ID   KARA_BROPL              Reviewed;          14 AA.
AC   P22442;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Karatasin;
DE            EC=3.4.22.-;
DE   Flags: Fragment;
OS   Bromelia plumieri (Karatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Bromelia.
OX   NCBI_TaxID=4617;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1368518; DOI=10.1271/bbb1961.54.17;
RA   Montes C., Amador M., Cuevas D., Cordoba F.;
RT   "Subunit structure of karatasin, the proteinase isolated from Bromelia
RT   plumieri (karatas).";
RL   Agric. Biol. Chem. 54:17-24(1990).
CC   -!- SUBUNIT: Dimer of two small subunits linked by disulfide bonds.
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   PIR; PT0029; PT0029.
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; Disulfide bond; Hydrolase; Protease;
KW   Thiol protease.
FT   CHAIN           1..>14
FT                   /note="Karatasin"
FT                   /id="PRO_0000050560"
FT   NON_TER         14
SQ   SEQUENCE   14 AA;  1604 MW;  FDA156893F0834FA CRC64;
     VPETWDXXDY GAQT