ID   A0A319CNP5_9EURO        Unreviewed;       595 AA.
AC   A0A319CNP5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN   ORFNames=BO82DRAFT_360219 {ECO:0000313|EMBL:PYH87106.1};
OS   Aspergillus uvarum CBS 121591.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH87106.1, ECO:0000313|Proteomes:UP000248340};
RN   [1] {ECO:0000313|EMBL:PYH87106.1, ECO:0000313|Proteomes:UP000248340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH87106.1,
RC   ECO:0000313|Proteomes:UP000248340};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C14B family.
CC       {ECO:0000256|ARBA:ARBA00009005}.
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DR   EMBL; KZ821674; PYH87106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319CNP5; -.
DR   VEuPathDB; FungiDB:BO82DRAFT_360219; -.
DR   OrthoDB; 2908943at2759; -.
DR   Proteomes; UP000248340; 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:UniProtKB-KW.
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:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          13..260
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          343..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  66655 MW;  2BCCBDA1A7C821B8 CRC64;
     MESSSERSSS KRALLIASPI HGLRGPLNDV ETIARVLERQ SFQIIRCCGP NATRNGILTA
     WRNLIDTSTT GDAVTIYYSG HGGLVKSSEP DTDIHRPLQF ILPFDYDKST DDDFRGILEI
     ELSHLLLETT EKTDNVTIIL DCCHAGRMAR HPRHGRRANP KRIADVQYRN LRQHLTQLRQ
     SGHLARELDP FGNPNAVRVM AAAATETAWE CEGPEGEWTG ALTNALASAI DEAGQRQVSW
     RSTLLRVHEL VHVQFPQQHP VAEGPDTRLL FATQRIASSA VLLKMQGNDP VLQSGYVSGV
     HKGDVYVLMP AGHEVPDSRF RIGEATVIAL NGFKAKVTVE LDSPGDATHA GPSRMTEVAA
     SSKPNSSDST HPELPGAIPR WVLMCYQQRG ENGHKYAHVR VCRGDRDRQL FQKLKSEYSS
     RLDIRRSFRP VKLMHFTQFK PDSGDYIAAR EDNVWPENGI PDWDIPDSES PAAARLRKIA
     TDSKYLAHRF NLSHENDGCM KWRKLKYALI RGIASAFPRV HDAEAAPTHI GETSVIETIP
     KRLRKEIQYS PTGNPPSWGL IVEEDVDTSV WKRAVKENLI RPRPNRPLGL MRLYF
//