MCA1_EMENI
ID MCA1_EMENI Reviewed; 404 AA.
AC Q8J140; C8VFM8; Q5B168;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Metacaspase-1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=casA; ORFNames=AN5712;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12482970; DOI=10.1128/mcb.23.1.163-177.2003;
RA Cheng J., Park T.-S., Chio L.-C., Fischl A.S., Ye X.S.;
RT "Induction of apoptosis by sphingoid long-chain bases in Aspergillus
RT nidulans.";
RL Mol. Cell. Biol. 23:163-177(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF81352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF528964; AAO13381.1; -; mRNA.
DR EMBL; AACD01000098; EAA62805.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81352.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_663316.1; XM_658224.1.
DR AlphaFoldDB; Q8J140; -.
DR SMR; Q8J140; -.
DR STRING; 162425.CADANIAP00003350; -.
DR EnsemblFungi; EAA62805; EAA62805; AN5712.2.
DR GeneID; 2872002; -.
DR KEGG; ani:AN5712.2; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_2_1; -.
DR InParanoid; Q8J140; -.
DR OrthoDB; 821819at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; 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 2: Evidence at transcript level;
KW Apoptosis; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000333648"
FT CHAIN ?..404
FT /note="Metacaspase-1"
FT /id="PRO_0000333649"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 44598 MW; 67B2DFAD0486F994 CRC64;
MHHHHQQPSY GSGYPGQAYR QQQNPYPQYG HPSPQPYPPQ NGYSHPSSGY PPSPAPPNGG
QMYHGRQPSY PPNQYPPAHG GPTAPPTNPQ AFGHGAPQGY NFQYSRCTGK RKALLIGINY
FGQKGQLRGC INDVKNMSTY LNQNFGYARE DMVILTDDQQ NPMSQPTKAN ILRAMHWLVK
DAQPNDSLFF HYSGHGGQTP DLDGDEDDGY DEVIYPVDFR VAGHIVDDEM HRIMVKPLQP
GVRLTAIFDS CHSGSALDLP YIYSTQGILK EPNLAKEAGQ GLLGVISSYA RGDMGGMMST
AVGFLKKAAK GDEAYQRTKQ TKTSPADVIM WSGSKDDQTS QDAQIAGQAT GAMSWAFITA
MRKNPQQSYV QLLNSIRDEL STRYTQKPQL SSSHPLDVNL LYVM
