CATV_NPVAP
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 03-AUG-2022, entry version 65.
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; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=161494;
OH NCBI_TaxID=7119; Antheraea pernyi (Chinese oak silk moth) (Bombyx pernyi).
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 nucleopolyhedrovirus
RT for improvement of baculovirus expression vector 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. 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; AB072731; BAB69773.1; -; Genomic_DNA.
DR RefSeq; YP_611001.1; NC_008035.3.
DR SMR; Q91CL9; -.
DR MEROPS; C01.083; -.
DR GeneID; 5141489; -.
DR KEGG; vg:5141489; -.
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; 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_0000322203"
FT CHAIN 114..324
FT /note="Viral cathepsin"
FT /id="PRO_0000050574"
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; 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
