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CYSP_SCHJA
ID   CYSP_SCHJA              Reviewed;         342 AA.
AC   P43157;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cathepsin B-like cysteine proteinase;
DE            EC=3.4.22.-;
DE   AltName: Full=Antigen Sj31;
DE   Flags: Precursor;
GN   Name=CATB;
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Chinese;
RX   PubMed=7899786;
RA   Merckelbach A., Hasse S., Dell R., Eschlbeck A., Ruppel A.;
RT   "cDNA sequences of Schistosoma japonicum coding for two cathepsin B-like
RT   proteins and Sj32.";
RL   Trop. Med. Parasitol. 45:193-198(1994).
CC   -!- FUNCTION: Thiol protease. Has a role as a digestive enzyme.
CC   -!- TISSUE SPECIFICITY: Intestine (gut).
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   EMBL; X70968; CAA50305.1; -; mRNA.
DR   PIR; S31907; S31907.
DR   AlphaFoldDB; P43157; -.
DR   SMR; P43157; -.
DR   MEROPS; C01.062; -.
DR   PRIDE; P43157; -.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR012599; Propeptide_C1A.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   Pfam; PF08127; Propeptide_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..89
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026170"
FT   CHAIN           90..342
FT                   /note="Cathepsin B-like cysteine proteinase"
FT                   /id="PRO_0000026171"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        115..159
FT                   /evidence="ECO:0000250"
FT   DISULFID        151..217
FT                   /evidence="ECO:0000250"
FT   DISULFID        152..155
FT                   /evidence="ECO:0000250"
FT   DISULFID        188..221
FT                   /evidence="ECO:0000250"
FT   DISULFID        196..207
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  38796 MW;  81BA89CD61A68B4C CRC64;
     MLKIAVYIVS LFTFLEAHVT TRNNQRIEPL SDEMISFINE HPDAGWKADK SDRFHSLDDA
     RILMGARKED AEMKRNRRPT VDHHDLNVEI PSQFDSRKKW PHCKSISQIR DQSRCGSCWA
     FGAVEAMTDR ICIQSGGGQS AELSALDLIS CCKDCGDGCQ GGFPGVAWDY WVKRGIVTGG
     SKENHTGCQP YPFPKCEHHT KGKYPACGTK IYKTPQCKQT CQKGYKTPYE QDKHYGDESY
     NVQNNEKVIQ RDIMMYGPVE AAFDVYEDFL NYKSGIYRHV TGSIVGGHAI RIIGWGVEKR
     TPYWLIANSW NEDWGEKGLF RMVRGRDECS IESDVVAGLI KT
 
 
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