ID   CYSP_PLAVS              Reviewed;         583 AA.
AC   P42666;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cysteine proteinase;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Plasmodium vivax (strain Salvador I).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=126793;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8057374; DOI=10.1006/jmbi.1994.1506;
RA   Rosenthal P.J., Ring C.S., Chen X., Cohen F.E.;
RT   "Characterization of a Plasmodium vivax cysteine proteinase gene identifies
RT   uniquely conserved amino acids that may mediate the substrate specificity
RT   of malarial hemoglobinases.";
RL   J. Mol. Biol. 241:312-316(1994).
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}.
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DR   EMBL; L26362; AAA60368.1; -; mRNA.
DR   PIR; S46265; S46265.
DR   AlphaFoldDB; P42666; -.
DR   SMR; P42666; -.
DR   STRING; 5855.PVX_117565; -.
DR   PRIDE; P42666; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..338
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026477"
FT   CHAIN           339..583
FT                   /note="Cysteine proteinase"
FT                   /id="PRO_0000026478"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        495
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        547
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        360..402
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   583 AA;  65722 MW;  15EA8A407717C406 CRC64;
     MAQDIKIMNL TKSSLEALNR NQMLSKKSSR KILKICMYAI LTFAMCGVVL ICLTAMSNSD
     GSLTQSGSHN QSGSLKGLSS TPGDGEILNK AEIETLRFIF SNYPHGNRDP TGDDVEKPAD
     AALPNEEDQK VKIADAGKHI KLMKQYNEIV ADMSEDNKEQ LAKMLRELLK KKINERKKKR
     EDPNGNNEEG KEVINISVPS FNYKRVSANQ DDSDDEEEVS VAQIEGLFVN LKYASKFFNF
     MNKYKRSYKD INEQMEKYKN FKMNYLKIKK HNETNQMYKM KVNQFSDYSK KDFESYFRKL
     VPIPDHLKKK YVVPFSSMNN GKGKNVVTSS SGANLLADVP EILDYREKGI VHEPKDQGLC
     GSCWAFASVG NVECMYAKEH NKTILTLSEQ EVVDCSKLNF GCDGGHPFYS FIYAIENGIC
     MGDDYKYKAM DNLFCLNYRC KNKVTLSSVG GVKENELIRA LNEVGPVSVN VGVTDDFSFY
     GGGIFNGTCT EELNHSVLLV GYGQVQSSKI FQEKNAYDDA SGVTKKGALS YPSKADDGIQ
     YYWIIKNSWS KFWGENGFMR ISRNKEGDNV FCGIGVEVFY PIL