ID   CATV_NPVR1              Reviewed;         323 AA.
AC   Q8B9D5;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=RO120;
OS   Rachiplusia ou multiple nucleopolyhedrovirus (strain R1) (RoMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=654904;
OH   NCBI_TaxID=7113; Helicoverpa zea (Corn earworm moth) (Heliothis zea).
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
OH   NCBI_TaxID=29057; Ostrinia nubilalis (European corn borer) (Pyralis nubilalis).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bonning B.C., Harrison R.L.;
RT   "The Rachiplusia ou multiple nucleopolyhedrovirus genome sequence.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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; AY145471; AAN28057.1; -; Genomic_DNA.
DR   SMR; Q8B9D5; -.
DR   MEROPS; C01.083; -.
DR   Proteomes; UP000007020; 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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..112
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322215"
FT   CHAIN           113..323
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050585"
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;  36965 MW;  F76C356CBD303B8D CRC64;
     MNKILFYLFV YGVVNSAAYD LLKAPNYFEE FVHRFNKDYG SEVEKLRRFK IFQHNLNEII
     IKNQNDSAKY EINKFSDLSK DETIAKYTGL SLPIQTQNFC KVIVLDQPPG KGPLEFDWRR
     LNKVTSVKNQ GMCGACWAFA TLASLESQFA IKHNQLINLS EQQMIDCDFV DAGCNGGLLH
     TAFEAIIKMG GVQLESDYPY EADNNNCRMN TNKFLVQVKD CYRYITVYEE KLKDLLRLVG
     PIPMAIDAAD IVNYKQGIIK YCFNSGLNHA VLLVGYGVEN NIPYWTFKNT WGTDWGEEGF
     FRVQQNINAC GMRNELASTA VIY