ID   CATV_NPVBS              Reviewed;         331 AA.
AC   Q9YWK4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-MAR-2009, entry version 45.
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   Buzura suppressaria nuclear polyhedrosis virus (BsNPV).
OC   Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=74320;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99036048; PubMed=9820162;
RA   Hu Z.H., Arif B.M., Jin F., Martens J.W.M., Chen X.W., Sun J.S.,
RA   Zuidema D., Goldbach R.W., Vlak J.M.;
RT   "Distinct gene arrangement in the Buzura suppressaria single-
RT   nucleocapsid nucleopolyhedrovirus genome.";
RL   J. Gen. Virol. 79:2841-2851(1998).
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; AF058929; AAC77812.1; -; Genomic_DNA.
DR   HSSP; P80067; 1JQP.
DR   MEROPS; C01.083; -.
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; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22    116       Activation peptide (Potential).
FT                                /FTId=PRO_0000322205.
FT   CHAIN       117    331       Viral cathepsin.
FT                                /FTId=PRO_0000050576.
FT   ACT_SITE    140    140       By similarity.
FT   ACT_SITE    274    274       By similarity.
FT   ACT_SITE    294    294       By similarity.
FT   DISULFID    137    178       By similarity.
FT   DISULFID    171    211       By similarity.
FT   DISULFID    267    315       By similarity.
SQ   SEQUENCE   331 AA;  37744 MW;  6DB980A418FA2BBC CRC64;
     MKKLVICIIL NLIVAKNYAF AYDLLKAGDY FETFLANYNK MYNDTSEKER RFSIFQQTLE
     EINYKNRLND SAVYQINKFA DLSKNEIISK YTGLNMPVQT TNFCKTIVID QPPGKGPLNF
     DWRQQNKVTS IKNQKACGAC WAFATLASIE SQYAIKNNVH IDLSEQQMID CDYVDMGCDG
     GLLHTAFEQM IQMGELVQEH EYPYAGVNKP CELRGDETGV VKVKGCYRYV VFREEKLKDL
     LRAVGPIPMA IDASGIVNYH HGIIHYCENY GLNHAVLLVG YGVENNVPFW TFKNTWGKDW
     GEEGYFRVRQ NVDACGMTNE LASSAVIDWD A
//