ID   CATV_NPVCD              Reviewed;         324 AA.
AC   Q6VTL7; Q6LCB9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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; ORFNames=Ac127, Op125;
OS   Choristoneura fumiferana defective polyhedrosis virus (Cfdef).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=74660;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15784888; DOI=10.1099/vir.0.80489-0;
RA   Lauzon H.A., Jamieson P.B., Krell P.J., Arif B.M.;
RT   "Gene organization and sequencing of the Choristoneura fumiferana defective
RT   nucleopolyhedrovirus genome.";
RL   J. Gen. Virol. 86:945-961(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Arif B., Peng H.;
RT   "CfDEF, defective virus from Choristoneura fumiferana
RT   nucleopolyhedrovirus.";
RL   Submitted (SEP-1996) 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; AY327402; AAQ91676.1; -; Genomic_DNA.
DR   EMBL; U72030; AAB68595.1; -; Genomic_DNA.
DR   RefSeq; NP_932731.1; NC_005137.2.
DR   SMR; Q6VTL7; -.
DR   MEROPS; C01.083; -.
DR   GeneID; 2943774; -.
DR   KEGG; vg:2943774; -.
DR   Proteomes; UP000202937; 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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322206"
FT   CHAIN           114..324
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000322207"
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"
FT   CONFLICT        210
FT                   /note="L -> A (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226..228
FT                   /note="VLM -> ITV (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="I -> S (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="L -> I (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259..261
FT                   /note="VIR -> IMK (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="E -> Q (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="T -> A (in Ref. 2; AAB68595)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   324 AA;  36849 MW;  ED605045A3F68BB0 CRC64;
     MNKIVLYLLI YVGTFSAAYD LLKAPSYFED FLHNFNKNYS SKSEKLHRFK IFQHNLEEII
     NKNLNDTSAQ YEINKFSDLS KDETISKYTG LSLPLQNQNF CEVVVLNRPP DKGPLEFDWR
     RLNKVTSVKN QGTCGACWAF ATLGSLESQF AIKHDQLINL SEQQLIDCDF VDMGCDGGLL
     HTAYEAVMNM GGIQAENDYP YEANNGDCRL NAAKFVVKVK KCYRYVLMFE EKLKDLLRIV
     GPLPVAIDAS DIVNYKRGVI RYCANHGLNH AVLLVGYAVE NGVPFWILKN TWGTDWGEQG
     YFRVQQNINA CGIQNELPSS AEIY