ID   CATV_GVCPM              Reviewed;         333 AA.
AC   O91466;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=ORF8R;
OS   Cydia pomonella granulosis virus (isolate Mexico/1963) (CpGV) (Cydia
OS   pomonella granulovirus).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Betabaculovirus.
OX   NCBI_TaxID=654905;
OH   NCBI_TaxID=82600; Cydia pomonella (Codling moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Mexican 1;
RX   PubMed=9747739; DOI=10.1099/0022-1317-79-9-2283;
RA   Kang W., Tristem M., Maeda S., Crook N.E., O'Reilly D.R.;
RT   "Identification and characterization of the Cydia pomonella granulovirus
RT   cathepsin and chitinase genes.";
RL   J. Gen. Virol. 79:2283-2292(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mexican 1;
RX   PubMed=11562546; DOI=10.1099/0022-1317-82-10-2531;
RA   Luque T., Finch R., Crook N., O'Reilly D.R., Winstanley D.;
RT   "The complete sequence of the Cydia pomonella granulovirus genome.";
RL   J. Gen. Virol. 82:2531-2547(2001).
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; U53466; AAK70678.1; -; Genomic_DNA.
DR   RefSeq; NP_148795.1; NC_002816.1.
DR   SMR; O91466; -.
DR   MEROPS; C01.047; -.
DR   GeneID; 921370; -.
DR   KEGG; vg:921370; -.
DR   Proteomes; UP000009249; 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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..124
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322218"
FT   CHAIN           125..333
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050588"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        145..186
FT                   /evidence="ECO:0000250"
FT   DISULFID        179..219
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..321
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  37434 MW;  F531CC9AC34FFF5A CRC64;
     MTKLLNFVIL ASVLTVTAHA LTYDLNNSDE LFKNFAIKYN KTYVSDEERA IKLENFKNNL
     KMINEKNMAS KYAVFDINEY SDLNKNALLR RTTGFRLGLK KNPSAFTMTE CSVVVIKDEP
     QALLPETLDW RDKHGVTPVK NQMECGSCWA FSTIANIESL YNIKYDKALN LSEQHLVNCD
     NINNGCAGGL MHWALESILQ EGGVVSAENE PYYGFDGVCK KSPFELSISG SRRYVLQNEN
     KLRELLVVNG PISVAIDVSD LINYKAGIAD ICENNEGLNH AVLLVGYGVK NDVPYWILKN
     SWGAEWGEEG YFRVQRDKNS CGMMNEYASS AIL