CATV_NPVOP
ID CATV_NPVOP Reviewed; 324 AA.
AC O10364;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; ORFNames=ORF125;
OS Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=262177;
OH NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT polyhedrosis virus genome.";
RL Virology 229:381-399(1997).
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; U75930; AAC59124.1; -; Genomic_DNA.
DR RefSeq; NP_046281.1; NC_001875.2.
DR SMR; O10364; -.
DR MEROPS; C01.083; -.
DR GeneID; 912077; -.
DR KEGG; vg:912077; -.
DR Proteomes; UP000009248; Genome.
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_0000322214"
FT CHAIN 114..324
FT /note="Viral cathepsin"
FT /id="PRO_0000050584"
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; 36982 MW; D36A709D6063C15C CRC64;
MNKIMLCLLV CGVVHAATYD LLKAPNYFED FLHKFNKNYS SESEKLHRFK IFQHNLEEII
NKNQNDSTAQ YEINKFSDLS KEEAISKYTG LSLPHQTQNF CEVVILDRPP DRGPLEFDWR
QFNKVTSVKN QGVCGACWAF ATLGSLESQF AIKYNRLINL SEQQFIDCDR VNAGCDGGLL
HTAFESAMEM GGVQMESDYP YETANGQCRI NPNRFVVGVR SCRRYIVMFE EKLKDLLRAV
GPIPVAIDAS DIVNYRRGIM RQCANHGLNH AVLLVGYAVE NNIPYWILKN TWGTDWGEDG
YFRVQQNINA CGIRNELVSS AEIY
