MCA1B_ASPNC
ID MCA1B_ASPNC Reviewed; 438 AA.
AC A2QU58;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Metacaspase-1B;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=casB; ORFNames=An09g04470;
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}.
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DR EMBL; AM270200; CAK40301.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QU58; -.
DR SMR; A2QU58; -.
DR PaxDb; A2QU58; -.
DR EnsemblFungi; CAK40301; CAK40301; An09g04470.
DR HOGENOM; CLU_029389_0_2_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
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_0000333626"
FT CHAIN ?..438
FT /note="Metacaspase-1B"
FT /id="PRO_0000333627"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 48738 MW; ED5AB4B420634FBE CRC64;
MYYHHSHQGW SGDYPRQQSW GQPPPSSYPY PYSSNAQYQP PPGPPPTSHY APPPGPPPSH
YYPPPGSYPS PAPSPYYGQH HTPTPPPQSS SPHQRSYHNH SPSWGQNLPP RPPQESQHFG
RGAPSNYRFQ YSNCTGRRKA LLIGINYIGQ PNQLRGCIND VTNMSTFLNE KYGYRREDMV
ILTDDQKNPM SIPNKANILR AMQWLVKDAQ PNDSLFIHFS GHGGRTPDLD GDEEDGYDDV
IYPLDYRTAG HIVDDDMHAI MVRPLRPGVR LTAIFDSCHS GTALDLPYVY STQGILKEPN
LAKEAAMDLF SAINSYGKGD LSSVAQTAIG FFKKAANGDT ARQRTVMTKT SPADVVMFSG
SKDTQTSADT FQDGEARGAL SWAFIKTLQQ RPNQSYLQLL NSIRNELEGK YTQKPQLSCS
HPLGMCNASL VPPRTEID