CATV_NPVSE
ID CATV_NPVSE Reviewed; 337 AA.
AC Q9J8B9;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=16;
OS Spodoptera exigua nuclear polyhedrosis virus (strain US) (SeMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=31506;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10567663; DOI=10.1099/0022-1317-80-12-3289;
RA Ijkel W.F.J., van Strien E.A., Heldens J.G.M., Broer R., Zuidema D.,
RA Goldbach R.W., Vlak J.M.;
RT "Sequence and organization of the Spodoptera exigua multicapsid
RT nucleopolyhedrovirus genome.";
RL J. Gen. Virol. 80:3289-3304(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF169823; AAF33546.1; -; Genomic_DNA.
DR RefSeq; NP_037776.1; NC_002169.1.
DR SMR; Q9J8B9; -.
DR MEROPS; C01.083; -.
DR GeneID; 2715768; -.
DR KEGG; vg:2715768; -.
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; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..126
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000322216"
FT CHAIN 127..337
FT /note="Viral cathepsin"
FT /id="PRO_0000050586"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /evidence="ECO:0000250"
FT ACT_SITE 303
FT /evidence="ECO:0000250"
FT DISULFID 147..188
FT /evidence="ECO:0000250"
FT DISULFID 181..221
FT /evidence="ECO:0000250"
FT DISULFID 276..324
FT /evidence="ECO:0000250"
SQ SEQUENCE 337 AA; 38387 MW; 373CC6B53A3024B1 CRC64;
MNKLLILFLL LNAALTRQDN HASANNKPML YNINSAPLYF EKFITQYNKQ YKSEDEKKYR
YNIFRHNIES INQKNSRNDS AVYKINRFAD MPKNEIVIRH TGLASGELGL NFCETIVVDG
PAQRQRPVSF DWRSMNKITS VKDQGMCGAC WRFASLGALE SQYAIKYDRL IDLSEQQLVD
CDFVDMGCDG GLIHTAYEQI MKMGGVEQEF DYSYKAERQP CALKPHKFAT GVRNCYRYVI
LNEERLEDLL RYVGPIAIAV DAVDLTDYYG GIVSFCENNG LNHAVLLVGY GVENNVPYWI
IKNSWGSDYG EDGYVRVRRG VNSCGMINEL ASSAQVV
