ID   CYSP_PLAVN              Reviewed;         506 AA.
AC   P46102;
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=Cysteine proteinase;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Plasmodium vinckei.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8485161; DOI=10.1016/0167-4781(93)90250-h;
RA   Rosenthal P.J.;
RT   "A Plasmodium vinckei cysteine proteinase shares unique features with its
RT   Plasmodium falciparum analogue.";
RL   Biochim. Biophys. Acta 1173:91-93(1993).
CC   -!- FUNCTION: Probably degrades erythrocyte hemoglobin.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L08500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S32561; S32561.
DR   AlphaFoldDB; P46102; -.
DR   SMR; P46102; -.
DR   MEROPS; C01.077; -.
DR   VEuPathDB; PlasmoDB:PVBDA_1302530; -.
DR   VEuPathDB; PlasmoDB:PVLDE_1302760; -.
DR   VEuPathDB; PlasmoDB:PVPCR_1302640; -.
DR   VEuPathDB; PlasmoDB:PVSEL_1302520; -.
DR   VEuPathDB; PlasmoDB:PVVCY_1302320; -.
DR   VEuPathDB; PlasmoDB:YYE_00220; -.
DR   VEuPathDB; PlasmoDB:YYG_03508; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
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; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..262
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026475"
FT   CHAIN           263..506
FT                   /note="Cysteine proteinase"
FT                   /id="PRO_0000026476"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        284..326
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  58255 MW;  7478494461A617F1 CRC64;
     MSDNIGQINF TIPGIQSLDE NDTYLKINHK KTIKICAYAI TAIALFFIGG VFFKNQAKIN
     ALDAIDEAVL MNKEIAHLRE ILNKYKATIN EDDEFVYQAY DNKNGDSENQ LLLMLHKLLK
     NNANKVNTFD VNNESNKNID PTYIFRQKLE SMQDNIKYAS KFFKYMKENN KKYENMDEQL
     QRFENFKIRY MKTQKHNEMV GKNGLTYVQK VNQYSDFSKE EFDNYFKKLL SVPMDLKSKY
     IVPLKKHLAN TNLISVDNKS KDFPDSRDYR SKFNFLPPKD QGNCGSCWAF AAIGNFEYLY
     VHTRHEMPIS FSEQQMVDCS TENYGCDGGN PFYAFLYMIN NGVCLGDEYP YKGHEDFFCL
     NYRCSLLGRV HFIGDVKPNE LIMALNYVGP VTIAVGASED FVLYSGGVFD GECNPELNHS
     VLLVGYGQVK KSLAFEDSHS NVDSNLIKKY KENIKGDDDD DIIYYWIVRN SWGPNWGEGG
     YIRIKRNKAG DDGFCGVGSD VFFPIY