ID   CATV_GVXN               Reviewed;         346 AA.
AC   Q9PYY5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=58;
OS   Xestia c-nigrum granulosis virus (XnGV) (Xestia c-nigrum granulovirus).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Betabaculovirus.
OX   NCBI_TaxID=51677;
OH   NCBI_TaxID=320016; Xestia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10502508; DOI=10.1006/viro.1999.9894;
RA   Hayakawa T., Ko R., Okano K., Seong S.I., Goto C., Maeda S.;
RT   "Sequence analysis of the Xestia c-nigrum granulovirus genome.";
RL   Virology 262:277-297(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; AF162221; AAF05172.1; -; Genomic_DNA.
DR   RefSeq; NP_059206.1; NC_002331.1.
DR   SMR; Q9PYY5; -.
DR   MEROPS; C01.047; -.
DR   GeneID; 1442292; -.
DR   KEGG; vg:1442292; -.
DR   Proteomes; UP000202921; 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..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..133
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322219"
FT   CHAIN           134..346
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050589"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        154..195
FT                   /evidence="ECO:0000250"
FT   DISULFID        188..228
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  38819 MW;  4B82DB0376C7C951 CRC64;
     MLFFNFYKHI MFLPWVFCVA LLTLNVCAVS YIAYDMSNAQ ELFNEFVVKY NKVYKDDQEK
     EARFEIFKQN LADINARNAL EDSAMFEINS RADISSNELL QKLTGLKLSL MRGEKKNSFC
     TPTVISGDSS GKVPDSFDWR DRNSVTSVKM QKECGSCWAF SAVANIESLY HIKHNVSLDL
     SEQQLVDCDK VNNGCNGGLM SWAFEGIIRA GGISYEAPYP YTGVDGVCKN TTRYVQLSGC
     YAYDLRSEKK LRQVLHEKGP VSVAIDVVDL TNYKSGVAKH CSVDHGLNHG VLLVGYGQEN
     DVKYWTLKNS WGSDWGEQGF FRIKRDVNSC GILNQFAASA ILSSSS