ID   CATV_NPVAP              Reviewed;         324 AA.
AC   Q91CL9;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   05-MAY-2009, entry version 38.
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;
OS   Antheraea pernyi nuclear polyhedrosis virus (ApNPV).
OC   Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=161494;
OH   NCBI_TaxID=7119; Antheraea pernyi (Chinese oak silk moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=16233185; DOI=10.1263/jbb.93.183;
RA   Huang Y.J., Kobayashi J., Yoshimura T.;
RT   "Genome mapping and gene analysis of Antheraea pernyi
RT   nucleopolyhedrovirus for improvement of baculovirus expression vector
RT   system.";
RL   J. Biosci. Bioeng. 93:183-191(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB072731; BAB69773.1; -; Genomic_DNA.
DR   RefSeq; YP_611001.1; -.
DR   HSSP; P80067; 1JQP.
DR   MEROPS; C01.083; -.
DR   GeneID; 5141489; -.
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     16       Potential.
FT   PROPEP       17    113       Activation peptide (Potential).
FT                                /FTId=PRO_0000322203.
FT   CHAIN       114    324       Viral cathepsin.
FT                                /FTId=PRO_0000050574.
FT   ACT_SITE    137    137       By similarity.
FT   ACT_SITE    270    270       By similarity.
FT   ACT_SITE    290    290       By similarity.
FT   CARBOHYD    159    159       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   DISULFID    134    175       By similarity.
FT   DISULFID    168    208       By similarity.
FT   DISULFID    263    311       By similarity.
SQ   SEQUENCE   324 AA;  36770 MW;  AA1D457183DEC547 CRC64;
     MNKIVLYLLV YGATLGAAYD LLKAPSYFEE FLHKFNKNYS SESEKLRRFK IFQHNLEEII
     NKNQNDTSAQ YEINKFSDLS KDETISKYTG LSLPLQKQNF CEVVVLDRPP DKGPLEFDWR
     RLNKVTSVKN QGMCGACWAF ATLGSLESQF AIKHDQLINL SEQQLIDCDF VDVGCDGGLL
     HTAYEAVMNM GGIQAENDYP YEANNGPCRV NAAKFVVRVK KCYRYVTLFE EKLKDLLRIV
     GPIPVAIDAS DIVGYKRGII RYCENHGLNH AVLLVGYGVE NGIPFWILKN TWGADWGEQG
     YFRVQQNINA CGIKNELPSS AEIY
//