ID   FIBR2_HEDJA             Reviewed;          32 AA.
AC   P86876;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Fibrinolytic enzyme 2;
DE            Short=NJF-2;
DE            EC=3.4.21.-;
DE   Flags: Fragments;
OS   Hediste japonica (Polychaete worm) (Neanthes japonica).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Hediste.
OX   NCBI_TaxID=73376;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MASS SPECTROMETRY.
RA   Hong M., Li Q., Wang S.H., Bo Q.Q., Ge X.;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- FUNCTION: Serine protease. Has fibrinolytic and fibrinogenolytic but no
CC       plasminogenolytic activity. Cleaves after Arg and Lys residues. Cleaves
CC       fibrinogen alpha chain, beta chain and gamma chain in that order.
CC       {ECO:0000269|Ref.1}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF. Not inhibited by benzamidine,
CC       aprotinin, SBTI, EDTA, EGTA, 2-mercaptoethanol, iodoacetic acid or
CC       pepstatin A. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 10. Active from pH 7 to 11. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Active from 30 to 70
CC         degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: Mass=29248.75; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC       4.55, its MW is: 31 kDa.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown. {ECO:0000305}.
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DR   AlphaFoldDB; P86876; -.
DR   SMR; P86876; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Fibrinogenolytic toxin;
KW   Fibrinolysis; Hemostasis; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Serine protease; Toxin.
FT   CHAIN           <1..>32
FT                   /note="Fibrinolytic enzyme 2"
FT                   /id="PRO_0000405025"
FT   DOMAIN          <1..>32
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        5
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10082"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         32
SQ   SEQUENCE   32 AA;  3453 MW;  F8734C6487AAA306 CRC64;
     ISGTSMSCPH VAGRAYVLDT SLRVYLLDTG LR