ID   CATV_NPVAH              Reviewed;         337 AA.
AC   Q80LP4;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=52;
OS   Adoxophyes honmai nucleopolyhedrovirus.
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=224399;
OH   NCBI_TaxID=85585; Adoxophyes honmai (Smaller tea tortrix moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ADN001;
RX   PubMed=14599801; DOI=10.1016/j.virol.2003.08.002;
RA   Nakai M., Goto C., Kang W., Shikata M., Luque T., Kunimi Y.;
RT   "Genome sequence and organization of a nucleopolyhedrovirus isolated from
RT   the smaller tea tortrix, Adoxophyes honmai.";
RL   Virology 316:171-183(2003).
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; AP006270; BAC67303.1; -; Genomic_DNA.
DR   RefSeq; NP_818699.1; NC_004690.1.
DR   SMR; Q80LP4; -.
DR   MEROPS; C01.083; -.
DR   GeneID; 1485819; -.
DR   KEGG; vg:1485819; -.
DR   Proteomes; UP000232720; 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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..126
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322202"
FT   CHAIN           127..337
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050573"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        147..188
FT                   /evidence="ECO:0000250"
FT   DISULFID        181..221
FT                   /evidence="ECO:0000250"
FT   DISULFID        276..324
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  37937 MW;  B36B91D79BCF8FD5 CRC64;
     MTLLMIFTIL LVASSQIEGH LKFDIHDAQH YFETFIINYN KQYPDTKTKN YRFKIFKQNL
     EDINEKNKLN DSAIYNINKF SDLSKNELLT KYTGLTSKKP SNMVRSTSNF CNVIHLDAPP
     DVHDELPQNF DWRVNNKMTS VKDQGACGSC WAHAAVGTLE TLYAIKHNYL INLSEQQLID
     CDSANMACDG GLMHTAFEQL MNAGGLMEEI DYPYQGTKGV CKIDNKKFAL SVSSCKRYIF
     QNEENLKKEL ITMGPIAMAI DAASISTYSK GIIHFCENLG LNHAVLLVGY GTEGGVSYWT
     LKNSWGSDWG EDGYFRVKRN INACGLNNQL AASATIH