrades fibinogen. Inhibits
CC       plasma coagulation. {ECO:0000269|PubMed:17482570}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by antipain and PMSF. Inhibited
CC       by benzamidine and aprotinin by 80% and 17% respectively. Little or no
CC       inhibition by EDTA, E-64, iodoacetic acid, leupeptin and FUT-175.
CC       {ECO:0000269|PubMed:17482570}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Retains over 50% of its activity after treatment
CC         for 20 min between pH 7.0 and 11.0. Inactivated by treatment at pH
CC         13.0 and at pH values less than 5.0. {ECO:0000269|PubMed:17482570};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. Stable from 25 to 40
CC         degrees Celsius. Activity is reduced considerably by incubation above
CC         40 degrees Celsius for 20 min. {ECO:0000269|PubMed:17482570};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17482570}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85156; -.
DR   SMR; P85156; -.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Prothrombin activator;
KW   Serine protease.
FT   CHAIN           1..>40
FT                   /note="Subtilisin-like serine protease AS-E1"
FT                   /id="PRO_0000291532"
FT   DOMAIN          4..>40
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        36
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P06873,
FT                   ECO:0000255|PROSITE-ProRule:PRU10080, ECO:0000255|PROSITE-
FT                   ProRule:PRU10081, ECO:0000255|PROSITE-ProRule:PRU10082"
FT   NON_TER         40
FT                   /evidence="ECO:0000303|PubMed:17482570"
SQ   SEQUENCE   40 AA;  4327 MW;  44303FB0C2344919 CRC64;
     DNVPWGLARI SHRTTGATSY VYDDSAGEGT CSYIIDTGIY