ID   CASP_SFAVA              Reviewed;         288 AA.
AC   Q5K5C1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Executioner caspase;
DE            EC=3.4.22.-;
GN   ORFNames=ORF73;
OS   Spodoptera frugiperda ascovirus 1a (SfAV-1a).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Ascovirus.
OX   NCBI_TaxID=113370;
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14573805; DOI=10.1099/vir.0.19290-0;
RA   Stasiak K., Renault S., Demattei M.V., Bigot Y., Federici B.A.;
RT   "Evidence for the evolution of ascoviruses from iridoviruses.";
RL   J. Gen. Virol. 84:2999-3009(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=15933068; DOI=10.1101/gad.1300205;
RA   Bideshi D.K., Tan Y., Bigot Y., Federici B.A.;
RT   "A viral caspase contributes to modified apoptosis for virus
RT   transmission.";
RL   Genes Dev. 19:1416-1421(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16987980; DOI=10.1128/jvi.01639-06;
RA   Bideshi D.K., Demattei M.V., Rouleux-Bonnin F., Stasiak K., Tan Y.,
RA   Bigot S., Bigot Y., Federici B.A.;
RT   "Genomic sequence of Spodoptera frugiperda Ascovirus 1a, an enveloped,
RT   double-stranded DNA insect virus that manipulates apoptosis for viral
RT   reproduction.";
RL   J. Virol. 80:11791-11805(2006).
CC   -!- FUNCTION: May induce host cell apoptosis and contribute of the
CC       establishment of a special cell cleavage process in which apoppotic
CC       bodies are rescued by the virus and differentiate to form large
CC       vesicles in which virion assembles. {ECO:0000269|PubMed:15933068}.
CC   -!- INDUCTION: Synthesized 9 hours after infection of cells ex vivo.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR   EMBL; AJ437059; CAD24627.1; -; Genomic_DNA.
DR   EMBL; AJ620301; CAF04324.1; -; Genomic_DNA.
DR   EMBL; AM398843; CAL44673.1; -; Genomic_DNA.
DR   RefSeq; YP_762428.1; NC_008361.1.
DR   SMR; Q5K5C1; -.
DR   MEROPS; C14.037; -.
DR   GeneID; 4306239; -.
DR   KEGG; vg:4306239; -.
DR   Proteomes; UP000008030; Genome.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR037554; Caspase_6.
DR   InterPro; IPR002398; Pept_C14.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR10454; PTHR10454; 1.
DR   PANTHER; PTHR10454:SF206; PTHR10454:SF206; 1.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; SSF52129; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..288
FT                   /note="Executioner caspase"
FT                   /id="PRO_0000329067"
FT   ACT_SITE        131
SQ   SEQUENCE   288 AA;  32639 MW;  0F532A743E22AD3B CRC64;
     MSICYYDTVG REKRLLIINQ RALALPNRTI SSDGTCCDGD EYLLVDTFTK LNFKVQTIRN
     ASKIVLETTV RNYIEKNVKR VACYFVVVLN DGNDADTILT TDGTYSLSEL YALFTLYTVR
     AIPKVFLIQS CLGAKIDRSH CDRASCQCDQ EEDAHPTSVC HDIFVNTVRR VIHACSRKSN
     GSTTTTETKC SDVATVVLTS PHTEETIIVY LRIEAYLRYG DTKCGCFMIE KFCKNLIKYG
     TRSSVHTTIT MVQNEMQITD PKHVPIVQMN CTKLLFLGDE NHIIMEEY