ID   MCA1B_ASPCL             Reviewed;         410 AA.
AC   A1CL82;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Metacaspase-1B;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=casB; ORFNames=ACLA_041220;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR   EMBL; DS027056; EAW09906.1; -; Genomic_DNA.
DR   RefSeq; XP_001271332.1; XM_001271331.1.
DR   AlphaFoldDB; A1CL82; -.
DR   SMR; A1CL82; -.
DR   STRING; 5057.CADACLAP00003197; -.
DR   EnsemblFungi; EAW09906; EAW09906; ACLA_041220.
DR   GeneID; 4702762; -.
DR   KEGG; act:ACLA_041220; -.
DR   VEuPathDB; FungiDB:ACLA_041220; -.
DR   eggNOG; KOG1546; Eukaryota.
DR   HOGENOM; CLU_029389_0_2_1; -.
DR   OMA; PTKANMI; -.
DR   OrthoDB; 821819at2759; -.
DR   Proteomes; UP000006701; 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_0000333614"
FT   CHAIN           ?..410
FT                   /note="Metacaspase-1B"
FT                   /id="PRO_0000333615"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..71
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   410 AA;  45568 MW;  E0E678C2DF2C84F3 CRC64;
     MYHRNSAPPP PGWSGGYPPP QSQWPPHSYQ YPPYPPQGPP PPPAHSYSPP PTYGNYPSPY
     STPPPHSPSP YQHPQHGHSR SWTNPSLPPR PPRESQSFGK GAPSNYRFQY SECTGRRRAL
     LIGINYIGQP NQLRGCINDV TNMSTFLHER FGYRREDMVI LTDDQKNPMS VPTKINILRA
     MQWLVKDAQP NDSLFIHFSG HGGRTPDLDG DEEDGYDDVI YPVDYRVAGH IVDDEMHNIM
     VRPLQPGVRL TAIFDSCHSG TALDLPYVYS TQGILKEPNL AKEAAQDLFS ALASYGKGDL
     SGVAMTAIGF LKKAAIGDSA RQRTVMTKTS PADVVMFSGS KDTQTSADTF QDGEARGALS
     WAFIKSQKQR PNQSYLQLLN SIRAELEGKY TQKPQLSCSH PLDVNLLFVM