ID   MCA1_YEAS7              Reviewed;         432 AA.
AC   A6ZP43;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Metacaspase-1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=MCA1; ORFNames=SCY_5258;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Mediates cell death (apoptosis) triggered by oxygen stress,
CC       salt stress or chronological aging. Regulated cell death can prevent a
CC       release of toxic cellular components, thus avoiding necrotic collapse
CC       of the colony, and can also provide nutrients for healthy cells.
CC       Therefore, regulated cell death in yeast colonies can be as important
CC       for their development as are apoptosis and related processes that occur
CC       within metazoa (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN63533.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000032; EDN63533.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZP43; -.
DR   SMR; A6ZP43; -.
DR   MEROPS; C14.035; -.
DR   PRIDE; A6ZP43; -.
DR   TopDownProteomics; A6ZP43; -.
DR   EnsemblFungi; EDN63533; EDN63533; SCY_5258.
DR   HOGENOM; CLU_029389_0_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Cytoplasm; Hydrolase; Nucleus; Protease; Thiol protease;
KW   Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000333675"
FT   CHAIN           ?..432
FT                   /note="Metacaspase-1"
FT                   /id="PRO_0000333676"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  47982 MW;  547D186E3EB481B7 CRC64;
     MYPGSGRYTY NNAGGNNGYQ RPMAPPPNQQ YGQQYGQQYE QQYGQQYGQQ NDQQFSQQYA
     PPPGPPPMAY NRPVYPPPQF QQEQAKAQLS NGYNNPNVNA SNMYGPPQNM SLPPPQTQTI
     QGTDQPYQYS QCTGRRKALI IGINYIGSKN QLRGCINDAH NIFNFLTNGY GYSSDDIVIL
     TDDQNDLVRV PTRANMIRAM QWLVKDAQPN DSLFLHYSGH GGQTEDLDGD EEDGMDDVIY
     PVDFETQGPI IDDEMHDIMV KPLQQGVRLT ALFDSCHSGT VLDLPYTYST KGIIKEPNIW
     KDVGQDGLQA AISYATGNRA ALIGSLGSIF KTVKGGMGNN VDRERVRQIK FSAADVVMLS
     GSKDNQTSAD AVEDGQNTGA MSHAFIKVMT LQPQQSYLSL LQNMRKELAG KYSQKPQLSS
     SHPIDVNLQF IM