ID   CATV_NPVEP              Reviewed;         323 AA.
AC   Q91GE3;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   05-MAY-2009, entry version 36.
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=111;
OS   Epiphyas postvittana nucleopolyhedrovirus (EppoMNPV).
OC   Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=70600;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21904457; PubMed=11907346;
RA   Hyink O., Dellow R.A., Olsen M.J., Caradoc-Davies K.M.B., Drake K.,
RA   Herniou E.A., Cory J.S., O'Reilly D.R., Ward V.K.;
RT   "Whole genome analysis of the Epiphyas postvittana
RT   nucleopolyhedrovirus.";
RL   J. Gen. Virol. 83:957-971(2002).
CC   -!- FUNCTION: Cysteine protease that plays an essential role in host
CC       liquefaction to facilitate horizontal transmission of the virus.
CC       May participate in the degradation of foreign protein expressed by
CC       the baculovirus system (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endopeptidase of broad specificity,
CC       hydrolyzing substrates of both cathepsin L and cathepsin B.
CC   -!- PTM: Synthesized as an inactive proenzyme and activated by
CC       proteolytic removal of the inhibitory propeptide (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   EMBL; AY043265; AAK85675.1; -; Genomic_DNA.
DR   RefSeq; NP_203280.1; -.
DR   HSSP; P53634; 1K3B.
DR   MEROPS; C01.083; -.
DR   GeneID; 921832; -.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; Peptidase_C1A; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   ProDom; PD000158; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 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;
KW   Thiol protease; Zymogen.
FT   SIGNAL        1     18       Potential.
FT   PROPEP       19    112       Activation peptide (Potential).
FT                                /FTId=PRO_0000322209.
FT   CHAIN       113    323       Viral cathepsin.
FT                                /FTId=PRO_0000050579.
FT   ACT_SITE    136    136       By similarity.
FT   ACT_SITE    269    269       By similarity.
FT   ACT_SITE    289    289       By similarity.
FT   CARBOHYD    158    158       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   DISULFID    133    174       By similarity.
FT   DISULFID    167    207       By similarity.
FT   DISULFID    262    310       By similarity.
SQ   SEQUENCE   323 AA;  36835 MW;  A0EB527CC5FF740E CRC64;
     MSKFLLYWFV YGVVCSAAYD ILKAPNYFEE FVRQYNKQYD SEYEKLRRYK IFQHNLNDII
     TKNRNDTAVY KINKFSDLSK DETIAKYTGL SLPLHTQNFC EVVVLDRPPG KGPLEFDWRR
     FNKITSVKNQ GMCGACWAFA TLASLESQFA IAHDRLINLS EQQMIDCDSV DVGCEGGLLH
     TAFEAIISMG GVQIENDYPY ESSNNYCRMD PTKFVVGVKQ CNRYITIYEE KLKDVLRLAG
     PIPVAIDASD ILNYEQGIIK YCANNGLNHA VLLVGYGVEN NVPYWILKNS WGTDWGEQGF
     FKIQQNVNAC GIKNELASTA EIN
//