ID   MCA1_AJECN              Reviewed;         356 AA.
AC   A6R7B8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Metacaspase-1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=MCA1; ORFNames=HCAG_05526;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476659; EDN09027.1; -; Genomic_DNA.
DR   RefSeq; XP_001540059.1; XM_001540009.1.
DR   AlphaFoldDB; A6R7B8; -.
DR   SMR; A6R7B8; -.
DR   STRING; 339724.A6R7B8; -.
DR   MEROPS; C14.035; -.
DR   EnsemblFungi; EDN09027; EDN09027; HCAG_05526.
DR   GeneID; 5445806; -.
DR   KEGG; aje:HCAG_05526; -.
DR   VEuPathDB; FungiDB:HCAG_05526; -.
DR   HOGENOM; CLU_029389_0_2_1; -.
DR   OMA; DFRTAGH; -.
DR   OrthoDB; 821819at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:EnsemblFungi.
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; Reference proteome; Thiol protease;
KW   Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000333608"
FT   CHAIN           ?..356
FT                   /note="Metacaspase-1"
FT                   /id="PRO_0000333609"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  38758 MW;  85F835FE8DF6D016 CRC64;
     MYSGRSGAPP PAHSPYPNSY NHGPPGHSAG HNVPPPPPTQ PVQFGHGAPQ GYSFQYSNCT
     GKRKALLIGI NYFGQRGQLR GCINDVKNMS TYLNQNFGYA REDMVILTDD QQNPMSQPTK
     ANILRAMHWL VKDARPNDSL FFHYSGHGGQ TKDLDGDEED GNDEVIYPVD FRSAGHIVDD
     EMHRIMVKSL LPGVRLTAIF DSCHSGSALD LPYIYSTQGI LKEPNLAKEA GQGLLSVVSA
     YARGDVSGML STVGGLIKKA TSGDASHSKA RQTKTSPADV IMWSGSKDNQ TSQDATIAGE
     ATGAMSWAFI TALKKNPQQS YVQLLRSIRD ELATKYSQKP QLSCSHPLNT DLLYVM