ID   ASE2_ACRSP              Reviewed;          18 AA.
AC   P85157;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Subtilisin-like serine protease AS-E2;
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 151-
CC       Ala-|-Met-152, 271-Arg-|-Thr-272 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, PMSF and
CC       aprotinin. Inhibited by benzamidine by 49%. Little or no inhibition by
CC       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. {ECO:0000269|PubMed:17482570};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:17482570};
CC   -!- SUBUNIT: Homodimer or multimer. {ECO:0000269|PubMed:17482570}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255}.
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DR   AlphaFoldDB; P85157; -.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Prothrombin activator;
KW   Serine protease.
FT   CHAIN           1..>18
FT                   /note="Subtilisin-like serine protease AS-E2"
FT                   /id="PRO_0000291533"
FT   NON_TER         18
FT                   /evidence="ECO:0000303|PubMed:17482570"
SQ   SEQUENCE   18 AA;  1914 MW;  8F834292999364B5 CRC64;
     AYVSQSGAPW GLGRISHK