ID   MCA1A_ASPTN             Reviewed;         403 AA.
AC   Q0CTN3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Metacaspase-1A;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=casA; ORFNames=ATEG_02951;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU36225.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH476597; EAU36225.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001212129.1; XM_001212129.1.
DR   AlphaFoldDB; Q0CTN3; -.
DR   SMR; Q0CTN3; -.
DR   STRING; 341663.Q0CTN3; -.
DR   EnsemblFungi; EAU36225; EAU36225; ATEG_02951.
DR   GeneID; 4317427; -.
DR   eggNOG; KOG1546; Eukaryota.
DR   OrthoDB; 821819at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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_0000333632"
FT   CHAIN           ?..403
FT                   /note="Metacaspase-1A"
FT                   /id="PRO_0000333633"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  44206 MW;  8661A6AA24646C61 CRC64;
     MQHHHHSSYG GGGGGYPGQA YRQQQPYYGQ PSPQPYAQPP PPNYQRPSGY GPPPSGGHMY
     QQGPPAPYQQ HNSYQGGHGR PAPPPTDPVA FGHGAPQGYN FQYSRCTGKR KALLIGINYF
     GQKGQLRGCI NDVKNMSTYL NQNFGYARED MVLLTDDQQN PMSQPTKANI LRAMHWLVKD
     AQPNDSLFFH YSGHGGQTPD LDGDEDDGYD EVIYPVDFRV AGHIVDDEMH RIMVNPLKPG
     TRLTAIFDSC HSGSALDLPY IYSTQGILKE PNLAKEAGQG LLGVVSAYAR GDMGSMVSTA
     VGFLKKAAKG DEAYERTKQT KTSPADVIMW SGSKDSQTSS DAQIQGQATG AMSWAFISAL
     RKNPQQSYVQ LLNSIRDELA TKYSQKPQLS CSHPLDVNLL YVM