ID   CYSP1_LEIPI             Reviewed;         354 AA.
AC   P35591;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cysteine proteinase 1;
DE            EC=3.4.22.-;
DE   AltName: Full=Amastigote cysteine proteinase A-1;
DE   Flags: Precursor;
GN   Name=CYS1;
OS   Leishmania pifanoi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida R.W.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 147-311.
RX   PubMed=8426606; DOI=10.1016/0166-6851(93)90248-v;
RA   Traub-Cseko Y.M., Duboise M., Boukai L.K., McMahon-Pratt D.;
RT   "Identification of two distinct cysteine proteinase genes of Leishmania
RT   pifanoi axenic amastigotes using the polymerase chain reaction.";
RL   Mol. Biochem. Parasitol. 57:101-115(1993).
CC   -!- FUNCTION: The cysteine proteinases have a potential role in host-
CC       parasite interaction and virulence.
CC   -!- DEVELOPMENTAL STAGE: Primarily expressed by the amastigote stage.
CC       Expressed 4 times more in amastigotes than in promastigotes.
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; L29168; AAA91859.1; -; Genomic_DNA.
DR   EMBL; L00717; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; B48566; B48566.
DR   AlphaFoldDB; P35591; -.
DR   SMR; P35591; -.
DR   MEROPS; C01.076; -.
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   Virulence; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..125
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000026384"
FT   CHAIN           126..354
FT                   /note="Cysteine proteinase 1"
FT                   /id="PRO_0000026385"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..191
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        282..330
FT                   /evidence="ECO:0000250"
FT   CONFLICT        149
FT                   /note="L -> Q (in Ref. 2; L00717)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="S -> W (in Ref. 2; L00717)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="F -> S (in Ref. 2; L00717)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  38746 MW;  37C5DE2900800AAA CRC64;
     MARRNPLLFA IVVTILFVVC YGSALIAQTP PPVDNFVASA HYGSFKKRHG KAFGGDAEEG
     HRFNAFKQNM QTAYFLNTQN PHAHYDVSGK FADLTPQEFA KLYLNPDYYA RHLKDHKEDV
     HVDDSAPSGV MSVDWRDKGA VTPVKNQGLC GSCWAFSAIG NIEGQWAASG HSLVSLSEQM
     LVSCDNIDEG CNGGLMDQAM NWIMQSHNGS VFTEASYPYT SGGGTRPPCH DEGEVGAKIT
     GFLSLPHDEE RIAEWVEKRG PVAVAVDATT WQLYFGGVVS LCLAWSLNHG VLIVGFNKNA
     KPPYWIVKNS WGSSWGEKGY IRLAMGSNQC MLKNYPVSAT VESPHTPHVP TTTA