ID   MCA1B_ASPFC             Reviewed;         408 AA.
AC   B0Y081;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Metacaspase-1B;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=casB; ORFNames=AFUB_035090;
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=EDP52345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS499596; EDP52345.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B0Y081; -.
DR   SMR; B0Y081; -.
DR   PhylomeDB; B0Y081; -.
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_0000333618"
FT   CHAIN           ?..408
FT                   /note="Metacaspase-1B"
FT                   /id="PRO_0000333619"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        199
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  45473 MW;  9443CB353DACB4E5 CRC64;
     MYHRHSAPPP PGWSGGYPPR QQQWPPPQPY EYPPYPPQGP PPAHTFPPPA HRDYPSPYPT
     PPPHSPSPYQ HPHHGHSQSW SVPAVPPRPP LEAQQFGNGA PSHYRFQYSA CTGRRRALLI
     GINYIGQPNQ LRGCINDVTN MSTFLHERYG YRREDMVILT DDQKNPLSIP TKANILRAMQ
     WLVKDAQPND SLFLHFSGHG GRTPDLDGDE EDGYDDVIYP VDYRVAGHIV DDEMHNIMVR
     PLRPGVRLTV IFDSCHSGTA LDLPYVYSTQ GILKEPNLAK EAAQDLFSAI SSYGKGDLSG
     VAMTAIGFLK KAAKGDSARQ RTVMTKTSPA DVVMFSGSKD TQTSADTFQD GEARGALSWA
     FIKSLKQWPN QSYLQLLNSI RAQLDGKYTQ KPQLSCSHPL DVNLLFVM