ID A0A3B0JKG0_DROGU Unreviewed; 521 AA.
AC A0A3B0JKG0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Blast:Caspase-3 {ECO:0000313|EMBL:SPP75840.1};
GN ORFNames=DGUA_6G003721 {ECO:0000313|EMBL:SPP75840.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP75840.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR EMBL; OUUW01000001; SPP75840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0JKG0; -.
DR STRING; 7266.A0A3B0JKG0; -.
DR OMA; FMSTRQT; -.
DR OrthoDB; 3581637at2759; -.
DR Proteomes; UP000268350; 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; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR47901; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 18; 1.
DR PANTHER; PTHR47901:SF8; CASPASE-3; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 3: Inferred from homology;
FT DOMAIN 311..427
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 445..519
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 56365 MW; CD1AD23CDB1101A1 CRC64;
MGWWGKKRDE QETDRSSGSA ASQALVLQDP RTRVKTTSAA TATTNTAVQN STITDSNKKT
ITFMSTRKTV THTQRALITE TTTRRTPSQA ELELLFAQMR MGGDGATTTT TTTSTSRGRP
PSLNGVAIRS TPSFKATTNN KRSSTVLKTE HTTVTKKNGR NVTQHVETQR VDLKAKGKPS
WPPSFFASNN SGSTSEPYVS PYAQKPSLAI TYVSPYAKST TGTSTSTSSS TGSVAGAPSG
SKAFKPTSKS LFSTNVPRSF TSIAASTGAT PKTTVGAHDA HGVGKSKLLA GVGTAKPIVA
KTKLKPARVY IFNNEKFDSK NEFRSGSAQD VKVLRNTFEQ LKCKVEVIKD ATLATVKSTV
RMLETKDFED KSALVLVFLS HGTRHDRLAA KDLDYSLDDD VLFPILRNRT LKDKPKMLFV
QACKGANEPG GFMTDSAQPN GSPNEILKCY STYEGYVSYR TEDGTPFIQT LCEALNRSGK
TTDIDGIMMS VRSVVKMQTK DGQIPSVTST LTSKYVFGDY V
//
