MCA1_ASHGO
ID MCA1_ASHGO Reviewed; 452 AA.
AC Q75B43;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Metacaspase-1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=MCA1; OrderedLocusNames=ADL266C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016817; AAS51654.1; -; Genomic_DNA.
DR RefSeq; NP_983830.1; NM_209183.1.
DR AlphaFoldDB; Q75B43; -.
DR SMR; Q75B43; -.
DR STRING; 33169.AAS51654; -.
DR MEROPS; C14.035; -.
DR EnsemblFungi; AAS51654; AAS51654; AGOS_ADL266C.
DR GeneID; 4619965; -.
DR KEGG; ago:AGOS_ADL266C; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_2_1; -.
DR InParanoid; Q75B43; -.
DR OMA; AMIPTRE; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:EnsemblFungi.
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_0000333610"
FT CHAIN ?..452
FT /note="Metacaspase-1"
FT /id="PRO_0000333611"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 50326 MW; 90936BB93F8AADCB CRC64;
MYPGAGRPTY HKQQEQKGPY GQPQYQQQYA PPYPERYQQP YYQPPPHDGY SRPSMPPPSH
NYAAAQYERP SCPPPGYAPH QGGFPAPGPP LQGRPRDLMR SDIQMNHSMD YSNIQGPASY
TRPEFVAPPP QERQFLDPGN RSVEYQYSQC TGNRKALLIG INYFNSSAEL RGCINDVQNI
KNFLISRYGY REENMVILTD DQHDPVRIPT KANILRAMHW LVQGAQPNDS LFLHYSGHGG
ETEDLDGDEQ DGKDSTLYPV DFETNGHIVD DEIHDILVKP LAPGVRLTAL IDACHSGSAL
DLPYMYSTKG IIKEPNVWKD IGSNSMQAAM AYVTGNTGDM FTSLKSLAST VSRKATGSGG
VDTERVRQTK FSPADVIMFS GSKDNQTSAD AVENGVATGA MSYSFVKVMS QQPQQTYLSL
LQNMRTELKG KYTQKPQLSC SHPLDVNLQF VL
