ID C3ZU40_BRAFL Unreviewed; 965 AA.
AC C3ZU40;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DED domain-containing protein {ECO:0000259|PROSITE:PS50168};
GN ORFNames=BRAFLDRAFT_87303 {ECO:0000313|EMBL:EEN43926.1};
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:EEN43926.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43926.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43926.1};
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; EEN43926.1; -; Genomic_DNA.
DR RefSeq; XP_002587915.1; XM_002587869.1.
DR AlphaFoldDB; C3ZU40; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3ZU40; -.
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 Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
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; 1.
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; 3.
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 67..145
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT REPEAT 699..742
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 805..835
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 883..926
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 147..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 386..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 108580 MW; F4FF9A690C1E8234 CRC64;
MVNGWGVVCL EAFDADGCEI ISLLQTCNKY IQSPFGYLYF DVVSFFRMAG PAREIEGFTD
EDRRHFEFVR PLILISDSLT KKETDDVKIY CAHVIPKGMI KGLKRAVDIF LKLKEIGKIN
QENLDFVEEV LEMIGRRDLA RDVLRPAQQP DRAVPENPEL QPEIPELQPD NPEPQPGPSQ
EEARAEETPM SNIYTVVHGH SSMTQETVDR HRQNIASACN TRRSQVKFRG YKKHKSILVH
FSIPRENTAV LRHMADHSDP RLVYMGVKSL QIDAEVPIKV QQEAPLYDIK RQLSVDDIEV
GCSTRTKHQR APHSWTRLSA LNLFSDALPL HLQAAASLEY QGFSYSLVRA LAQKDRLREH
QMRQAIQNLR NAEVDSNTLR QKARVDSNTL RQKAEVDSNT LRQKAEVDSN TLRQKAEADS
NTLRQKAEVD SNTIMTLRSK LNISENRLKE ALETNEILEE KLQQAQEYAE KAAKQVTSHV
TEYRGEKPPG GWPQEYRGEK PPGGWSQEYR GEKPPGGWLQ EYRGEKPSGG WPLEYRGEKP
LGGWPQEYRG EKPPGGWQQE YMGEKPPGGW PQEYRGEKPP GGWQQEYMGE KPPGGWPQEY
RGERPPGGWS AQVEKADSAT QTHLAGAVGT TVIPGDVDDK LGEDPIIKEE DMTVERQVSE
RGIYERQDVL GTKSPEQERH TAGIEGSASR STGELEQSVI IFGGEGSKPG KFSYPRGVVV
SPSNEIFVVD RLNRRVQVHS TEGVYLRHFP TAVPGTGKDM QPHDVCMDGN GTLWVVGRGE
TAHHVVQYST DGTAMAGFDL KKSHDYPRGI AVDMRTNHIL VTDPDQGEVH VFRPDGSLVR
TVRHPRGEMV HPRYVTVDGE GNILVSDWDT HYVYVYDESG KFLFQFGGEG SGEGQLDYPR
GIRTDSSGLI LVADFWNERV QIFTRHGEFV RTVRTGFGPE GLAVGPEGQL VVTNVTDTVT
VYPNY
//
