ID   CATV_NPVOP              Reviewed;         324 AA.
AC   O10364;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=ORF125;
OS   Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC   Alphabaculovirus orpseudotsugatae.
OX   NCBI_TaxID=262177;
OH   NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA   Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT   "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT   polyhedrosis virus genome.";
RL   Virology 229:381-399(1997).
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; U75930; AAC59124.1; -; Genomic_DNA.
DR   RefSeq; NP_046281.1; NC_001875.2.
DR   SMR; O10364; -.
DR   MEROPS; C01.083; -.
DR   GlyCosmos; O10364; 1 site, No reported glycans.
DR   GeneID; 912077; -.
DR   KEGG; vg:912077; -.
DR   OrthoDB; 4752at10239; -.
DR   Proteomes; UP000009248; 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   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411:SF947; CATHEPSIN O; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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_0000322214"
FT   CHAIN           114..324
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050584"
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;  36982 MW;  D36A709D6063C15C CRC64;
     MNKIMLCLLV CGVVHAATYD LLKAPNYFED FLHKFNKNYS SESEKLHRFK IFQHNLEEII
     NKNQNDSTAQ YEINKFSDLS KEEAISKYTG LSLPHQTQNF CEVVILDRPP DRGPLEFDWR
     QFNKVTSVKN QGVCGACWAF ATLGSLESQF AIKYNRLINL SEQQFIDCDR VNAGCDGGLL
     HTAFESAMEM GGVQMESDYP YETANGQCRI NPNRFVVGVR SCRRYIVMFE EKLKDLLRAV
     GPIPVAIDAS DIVNYRRGIM RQCANHGLNH AVLLVGYAVE NNIPYWILKN TWGTDWGEDG
     YFRVQQNINA CGIRNELVSS AEIY
//