ID   CATV_NPVHZ              Reviewed;         367 AA.
AC   Q8V5U0;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=57;
OS   Heliothis zea nuclear polyhedrosis virus (HzSNPV) (Helicoverpa zea single
OS   nucleocapsid nuclear polyhedrosis virus).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC   unclassified Alphabaculovirus.
OX   NCBI_TaxID=28290;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Chen X., Zhang W.-J., Wong J., Chun G., Lu A., McCutchen B.F.,
RA   Presnail J.K., Herrmann R., Dolan M., Tingey S., Hu Z.-H., Vlak J.M.;
RT   "Genome sequence analysis of Helicoverpa zea single nucleocapsid
RT   nucleopolyhedrovirus.";
RL   Submitted (JAN-2001) 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:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AF334030; AAL56202.1; -; Genomic_DNA.
DR   SMR; Q8V5U0; -.
DR   MEROPS; C01.083; -.
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; 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; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..156
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322211"
FT   CHAIN           157..367
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050581"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        177..218
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..354
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  42203 MW;  317FEAE4F3D1CA8F CRC64;
     MRKYHSNIMH KIITFVSLLW TFVVCDEISL HTSSSPPPLS SPVPVLYYNL DQSEIYFKHF
     LQQYNKSYDD PKEYQYRYNV FKDNLNKINS QNRENLLNNK NNNDSLSTSA QFGVNKFSDK
     TPDEVLHSNT GFFLNLSQHY TLCENRIVKG APDIRLPDYY DWRDTNKVTP IKDQGVCGSC
     WAFVAIGNIE SQYAIRHNKL IDLSEQQLLD CDEVDLGCNG GLMHLAFQEL LLMGGVETEA
     DYPYQGSEQM CTLDNRKIAV KLNSCFKYDI RDENKLKELV YTTGPVAIAV DAMDIINYRR
     GILNQCHIYD LNHAVLLIGW GIENNVPYWI IKNSWGEDWG ENGFLRVRRN VNACGLLNEF
     GASSVIQ