ID   CATV_NPVAP              Reviewed;         324 AA.
AC   Q91CL9;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   10-JUN-2026, entry version 75.
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;
OS   Antheraea pernyi nuclear polyhedrosis virus (ApNPV).
OC   Viruses; Viruses incertae sedis; Naldaviricetes; Lefavirales;
OC   Baculoviridae; Alphabaculovirus; Alphabaculovirus anpernyi.
OX   NCBI_TaxID=161494;
OH   NCBI_TaxID=7119; Antheraea pernyi (Chinese oak silk moth) (Bombyx pernyi).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=16233185; DOI=10.1263/jbb.93.183;
RA   Huang Y.J., Kobayashi J., Yoshimura T.;
RT   "Genome mapping and gene analysis of Antheraea pernyi nucleopolyhedrovirus
RT   for improvement of baculovirus expression vector system.";
RL   J. Biosci. Bioeng. 93:183-191(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; AB072731; BAB69773.1; -; Genomic_DNA.
DR   RefSeq; YP_611001.1; NC_008035.3.
DR   SMR; Q91CL9; -.
DR   MEROPS; C01.083; -.
DR   GlyCosmos; Q91CL9; 1 site, No reported glycans.
DR   GeneID; 5141489; -.
DR   KEGG; vg:5141489; -.
DR   OrthoDB; 4752at10239; -.
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   FunFam; 3.90.70.10:FF:000103; Hypothetical LOC496748; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322203"
FT   CHAIN           114..324
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050574"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        134..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        168..208
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..311
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36770 MW;  AA1D457183DEC547 CRC64;
     MNKIVLYLLV YGATLGAAYD LLKAPSYFEE FLHKFNKNYS SESEKLRRFK IFQHNLEEII
     NKNQNDTSAQ YEINKFSDLS KDETISKYTG LSLPLQKQNF CEVVVLDRPP DKGPLEFDWR
     RLNKVTSVKN QGMCGACWAF ATLGSLESQF AIKHDQLINL SEQQLIDCDF VDVGCDGGLL
     HTAYEAVMNM GGIQAENDYP YEANNGPCRV NAAKFVVRVK KCYRYVTLFE EKLKDLLRIV
     GPIPVAIDAS DIVGYKRGII RYCENHGLNH AVLLVGYGVE NGIPFWILKN TWGADWGEQG
     YFRVQQNINA CGIKNELPSS AEIY
//