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Database: UniProt
Entry: U4LW63_PYROM
LinkDB: U4LW63_PYROM
Original site: U4LW63_PYROM 
ID   U4LW63_PYROM            Unreviewed;       442 AA.
AC   U4LW63;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Similar to Metacaspase-1A acc. no. B0XPP3 {ECO:0000313|EMBL:CCX33246.1};
GN   ORFNames=PCON_14286 {ECO:0000313|EMBL:CCX33246.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX33246.1};
RN   [1] {ECO:0000313|EMBL:CCX33246.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX33246.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX33246.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- SIMILARITY: Belongs to the peptidase C14B family.
CC       {ECO:0000256|ARBA:ARBA00009005}.
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DR   EMBL; HF936042; CCX33246.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4LW63; -.
DR   eggNOG; KOG1546; Eukaryota.
DR   OMA; MHRIMVT; -.
DR   OrthoDB; 1077459at2759; -.
DR   Proteomes; UP000018144; 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; 3.40.50.12660; -; 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   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          148..433
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..82
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  48558 MW;  A1B1284169C53B9F CRC64;
     MSGGYPGQYS GYPGQHHGQH PQYPPQQQYP PQGYPPQQGY YPPPNSAPPQ GYYPPPAGAP
     PQQGGYYPPP GSAPPQQWAP PPQGYPQQQS MTPTTHRGNN SDRNKVPTYQ NAYVNHQPGA
     PPPPPTGQTS FGVPGSDYSY SYSNCSGKRK ALLIGINYFG QKGQLRGCIN DVKNMSKFLH
     DRFQYKWDDM VILTDDQQHP KSQPTKQNIL AAMHWLVKDA QPNDSLFFHY SGHGGQTKDL
     DGDEGDGYDE TIYPLDFRYT GHIVDDEMHR IMVQPLKPGV RLTAIFDSCH SGSVLDLPYL
     YSTSGKQKEP NLAREAGMGL FGALQAYSKG DLNGVAASAM SIAKRLTTGR SAEEKAMRTK
     TSPADVIQWS GSKDSQTSAD ATEGGQATGA MSYAFIKALT KNPQQSYAQL LNSIRDELSQ
     KYSQKPQLSC SHPLDTNLLY VM
//
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