ID C3ZU64_BRAFL Unreviewed; 857 AA.
AC C3ZU64;
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_87327 {ECO:0000313|EMBL:EEN43950.1};
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:EEN43950.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43950.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43950.1};
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; EEN43950.1; -; Genomic_DNA.
DR RefSeq; XP_002587939.1; XM_002587893.1.
DR AlphaFoldDB; C3ZU64; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3ZU64; -.
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; 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; 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 18..96
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT REPEAT 592..635
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 701..728
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 774..817
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 447..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 370..439
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 95568 MW; AC1391BD5DF95205 CRC64;
MASPVRERVT AADRRHFDFV KTLLRISDEL TEEETANVKI FCLHLIPKGH LAQLRRAMDV
FVKLMELDKI DQENLDFLKE ILEGIGRQDL IQNVLQRFQP PDREIPENPG LQPENPDLQP
ENPDLQPENP DLQPENPDLQ PENPDLQPEN PGLQPENPDL QPQNSDLQPQ NPELQPGDPE
IQSGQSNAER ANEEANATSN IYVVVHGQVR MIQEALDRLK GDLARLSGTR RSQVKYRGHK
KHKSILVHFS IPRENTAVLR HMADHSDPRL VYMGVKSLQI DAEVPIKVQQ EAPVYDVKRQ
LPVDDIEVGC STRTRHQRAP QGWTRLSALN LFSDALPLHL QAAESLEYQG FSYSLVRALV
QKDRLREHQM RQAIQNLRNA ELDSNTLRQK AEVDSNTIMT LRSKLNISEN RLKEALDTIE
VLQEKLQQAQ EYAEKAAKQV TSHVAEYRGE KPPGGWPQEY RGEKPPGGWP QEYRGEKPPG
GWPQEYRGEK PPGGWPQEYR GEKPPGGWSA QVENADAATQ THLADAVSTT GGSGDVDDKL
GEDPTVTEED KGTAGQDSDT DPDGPKATEE KRHTAGAEGA ASDTTGDLTQ DVMTFGRKGS
EPGEFHHPRG VVVSPSNDIF VADMSNKRVQ VHTTEGVYLR HFPTVVPGTA DKDMGPHDVC
MDGNGTLWVV GEGGSAEHVV QYSTDGIAMG GFHLEEIGYF RGIAVDMRTN HILVTDAHQG
AVHVFRPDGS LVRTVQHPRE EMRRPRYVTV DGNFLVSDRD THRVYVYDES GKFLFQFGGE
GSGEGQMSFP HGICTDSSGH ILVADYGNER VQIFTRHGEF VRTVHPGFNP EGLAVGPEGQ
LVVTSHFDHT VTVYPCY
//
