ID   MCA1A_ASPFC             Reviewed;         413 AA.
AC   B0XPP3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Metacaspase-1A;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=casA; ORFNames=AFUB_007090;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Involved in cell death (apoptosis) (By similarity). Required
CC       for the apoptotic-like loss of membrane phospholipid asymmetry at
CC       stationary phase and facilitates growth under conditions of endoplasmic
CC       reticulum stress. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP56007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS499594; EDP56007.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B0XPP3; -.
DR   SMR; B0XPP3; -.
DR   PhylomeDB; B0XPP3; -.
DR   Proteomes; UP000001699; 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; Thiol protease; Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000333616"
FT   CHAIN           ?..413
FT                   /note="Metacaspase-1A"
FT                   /id="PRO_0000333617"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..61
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  45199 MW;  571774D794E201D5 CRC64;
     MQNHHHQQSS YGGGYPGQAY REQHPPPNPY GYGQPSPQPG YGAPPPHNGY GQPPSGYGQP
     PPPTGNAVYG GRQPGMNQYQ NTYSHGHQGG PPPPPTDPVA FGHGAPQGYS FQYSRCTGKR
     KALLIGINYF GQKGQLRGCI NDVKNMSTYL NQNFGYARED MVLLTDDQQN PMSQPTKANI
     LRAMHWLVKD AQPNDSLFFH YSGHGGQTPD LDGDEEDGYD EVIYPVDFRQ AGHIVDDEMH
     RIMVRPLRPG VRLTAIFDSC HSGSALDLPY IYSTQGILKE PNLAKEAGQG LLGVVSAYAR
     GDMSGMVSTA VGFLKRATKG DEAYTRSKQT KTSPADVIMW SGSKDSQTSQ DAQIGGQATG
     AMSWAFITAL RKNPQQSYVQ LLNSIRDELA TKYSQKPQLS CSHPLDTNLL YVM