CATV_NPVMC
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 03-AUG-2022, entry version 62.
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; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC unclassified Alphabaculovirus.
OX NCBI_TaxID=191492;
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}.
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DR EMBL; U59461; AAM09141.1; -; Genomic_DNA.
DR SMR; Q8QLK1; -.
DR MEROPS; C01.083; -.
DR PRIDE; Q8QLK1; -.
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..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
