ID C3ZU17_BRAFL Unreviewed; 856 AA.
AC C3ZU17;
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_87280 {ECO:0000313|EMBL:EEN43903.1};
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:EEN43903.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43903.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43903.1};
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; EEN43903.1; -; Genomic_DNA.
DR RefSeq; XP_002587892.1; XM_002587846.1.
DR AlphaFoldDB; C3ZU17; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3ZU17; -.
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; 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 580..623
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 765..808
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 820..848
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 451..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..446
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 95482 MW; 081B08F996D829F8 CRC64;
MASPVRERVT DADRRHFDFV KTLLRISDEL TEEETANLKI FCLHIIPKDH LAQLRRAMDV
FVKLMELDKI DRENLDFLKE ILEGIGRQDL IRDVLRQFQP PDREIPENPD LQPEYPGLQP
ENTDLQPENP DLQPENPDLQ PENPDLQPEN PDLQPENPDL QPQNSELQPQ NPELQPGDPE
IQSGQSNAEG ANEEGDATSN IYVVVHGQVR MIQEALDRLK CDLARLSGTR RSQVMYRGHK
KHKSILVHFS IPRENTAVLR HMADHSDPRL VYMGIKSLQI DAEVPIKVQQ EEPVYDIKRQ
LPVDDIEVGC STRTKHQSWT RLSALNLFSD ALPLHLQAAA SLEYQGFSYS LVRALVQKDR
LREHQMRQAI QNLRNAEVDS NTLRQKAEVD SNTLRQKAEV DSNTIMTLHS KLNITENRLK
EALETIAVLQ EKMKQAQEYA ENAAKHVTSH VTEYRGEKPP GGWAHEYRGE KSPGGSPLEY
RGEKPPGGWS SQVEKADSAT QTHQTDPFGT TGIPGDVGGD KVGADPTVKE EVGKTPRQDS
GSGSNGKEDV LGTEALEQER QTAGTEGTAS GSTGDRKQRV ITFGVMGTEP REFLDPRGVV
VSPSNEIFVA DRGNERVQVR STEGVYLRHF PTVVPGTGDK DMQPHDVCMD GNGTLWVVGR
GETTDHVVQY STDGTAMAGF DLKKIGYSRG IALNMRTNHI LVTDADQGAV HVFRPDGSLV
RTVRHPRGGE MKRPGYITVD GEGNILVSDW DSNFVYVYDA SGKFLFQFGG WGSGEDQLWN
PAGICTDSSG HIIVVDTGNE RIQIFTRHGE FVRAVRTGFQ PVGLALGPEG QLVVTSRWNR
TVTVFTTEFL TTELDL
//
