CATV_NPVBM
ID CATV_NPVBM Reviewed; 323 AA.
AC P41721; Q80QU5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Bombyx mori nuclear polyhedrosis virus (BmNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=271108;
OH NCBI_TaxID=7091; Bombyx mori (Silk moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T3;
RX PubMed=8083997; DOI=10.1128/jvi.68.10.6619-6625.1994;
RA Ohkawa T., Majima K., Maeda S.;
RT "A cysteine protease encoded by the baculovirus Bombyx mori nuclear
RT polyhedrosis virus.";
RL J. Virol. 68:6619-6625(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3;
RX PubMed=10355780; DOI=10.1099/0022-1317-80-5-1323;
RA Gomi S., Majima K., Maeda S.;
RT "Sequence analysis of the genome of Bombyx mori nucleopolyhedrovirus.";
RL J. Gen. Virol. 80:1323-1337(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZJ-8;
RA Lin X., Zhang Z., Li W., He J., Shang J.;
RT "Sequence analysis and expression of cysteine proteinase gene from Bombyx
RT mori baculovirus.";
RL Can Ye Ke Xue 28:36-40(2002).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9339553; DOI=10.1271/bbb.61.1507;
RA Takahashi S., Ushiyama S., Suzuki T., Ogawa K., Oda K.;
RT "Purification and characterization of cysteine proteinase from a
RT baculovirus gene.";
RL Biosci. Biotechnol. Biochem. 61:1507-1511(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.
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 -!- MISCELLANEOUS: Optimal pH is 4.0, also active at neutral pHs.
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; U12688; AAB49542.1; -; Genomic_DNA.
DR EMBL; L33180; AAC63793.1; -; Genomic_DNA.
DR EMBL; AY182246; AAO23117.1; -; Genomic_DNA.
DR PIR; JC5691; JC5691.
DR RefSeq; NP_047524.1; NC_001962.1.
DR SMR; P41721; -.
DR MEROPS; C01.083; -.
DR GeneID; 1724490; -.
DR KEGG; vg:1724490; -.
DR BRENDA; 3.4.22.50; 891.
DR Proteomes; UP000204315; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..112
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000322204"
FT CHAIN 113..323
FT /note="Viral cathepsin"
FT /id="PRO_0000050575"
FT ACT_SITE 136
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 133..174
FT /evidence="ECO:0000250"
FT DISULFID 167..207
FT /evidence="ECO:0000250"
FT DISULFID 262..310
FT /evidence="ECO:0000250"
FT CONFLICT 166
FT /note="D -> G (in Ref. 3; AAO23117)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="P -> R (in Ref. 3; AAO23117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36922 MW; A8830FCE1D7B00A4 CRC64;
MNKILFYLFV YAVVKSAAYD PLKAPNYFEE FVHRFNKNYS SEVEKLRRFK IFQHNLNEII
NKNQNDSAKY EINKFSDLSK DETIAKYTGL SLPTQTQNFC KVILLDQPPG KGPLEFDWRR
LNKVTSVKNQ GMCGACWAFA TLGSLESQFA IKHNELINLS EQQMIDCDFV DAGCNGGLLH
TAFEAIIKMG GVQLESDYPY EADNNNCRMN SNKFLVQVKD CYRYIIVYEE KLKDLLPLVG
PIPMAIDAAD IVNYKQGIIK YCFDSGLNHA VLLVGYGVEN NIPYWTFKNT WGTDWGEDGF
FRVQQNINAC GMRNELASTA VIY
