CATV_NPVLD
ID CATV_NPVLD Reviewed; 356 AA.
AC Q9YMP9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Lymantria dispar multicapsid nuclear polyhedrosis virus (LdMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=10449;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Cl 5-6;
RX PubMed=9887315; DOI=10.1006/viro.1998.9469;
RA Kuzio J., Pearson M.N., Harwood S.H., Funk C.J., Evans J.T., Slavicek J.M.,
RA Rohrmann G.F.;
RT "Sequence and analysis of the genome of a baculovirus pathogenic for
RT Lymantria dispar.";
RL Virology 253:17-34(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}.
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DR EMBL; AF081810; AAC70264.1; -; Genomic_DNA.
DR PIR; T30426; T30426.
DR RefSeq; NP_047715.1; NC_001973.1.
DR SMR; Q9YMP9; -.
DR MEROPS; C01.083; -.
DR GeneID; 1488519; -.
DR KEGG; vg:1488519; -.
DR Proteomes; UP000203997; 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; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT PROPEP 41..144
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000322212"
FT CHAIN 145..356
FT /note="Viral cathepsin"
FT /id="PRO_0000050582"
FT ACT_SITE 168
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /evidence="ECO:0000250"
FT DISULFID 165..206
FT /evidence="ECO:0000250"
FT DISULFID 199..239
FT /evidence="ECO:0000250"
FT DISULFID 295..343
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39770 MW; AFC3584B37D91611 CRC64;
MYANALVCLN PSFIKLQFHI VCTMNIIGIV TLALCSAASA ADEGAAYNLQ RAPDYFESFV
ENYNKNYTSD WEKNKRYSIF KDNLHEINAK NGNATDGPTA TYKINKFSDL SKSELIAKFT
GLSIPERVSN FCKTIILNQP PDKGPLHFDW REQNKVTSIK NQGACGACWA FATLASVESQ
FAMRHNRLID LSEQQLIDCD SVDMGCNGGL LHTAFEEIMR MGGVQTELDY PFVGRNRRCG
LDRHRPYVVS LVGCYRYVMV NEEKLKDLLR AVGPIPMAID AADIVNYYRG VISSCENNGL
NHAVLLVGYG VENGVPYWVF KNTWGDDWGE NGYFRVRQNV NACGMVNDLA STAVLA
