ID   MCA1_PICST              Reviewed;         403 AA.
AC   A3LSY7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Metacaspase-1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=MCA1; ORFNames=PICST_83452;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000498; ABN65975.1; -; Genomic_DNA.
DR   RefSeq; XP_001384004.1; XM_001383967.1.
DR   AlphaFoldDB; A3LSY7; -.
DR   SMR; A3LSY7; -.
DR   STRING; 4924.XP_001384004.1; -.
DR   EnsemblFungi; ABN65975; ABN65975; PICST_83452.
DR   GeneID; 4838642; -.
DR   KEGG; pic:PICST_83452; -.
DR   eggNOG; KOG1546; Eukaryota.
DR   HOGENOM; CLU_029389_0_2_1; -.
DR   InParanoid; A3LSY7; -.
DR   OMA; AMIPTRE; -.
DR   OrthoDB; 821819at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
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; Reference proteome; Thiol protease;
KW   Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000333666"
FT   CHAIN           ?..403
FT                   /note="Metacaspase-1"
FT                   /id="PRO_0000333667"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  43887 MW;  3B18956B192E01F2 CRC64;
     MFPGSGHNTY GGYPPPQGPP PNNNGYNSGP NNSYRQQGYS RPQGPPPGQY DQQSQYSQQS
     QPSAPPQGGT GYGDQSQWGR PTGPPPSGSQ SFGQNSGYTF QYSNCSGRKK ALLVGVNYFG
     SPNELRGCIN DVKNMSSFLV DHWGYQWNDI VILTDDQNDI SRVPTKNNII RAMQWLVKDA
     RPNDSLVFHY SGHGGTTADT DGDEESGYDD VIYPVDFQQA GHIVDDDMHA IMVRPLPPGC
     RLTALYDSCH SGTALDLPYV YSTKGVVKEP NLLKDAGSDA LNAFISYERG NIGGAISSLT
     GLVKKVARQG STNQDQVRQA KFSAADVISI SGCKDDQTSA DAKENGRATG AMSWSFIKVL
     NELPNQSYLS LLNNMRTILA AKYSQKPQLS CSHPQDMNIQ FIM