MCA1A_ASPCL
ID MCA1A_ASPCL Reviewed; 429 AA.
AC A1CQZ0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Metacaspase-1A;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=casA; ORFNames=ACLA_027860;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW08061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027059; EAW08061.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001269487.1; XM_001269486.1.
DR AlphaFoldDB; A1CQZ0; -.
DR SMR; A1CQZ0; -.
DR STRING; 5057.CADACLAP00001846; -.
DR EnsemblFungi; EAW08061; EAW08061; ACLA_027860.
DR GeneID; 4702054; -.
DR KEGG; act:ACLA_027860; -.
DR eggNOG; KOG1546; Eukaryota.
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_0000333612"
FT CHAIN ?..429
FT /note="Metacaspase-1A"
FT /id="PRO_0000333613"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 47379 MW; A7DE1A220FFD9457 CRC64;
MQHHHQGSYG GGGGGGGYPG QAYREQNPYG YGQQSPQQGY GAPQQHNGYN QPPSGYGQPQ
HNGGQMYGQR QQGMWLRVRI ASRDRKFLTF ALGQYQNHYS HPHQGGPPPP PSEPVAFGHG
APQGYNFQYS RCTGKRKALM IGINYFGQKG QLRGCINDVK NMSTYLNQNF GYAREDMVLL
TDDQQNPMSQ PTKANILRAM HWLVKDAQPN DSLFFHYSGH GGQTPDLDGD EEDGYDEVIY
PVDFRQAGHI VDDEMHRIMV QPLRPGVRLT AIFDSCHSGS ALDLPYIYST QGILKEPNLA
KEAGQGLLGV VSAYARGDMG SMVSTAVGFL KRAAKGDEAY ERTKQTKTSP ADVIMWSGSK
DSQTSQDAQI AGQATGAMSW AFISALRKNP QQSYVQLLNS IRDELATKYT QKPQLSCSHP
LDTNLLYVM