ID C3ZU45_BRAFL Unreviewed; 800 AA.
AC C3ZU45;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=DED domain-containing protein {ECO:0000259|PROSITE:PS50168};
GN ORFNames=BRAFLDRAFT_87308 {ECO:0000313|EMBL:EEN43931.1};
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:EEN43931.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43931.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43931.1};
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; EEN43931.1; -; Genomic_DNA.
DR RefSeq; XP_002587920.1; XM_002587874.1.
DR AlphaFoldDB; C3ZU45; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3ZU45; -.
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; 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; 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 29..107
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT REPEAT 536..576
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 642..669
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 717..760
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 112..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 474..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89191 MW; 073E51A566C12BEF CRC64;
MVPVVPAVSA RMAGPVRERV TDADRRHFDF VQTLLRISDE LTEEETANVK VFCLHLIPKG
HLEQLRRAMD VFVKLMELDK IDQENLDFLK EILERIGRQD LIQNVLRRFQ PPDREIPENP
ELQPGTIQQG ADAEGNATSN TYVVVNGQVR MIQETLDRLR NHIATLSGTR RSQVKFRGYK
KHKSILVHFS IPRENTAVLR HMADHSDPRL VYMGVKSLQI DSEVPIKVQP GVPLYDVKRQ
LPVDDIEVGC STRTKHQRAP QSWTRLSALN LFSDALPLHL QAAASLEYQG FSYSLVRALV
QKDRLREHQM RQAIQNLRNA EVDSNTLRQK AEVDSNTLRQ KAEVDSNTIM TFRSKLDITE
NRLKEALETI AVLEEKLQQA QEYAEKAAKQ VTSHVTEYKG EKPPGGWPQE YRGEKPPGGW
PQQYMGEKPP GGWPQEYRGE KPPGDLSAQV EKADAATQTH LAGPVGTAVR PGDVGDKLGE
DPTVQEEEKR SSRQDSGIGR EDALGSEAPE QERDTSGTEG AASRSTGDSK QDVVTFGGKG
SEPGKFKFLR GVVVSPSNEI CVADMGNRRV QVHSMEGVYL RNFPTVVPGT GESTMLPRDV
CMDSNGTLWV VGEGETAEHV VQYSTDGAAM ARFDLKKSHN FRGIAVDTRT NHILVTDAAN
TEVQVFRPDG SLVRTVRHPE GEMKYPHYVT VDGEGNILVS DWRSDSVYVY DESGKFLFQF
GGKGSGEGQL MYPRGICTGS SGHILVADNE NRRVQIFTRH GEFVRTFRTG FKPTGLAVGP
EGQLVVTDQP NHTLAVFSNY
//
