ID   FIBR_CORMI              Reviewed;          10 AA.
AC   P85318;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Fibrinolytic enzyme;
DE            EC=3.4.-.-;
DE   AltName: Full=CMase;
DE   Flags: Fragment;
OS   Cordyceps militaris (Caterpillar fungus) (Clavaria militaris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=73501;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR LOCATION.
RX   AGRICOLA=IND44034274; DOI=10.1007/s11274-007-9497-1;
RA   Cui L., Dong M.S., Chen X.H., Jiang M., Lv X., Yan G.;
RT   "A novel fibrinolytic enzyme from Cordyceps militaris, a Chinese
RT   traditional medicinal mushroom.";
RL   World J. Microbiol. Biotechnol. 24:483-489(2008).
CC   -!- FUNCTION: Hydrolyzes fibrin. {ECO:0000269|Ref.1}.
CC   -!- ACTIVITY REGULATION: Activated by Mg(2+) and Fe(2+) ions. Inhibited by
CC       Cu(2+) ions and EDTA. Activity is unaffected by Ca(2+), Ba(2+), Zn(2+),
CC       K(+) and Mn(2+) ions. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. Active from pH 5.0 to 8.0 at 37 degrees Celsius,
CC         above pH 8.0 stability decreases rapidly. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius. Active between 15 and 45
CC         degrees Celsius, however activity rapidly decreases after 1 hour
CC         incubation at temperatures above 40 degrees Celsius.
CC         {ECO:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F: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.
FT   CHAIN           1..>10
FT                   /note="Fibrinolytic enzyme"
FT                   /id="PRO_0000312841"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   10 AA;  943 MW;  32C470C2D5A2C878 CRC64;
     IVGGVSVAIE