MCA1A_ASPNC
ID MCA1A_ASPNC Reviewed; 404 AA.
AC A2RB75;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Metacaspase-1A;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=casA; ORFNames=An18g05760;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK97495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM270409; CAK97495.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A2RB75; -.
DR SMR; A2RB75; -.
DR MEROPS; C14.035; -.
DR PaxDb; A2RB75; -.
DR EnsemblFungi; CAK97495; CAK97495; An18g05760.
DR Proteomes; UP000006706; Chromosome 8L.
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_0000333624"
FT CHAIN ?..404
FT /note="Metacaspase-1A"
FT /id="PRO_0000333625"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 44268 MW; 9374D0BCCD4BC999 CRC64;
MNPHHSHHHS SYGGGGYPGQ AYRQQQPPSN PYQYNQPSPQ PYQGSQPPQN GYNGGYPAAS
QGPMYGGRPG IADVYHNSYN QGNHSAPAPP PSDPVSFGQG APQGYNFQYS RCTGKRKALL
IGINYFNQKG QLRGCINDVK NMSTYLNQNF GYAREDMVVL TDDQQNPMSQ PTKANILRAM
HWLVKDAQPN DSLFFHYSGH GGQTPDLDGD EDDGYDEVIY PVDFRAAGHI VDDEMHRIMV
KPLQPGVRLT AIFDSCHSGS ALDLPYIYST QGILKEPNLA KEAGQGLLGV VSAYARGDMS
SMMSTAVGFF KKATKGDEAY ERTIQTKTSP ADVVMWSGSK DDQTSQDAQI AGQATGAMSW
AFISALRKNP QQSYVQLLNS IRDELSAKYT QKPQLSCSHP LVAL