ID   SP01_SCEBO              Reviewed;          13 AA.
AC   Q10721;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Serine proteinase;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Scedosporium boydii (Pseudallescheria boydii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Microascaceae; Scedosporium.
OX   NCBI_TaxID=5597;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=4595.90 {ECO:0000269|PubMed:8670095};
RX   PubMed=8670095; DOI=10.1042/bj3150119;
RA   Larcher G., Cimon B., Symoens F., Tronchin G., Chabasse D., Bouchara J.-P.;
RT   "A 33 kDa serine proteinase from Scedosporium apiospermum.";
RL   Biochem. J. 315:119-126(1996).
CC   -!- FUNCTION: Serine protease. Degrades fibrinogen.
CC       {ECO:0000269|PubMed:8670095}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by pMSF, chymotrypsin and SDS.
CC       Inhibited by the trypsin inhibitors Tos-Phe-CH2Cl, Tos-Lys-CH2Cl and
CC       SBTI, and by bivalent cations. Slightly inhibited by the elastitinal
CC       and metal chelators EDTA and EGTA, by ethanol and by non-ionic
CC       detergents. Not inhibited by alkylating agents, reducing agents,
CC       pepstatin, o-phenanthroline, leupeptin, E-64, bestatin, DMSO and
CC       methanol. {ECO:0000269|PubMed:8670095}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.35 mM for N-Suc-Ala-Ala-Pro-Phe-pNA
CC         {ECO:0000269|PubMed:8670095};
CC         KM=0.31 mM for N-Ac-Ile-Glu-Ala-Arg-pNA {ECO:0000269|PubMed:8670095};
CC         KM=2.59 mM for N-Suc-Ala-Ala-Pro-Leu-pNA
CC         {ECO:0000269|PubMed:8670095};
CC         Vmax=1032 umol/min/mg enzyme toward N-Suc-Ala-Ala-Pro-Phe- pNA
CC         {ECO:0000269|PubMed:8670095};
CC         Vmax=234 umol/min/mg enzyme toward N-Ac-Ile-Glu-Ala-Arg- pNA
CC         {ECO:0000269|PubMed:8670095};
CC         Vmax=613 umol/min/mg enzyme toward N-Suc-Ala-Ala-Pro-Leu- pNA
CC         {ECO:0000269|PubMed:8670095};
CC       pH dependence:
CC         Optimum pH is 9.0. 20% of maximum activity is seen at pH 5.0.
CC         Inactive below pH 5.0 and above pH 11.0, inactivation by acidic pH is
CC         reversible. {ECO:0000269|PubMed:8670095};
CC       Temperature dependence:
CC         Optimum temperature is 37-50 degrees Celsius. 49% of maximum activity
CC         is seen at 60 degrees Celsius, no activity is seen at 70 degrees
CC         Celsius. Thermolabile, a significant decrease in activity is seen
CC         after incubation at temperatures above 42 degrees Celsius for 20 min.
CC         {ECO:0000269|PubMed:8670095};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8670095}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8670095}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:8670095}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255}.
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DR   PIR; S66558; S66558.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Secreted; Serine protease.
FT   CHAIN           1..>13
FT                   /note="Serine proteinase"
FT                   /id="PRO_0000298772"
FT   NON_TER         13
FT                   /evidence="ECO:0000303|PubMed:8670095"
SQ   SEQUENCE   13 AA;  1292 MW;  9DD5F3294A68D861 CRC64;
     AYTGQTGAPW GLA