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Database: UniProt
Entry: C3YZ38_BRAFL
LinkDB: C3YZ38_BRAFL
Original site: C3YZ38_BRAFL 
ID   C3YZ38_BRAFL            Unreviewed;       809 AA.
AC   C3YZ38;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Caspase family p20 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BRAFLDRAFT_66918 {ECO:0000313|EMBL:EEN54546.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN54546.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54546.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN54546.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR   EMBL; GG666565; EEN54546.1; -; Genomic_DNA.
DR   RefSeq; XP_002598534.1; XM_002598488.1.
DR   AlphaFoldDB; C3YZ38; -.
DR   STRING; 7739.C3YZ38; -.
DR   eggNOG; KOG3573; Eukaryota.
DR   InParanoid; C3YZ38; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00032; CASc; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR016129; Caspase_his_AS.
DR   InterPro; IPR027417; P-loop_NTPase.
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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        120..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          565..687
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          717..805
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
FT   REGION          687..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  92179 MW;  7AD661CEBEAF822A CRC64;
     MWRQHVMTEQ IFREDKERET YRDVREGEKR GKLPFNRSKV LFVGDTWQGK TSLKKRLTGQ
     EFDPHEGRTE GIQTKMVETQ EVDQTWATRH HNESDYSRSL AWFVAQRSKK RPKKGATKDL
     GSLMKTASFY FVLSFLAVTA LEFGSRVGYA VASLLLTSTI FMMHLNSDFY HVTRIASAIA
     VNSVFIGVMK NGVEDLYQSI GPILSMGPFS LQGFVFCVTV LVDAMKSITT LPRHTAELPT
     YRERHAMLRA QGILDGDFLA EVLNEVKPDH ADVLTTLLVS HDFLCPLPQH PADKKSPLMK
     QRYLVPPMLP RYETDQPGGL FEKHHDDDNV EYYIDFDSFE PSPVFYRLVA KLVCETDFKI
     RARGAPFVFK DRACFQLHRL FYFTLELVRA STDQHLIQIT VKKTSSTAAD GQLIKELHGK
     LEMIRQRDFP CLTYTMGPRC PHPPPHLDHS TEPGAVHVVE VVESGEEFPD STQPLKLLCR
     DREVVVDMSV PTQERSFQPT ASAYAGRCRH SQPSTIVIQE TAPPSDLLPK PDEHGLYDVK
     RWLQVAQDPE SAFDKGECYP MWKRPRGDAL IINNRDFVTM ATRHGTDVDA ENLERLFEAL
     YFTTERWNNL RAPVMKLVLE DFAQRSHAQS QCCLVAILSH GGDEGVYSTD EQLLSHADIL
     SKFDGNNCPD LSSKPKVFFM QACRGTDKDR GSPATDSGET FRKHETARTS PDTHRTFSTR
     VPNLTDVYLA YSTTPGHVSW RDCEGGSWFI QVLVSVFLKY AATKDINQLM TKVNHEVSRK
     FESDKHDKQM PAPVNMLTKD LFFCSGWHR
//
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