ID   FIBR_EISFE              Reviewed;          25 AA.
AC   P81802;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Fibrinolytic enzyme large subunit;
DE            EC=3.4.-.-;
DE   Flags: Fragment;
OS   Eisenia fetida (Red wiggler worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Eisenia.
OX   NCBI_TaxID=6396;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=9467874; DOI=10.1016/s0305-0491(97)00223-x;
RA   Yang J.-S., Ru B.-G.;
RT   "Purification and characterization of an SDS-activated fibrinolytic enzyme
RT   from Eisenia fetida.";
RL   Comp. Biochem. Physiol. 118B:623-631(1997).
CC   -!- FUNCTION: Cleaves the carboxyl side of basic amino acids, small neutral
CC       amino acids, and Met residue. It is also a plasminogen activator.
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit held together by
CC       hydrophobic interactions.
CC   -!- MISCELLANEOUS: Activated by sodium dodecyl sulfate (SDS).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   AlphaFoldDB; P81802; -.
DR   SMR; P81802; -.
DR   GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..>25
FT                   /note="Fibrinolytic enzyme large subunit"
FT                   /id="PRO_0000088687"
FT   DOMAIN          1..>25
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2684 MW;  E70AC798E85B0175 CRC64;
     VIGGTNASPG EIPWQLSQQR QSGSW