ID   CATV_NPVBS              Reviewed;         331 AA.
AC   Q9YWK4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 74.
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   Buzura suppressaria nuclear polyhedrosis virus (BsNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=74320;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9820162; DOI=10.1099/0022-1317-79-11-2841;
RA   Hu Z.H., Arif B.M., Jin F., Martens J.W.M., Chen X.W., Sun J.S.,
RA   Zuidema D., Goldbach R.W., Vlak J.M.;
RT   "Distinct gene arrangement in the Buzura suppressaria single-nucleocapsid
RT   nucleopolyhedrovirus genome.";
RL   J. Gen. Virol. 79:2841-2851(1998).
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; AF058929; AAC77812.1; -; Genomic_DNA.
DR   RefSeq; YP_009001801.1; NC_023442.1.
DR   SMR; Q9YWK4; -.
DR   MEROPS; C01.083; -.
DR   GeneID; 18266944; -.
DR   KEGG; vg:18266944; -.
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; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..116
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322205"
FT   CHAIN           117..331
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050576"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000250"
FT   DISULFID        137..178
FT                   /evidence="ECO:0000250"
FT   DISULFID        171..211
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..315
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  37744 MW;  6DB980A418FA2BBC CRC64;
     MKKLVICIIL NLIVAKNYAF AYDLLKAGDY FETFLANYNK MYNDTSEKER RFSIFQQTLE
     EINYKNRLND SAVYQINKFA DLSKNEIISK YTGLNMPVQT TNFCKTIVID QPPGKGPLNF
     DWRQQNKVTS IKNQKACGAC WAFATLASIE SQYAIKNNVH IDLSEQQMID CDYVDMGCDG
     GLLHTAFEQM IQMGELVQEH EYPYAGVNKP CELRGDETGV VKVKGCYRYV VFREEKLKDL
     LRAVGPIPMA IDASGIVNYH HGIIHYCENY GLNHAVLLVG YGVENNVPFW TFKNTWGKDW
     GEEGYFRVRQ NVDACGMTNE LASSAVIDWD A