ID   CATV_NPVMC              Reviewed;         337 AA.
AC   Q8QLK1;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   02-SEP-2026, entry version 74.
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   Mamestra configurata nucleopolyhedrovirus (MacoNPV).
OC   Viruses; Viruses incertae sedis; Naldaviricetes; Lefavirales;
OC   Baculoviridae; Alphabaculovirus; Alphabaculovirus maconfiguratae.
OX   NCBI_TaxID=207830;
OH   NCBI_TaxID=174822; Mamestra configurata (bertha armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90/2;
RX   PubMed=11886270; DOI=10.1006/viro.2001.1313;
RA   Li Q., Donly C., Li L., Willis L.G., Theilmann D.A., Erlandson M.;
RT   "Sequence and organization of the Mamestra configurata nucleopolyhedrovirus
RT   genome.";
RL   Virology 294:106-121(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U59461; AAM09141.1; -; Genomic_DNA.
DR   RefSeq; NP_613116.1; NC_003529.1.
DR   AlphaFoldDB; Q8QLK1; -.
DR   SMR; Q8QLK1; -.
DR   MEROPS; C01.083; -.
DR   GeneID; 935864; -.
DR   KEGG; vg:935864; -.
DR   Proteomes; UP000202529; Segment.
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   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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; Reference proteome; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..126
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322213"
FT   CHAIN           127..337
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050583"
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;  37890 MW;  2437696EAA2A1AAC CRC64;
     MNKILILLLL VSAVLTSHDQ VVAVTIKPNL YNINSAPLYF EKFISQYNKQ YSSEDEKKYR
     YNIFRHNIES INAKNSRNDS AVYKINRFAD MTKNEVVNRH TGLASGDIGA NFCETIVVDG
     PGQRQRPANF DWRNYNKVTS VKDQGMCGAC WAFAGLGALE SQYAIKYDRL IDLAEQQLVD
     CDFVDMGCDG GLIHTAYEQI MHIGGVEQEY DYPYKAVRLP CAVKPHKFAV GVRNCYRYVL
     LSEERLEDLL RHVGPIAIAV DAVDLTDYYG GVISFCENNG LNHAVLLVGY GIENNVPYWT
     IKNSWGSDYG ENGYVRIRRG VNSCGMINEL ASSAQIA
//