CATV_NPVST
ID CATV_NPVST Reviewed; 337 AA.
AC Q91BH1;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=54;
OS Spodoptera litura multicapsid nucleopolyhedrovirus (SpltMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46242;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G2;
RX PubMed=11531416; DOI=10.1006/viro.2001.1056;
RA Pang Y., Yu J., Wang L., Hu X., Bao W., Li G., Chen C., Han H., Hu S.,
RA Yang H.;
RT "Sequence analysis of the Spodoptera litura multicapsid
RT nucleopolyhedrovirus genome.";
RL Virology 287:391-404(2001).
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}.
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DR EMBL; AF325155; AAL01738.1; -; Genomic_DNA.
DR RefSeq; NP_258322.1; NC_003102.1.
DR SMR; Q91BH1; -.
DR MEROPS; C01.083; -.
DR GeneID; 922190; -.
DR KEGG; vg:922190; -.
DR Proteomes; UP000202667; 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; 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; 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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..126
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000322217"
FT CHAIN 127..337
FT /note="Viral cathepsin"
FT /id="PRO_0000050587"
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; 38098 MW; A3C258643D45C379 CRC64;
MYLIYYYTII AVATASIANE KIFYDIDSAS VYYENFIKQH NKEYTTPDQR DAAFVNFKRN
LADMNAMNNV SNQAVYGINK FSDIDKITFV NEHAGLVSNL INSTDSNFDP YRLCEYVTVA
GPSARTPESF DWRKLNKVTK VKEQGVCGSC WAFAAIGNIE SQYAIMHDSL IDLSEQQLLD
CDRVDQGCDG GLMHLAFQEI IRIGGVEHEI DYPYQGIEYA CRLAPSKLAV RLSHCYQYDL
RDERKLLELL YKNGPIAVAI DCVDIIDYRS GIATVCNDNG LNHAVLLVGY GIENDTPYWI
FKNSWGSNWG ENGYFRARRN INACGMLNEF AASAVLL
