ID A0A090C865_PODAN Unreviewed; 449 AA.
AC A0A090C865;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Metacaspase {ECO:0000313|EMBL:CDP22321.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP22321.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP22321.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; FO904936; CDP22321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090C865; -.
DR eggNOG; KOG1546; Eukaryota.
DR InParanoid; A0A090C865; -.
DR Proteomes; UP000001197; Chromosome 1.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.12660; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR PANTHER; PTHR48104:SF30; METACASPASE-1; 1.
DR PANTHER; PTHR48104; METACASPASE-4; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022807};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 155..439
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 48608 MW; 1B25D5CBDF0A0EFA CRC64;
MSYGGYPGQG YGPSGGGGGG YQQSPAPQGY GQYPPPQQGY GQPPPQHHQQ GYGQPPPQHG
GYQQGGYQQG GYQQGGYQQQ HGGYQPPQQQ QYYQPPQHPP PPHLDSYGYP TAGGGYGGHR
GQSTRAGPPP PSGHQEFGHG APAGYTFQYS NCTGKRRALL IGINYFGQEG ELRGCINDTK
NLSQYLIENH GYKREDMVIL TDDQTNPVMQ PTKQNIINAM GWLVANAQPN DALFLHFSGH
GGQTEDHDGD EEDGHDEVIY PVDFKENGHI VDDEIHFHVV KPLVEGVRLT AIFDSCHSGS
VLDLPYVYNT KGLLKEPNLA KEAGAGLLSA VGAYARGDMA SVATSIFGLA KSAFKGNDAY
EHTKRTKTSP ADVIMWSGSK DDQTSADATI NSQATGAMSH AFISALKANP QQSYVELLNN
IRDILERDYS QKPQLSCSHP LDTSLLFVM
//
