ID   MCA1_BOTFB              Reviewed;         431 AA.
AC   A6SDT7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Metacaspase-1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=casA; ORFNames=BC1G_11354;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR   EMBL; CH476918; EDN31869.1; -; Genomic_DNA.
DR   RefSeq; XP_001550581.1; XM_001550531.1.
DR   AlphaFoldDB; A6SDT7; -.
DR   SMR; A6SDT7; -.
DR   MEROPS; C14.035; -.
DR   OMA; DFRTAGH; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   SUPFAM; SSF52129; SSF52129; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Hydrolase; Protease; Thiol protease; Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000333636"
FT   CHAIN           ?..431
FT                   /note="Metacaspase-1"
FT                   /id="PRO_0000333637"
FT   REGION          41..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   431 AA;  47160 MW;  A641772DE3424533 CRC64;
     MEAMEHQTSS TRPNPTTRRI KLPPLYAVLL ELSLTLISPQ PAYGAPPPQG GGYGYHQPPP
     PQQPYGYSQP PPQQYGGYNG VPPNAPQYGR PGMPSVNSNA YTNGNQNAPP PPPQGMHAFG
     QGAPQGYAFQ YSNCTGKRKA LLIGINYFGQ RGQLRGCIND VKNMSSYLHE NFGYQRDDMV
     LLTDDQQNPM SQPTKQNILR AMHWLVKDAR PNDSLFFHYS GHGGQTKDLD GDEEDGYDEV
     IYPVDFRQVG HIVDDEMHRI MVQPLQPGVR LTAIFDSCHS GTALDLPYVY STQGVLKEPN
     LAKEAGQGLL GVISSYSQGD MSGVASNLMG FFKKATTGDD AYNKTLATKT SPADVIMWSG
     SKDDQTSADA TIAAQATGAM SWAFITAMKK NPQQSYVQLL NSIRDELATK YTQKPQLSCS
     HPLSMFSPLA L