ID   CYSP_TRIVA              Reviewed;          22 AA.
AC   P33404;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Cysteine proteinase;
DE            EC=3.4.22.-;
DE   Flags: Fragment;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8319888; DOI=10.1111/j.1574-6968.1993.tb06304.x;
RA   Irvine J.W., Coombs G.H., North M.J.;
RT   "Purification of cysteine proteinases from trichomonads using bacitracin-
RT   sepharose.";
RL   FEMS Microbiol. Lett. 110:113-120(1993).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   MEROPS; C01.148; -.
DR   GO; GO:0008234; F:cysteine-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; Thiol protease.
FT   CHAIN           1..>22
FT                   /note="Cysteine proteinase"
FT                   /id="PRO_0000050546"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   UNSURE          1
FT                   /note="G or K"
FT   NON_TER         22
SQ   SEQUENCE   22 AA;  2399 MW;  0EE40FD86661ACCB CRC64;
     GADDSDWRKK GAVNVIXKDQ GQ