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Database: UniProt
Entry: J4G1U3_9APHY
LinkDB: J4G1U3_9APHY
Original site: J4G1U3_9APHY 
ID   J4G1U3_9APHY            Unreviewed;       734 AA.
AC   J4G1U3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN   ORFNames=FIBRA_02547 {ECO:0000313|EMBL:CCM00513.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00513.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM00513.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00513.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
CC   -!- SIMILARITY: Belongs to the peptidase C14B family.
CC       {ECO:0000256|ARBA:ARBA00009005}.
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DR   EMBL; HE796987; CCM00513.1; -; Genomic_DNA.
DR   RefSeq; XP_012179796.1; XM_012324406.1.
DR   AlphaFoldDB; J4G1U3; -.
DR   GeneID; 24095424; -.
DR   HOGENOM; CLU_011935_1_0_1; -.
DR   InParanoid; J4G1U3; -.
DR   OrthoDB; 1582860at2759; -.
DR   Proteomes; UP000006352; Unassembled WGS sequence.
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; 3.40.50.1460; -; 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:UP000006352};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          90..353
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          25..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  80528 MW;  35196C35419B78F2 CRC64;
     MFLPFLNITV YDIPQLLWAL LNGRPPSTPI GPQPETPSAP GPGVPASTEP DSATPGAEPL
     PPTGQQPNVP SQGEDLGTEV PLPRPDPRLF ALIIGINNYK YPGVHNLLGA VPDADAVRDY
     LQEQLGVPNS QIINLRDSQA TRAAILHEIN ALMNDKRIQK GDPILIYYSG HGASALAPPN
     WEAGGSHIQL LVPHDQSCID RSGRQVLGIP DRTLGVLLAR LAHEKGDNIS VILDCCHSGS
     GTRTDEIEPT RLVRGIKVEH IPVDLDEEIW ATFQPSSSHD RATAIAAGFT HSGLASHVLL
     AACGAEEFSY EEEGRGLFTK ALVDALVSYG ADKLTYADVV QRMASLPKQN PQCEGVNQSR
     ILFNARAADQ RPLLYKIRKD GNQYLMSAGA AHGVAAEAQF AVYRDWNSSL KGESLGTVTA
     RLPGPFHTIL DAFPKGSDFA LETEGLALQT RAGAEEDLRL HIVMDEMLVT VFEALGKEMQ
     RTDPARRSIM LVEKEKAELD IALENGSVVF NILNPLVTQY GLTRMPFVVE PTVDAVQPVI
     RAAAHFYWHL RRKSAKGVLQ KWVDIEFTQL IDSEEEYDDE LQPVLRPYGP NLNRDNVIDL
     RVKDSARYGL KITNRSNVAL YPALFYFDNS DLSIESYYQP PTANGIVDPP LRGKDSLTIG
     YGDSGSPPQR FFLRDGQKLD VGLLKLFLST EYVDLSHIPQ PSPFGEGRGS TPDPVKPHHI
     WDTILVPLIQ RSVL
//
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