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Database: UniProt
Entry: C3ZU23_BRAFL
LinkDB: C3ZU23_BRAFL
Original site: C3ZU23_BRAFL 
ID   C3ZU23_BRAFL            Unreviewed;       851 AA.
AC   C3ZU23;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=DED domain-containing protein {ECO:0000259|PROSITE:PS50168};
GN   ORFNames=BRAFLDRAFT_87286 {ECO:0000313|EMBL:EEN43909.1};
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:EEN43909.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43909.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN43909.1};
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).
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DR   EMBL; GG666681; EEN43909.1; -; Genomic_DNA.
DR   RefSeq; XP_002587898.1; XM_002587852.1.
DR   AlphaFoldDB; C3ZU23; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; C3ZU23; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd00045; DED; 1.
DR   CDD; cd05819; NHL; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR001875; DED_dom.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR049341; TRADD-like_N.
DR   PANTHER; PTHR10680:SF28; DED DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10680; PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE; 1.
DR   Pfam; PF01335; DED; 1.
DR   Pfam; PF01436; NHL; 2.
DR   Pfam; PF20694; TRADD-like_N; 1.
DR   SMART; SM00031; DED; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   PROSITE; PS50168; DED; 1.
DR   PROSITE; PS51125; NHL; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          18..96
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   REPEAT          584..627
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          768..811
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          100..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          370..450
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        115..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  94581 MW;  6A3DAEB82CB2A060 CRC64;
     MASPVRERVT DADRRHFDFV KTLLRISDEL TEEETANLKI FCLHLIPKGH LAQLRRAMDV
     FVKLMELDKI DRENLDFLKE ILEGIGRQDL IRDVLRQFQP PDREIPENPD LQPENPGLQP
     ENTDLQPENP DLQPENPDLQ PENPDLQPEN PDLQPENPDL QPQNSELQPQ NPELQPGDPE
     IQSGQSNAEG ANEEGDATSN IYVVVHGQVR MIQEALDRLK GDLARLSGTR RSQVMYRGHK
     KHKSILVHFS IPRENTAVLR HMADHSDPRL VYMGIKYLQI DAEVPIKVQQ EEPVYDIKRQ
     LPVDDIEVGC STRTKHQKAP QSWSRLSALN LFSDALPLHL QAAASLEYQG FSYSLVRALV
     QKDRLREHQM RQAIQNLRNA EVDSNTLRQK AEVDSNTLRQ KAEADSNTIM TLRSKLNITE
     NRLKEALETI AVLQEKMKQA QEYAENAAKH VTSHVTEYRG EKPPGGWAQE YRGEKSPGGS
     PLEYRGEKPP GGWSSQVEKA DSATQTHQTD PFGTTGIPGD VGGDKVGADP TVKEEVGKTP
     TQDSGSGSNG KEDVLGTEAL EQERQTAGTA GTASGSTGDR KQRVITFGVM GTEPRQFLDP
     RGVVVSPSNE IFVANRGNER VQVRSTEGVY LRHFPTVVPG TGDKVMVPHD VCMDANGTLW
     VVGRGQTADH VVQYSTDGTA MAGFDLEKIG YFRGIAVNMR TNHILVTDAD QGEVHVFRPD
     GSLVRTVRHP RAGKTRPRYI TVDGEGNILV SDWNNNYVYM YDESGEFLFQ FGGEGSGEGQ
     LSGPSGICTD SSGHILVADS GNGRIQIFTR HGEFVRTVST GFTPYGLAVG PEGQLVVTNY
     WKHTVTVYPN Y
//
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