ID   A0A2J6TJA3_9HELO        Unreviewed;       519 AA.
AC   A0A2J6TJA3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN   ORFNames=K444DRAFT_609971 {ECO:0000313|EMBL:PMD63094.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD63094.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD63094.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD63094.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ613782; PMD63094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6TJA3; -.
DR   InParanoid; A0A2J6TJA3; -.
DR   OrthoDB; 2695256at2759; -.
DR   Proteomes; UP000235371; Unassembled WGS sequence.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   Pfam; PF00656; Peptidase_C14; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000235371}.
FT   DOMAIN          91..252
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..336
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  59033 MW;  689EFEB9EF1DF159 CRC64;
     MASSSSPTVI AGRAKQTPPR EIPALTTTQP SSGASVPHKI DYLEKRVQEE ANYQVQWSKW
     MSDGQQKSFY KHVFVLLLSW HPECDDMEVD LEVQRLKSVF EDIYNYNVES IQLDCRKDAT
     PQAQANLAVA NFVHLNDKED ALFVVYYAGH GSPGKERGLL NMTGRRRQKG KRLAQQFTHI
     TWNLVENNLK TTRADVFQIF DCCHSSDLGR DSALNSRSFE YLAASTTPYT RSPGKSSFTS
     ALIWALEKLA HQSPREDSQW SPMFTTSKLA KKISECPDFP EEQNPSLTTR DVEAWQHIIL
     APLPREGVSA LTPAPNSEDE DGNEDEDEDE EEEEDNKPVQ QFLSLTFHFK HKEDESELLK
     KLADHLKKFM KLEPSLHKVQ WGGIWGELRP PPGHRWREAV RKVMSKSPVS RFPSNLVQSG
     SLSPQTGHLL PSSSTESTPL LSDASSVKFK EELTTRSLWS HISSFFRNFR KPNLAEPQGQ
     PASTVSNPGR QDSRKWTRRL ADKLRNLFYR PLPRIQISS
//