ID   CATV_NPVEP              Reviewed;         323 AA.
AC   Q91GE3;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Viral cathepsin;
DE            Short=V-cath;
DE            EC=3.4.22.50;
DE   AltName: Full=Cysteine proteinase;
DE            Short=CP;
DE   Flags: Precursor;
GN   Name=VCATH; Synonyms=111;
OS   Epiphyas postvittana nucleopolyhedrovirus (EppoMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=70600;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11907346; DOI=10.1099/0022-1317-83-4-957;
RA   Hyink O., Dellow R.A., Olsen M.J., Caradoc-Davies K.M.B., Drake K.,
RA   Herniou E.A., Cory J.S., O'Reilly D.R., Ward V.K.;
RT   "Whole genome analysis of the Epiphyas postvittana nucleopolyhedrovirus.";
RL   J. Gen. Virol. 83:957-971(2002).
CC   -!- FUNCTION: Cysteine protease that plays an essential role in host
CC       liquefaction to facilitate horizontal transmission of the virus. May
CC       participate in the degradation of foreign protein expressed by the
CC       baculovirus system (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase of broad specificity, hydrolyzing substrates of
CC         both cathepsin L and cathepsin B.; EC=3.4.22.50;
CC   -!- PTM: Synthesized as an inactive proenzyme and activated by proteolytic
CC       removal of the inhibitory propeptide. {ECO:0000250}.
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; AY043265; AAK85675.1; -; Genomic_DNA.
DR   RefSeq; NP_203280.1; NC_003083.1.
DR   SMR; Q91GE3; -.
DR   MEROPS; C01.083; -.
DR   GeneID; 921832; -.
DR   KEGG; vg:921832; -.
DR   Proteomes; UP000203221; Genome.
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; Reference proteome;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..112
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322209"
FT   CHAIN           113..323
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050579"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        133..174
FT                   /evidence="ECO:0000250"
FT   DISULFID        167..207
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..310
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  36835 MW;  A0EB527CC5FF740E CRC64;
     MSKFLLYWFV YGVVCSAAYD ILKAPNYFEE FVRQYNKQYD SEYEKLRRYK IFQHNLNDII
     TKNRNDTAVY KINKFSDLSK DETIAKYTGL SLPLHTQNFC EVVVLDRPPG KGPLEFDWRR
     FNKITSVKNQ GMCGACWAFA TLASLESQFA IAHDRLINLS EQQMIDCDSV DVGCEGGLLH
     TAFEAIISMG GVQIENDYPY ESSNNYCRMD PTKFVVGVKQ CNRYITIYEE KLKDVLRLAG
     PIPVAIDASD ILNYEQGIIK YCANNGLNHA VLLVGYGVEN NVPYWILKNS WGTDWGEQGF
     FKIQQNVNAC GIKNELASTA EIN