ID   CATV_NPVCF              Reviewed;         324 AA.
AC   P41715; O41479;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 nuclear polyhedrosis virus (CfMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=208973;
OH   NCBI_TaxID=7141; Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ireland;
RX   PubMed=8547313; DOI=10.1016/0167-4781(95)00195-6;
RA   Hill J.E., Kuzio J., Faulkner P.;
RT   "Identification and characterization of the v-cath gene of the baculovirus,
RT   CfMNPV.";
RL   Biochim. Biophys. Acta 1264:275-278(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ireland;
RX   PubMed=15784887; DOI=10.1099/vir.0.80490-0;
RA   de Jong J.G., Lauzon H.A.M., Dominy C., Poloumienko A., Carstens E.B.,
RA   Arif B.M., Krell P.J.;
RT   "Analysis of the Choristoneura fumiferana nucleopolyhedrovirus genome.";
RL   J. Gen. Virol. 86:929-943(2005).
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; M97906; AAA96732.1; -; Genomic_DNA.
DR   EMBL; AF512031; AAP29900.1; -; Genomic_DNA.
DR   PIR; S62735; S62735.
DR   RefSeq; NP_848429.1; NC_004778.3.
DR   SMR; P41715; -.
DR   MEROPS; C01.083; -.
DR   GeneID; 1482738; -.
DR   KEGG; vg:1482738; -.
DR   BRENDA; 3.4.22.50; 1364.
DR   Proteomes; UP000204418; 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; 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_0000322208"
FT   CHAIN           114..324
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050578"
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;  36682 MW;  ADCF99F03CF649B5 CRC64;
     MNKIVLYLLV YGAVQCAAYD VLKAPNYFED FLHKFNKSYS SESEKLRRFQ IFRHNLEEII
     NKNHNDSTAQ YEINKFADLS KDETISKYTG LSLPLQTQNF CEVVVLDRPP DKGPLEFDWR
     RLNKVTSVKN QGMCGACWAF ATLGSLESQF AIKHNQFINL SEQQLIDCDF VDAGCDGGLL
     HTAFEAVMNM GGIQAESDYP YEANNGDCRA NAAKFVVKVK KCYRYITVFE EKLKDLLRSV
     GPIPVAIDAS DIVNYKRGIM KYCANHGLNH AVLLVGYAVE NGVPFWILKN TWGADWGEQG
     YFRVQQNINA CGIQNELPSS AEIY