ID   KLHDB_DROSI             Reviewed;         623 AA.
AC   B4QLQ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Kelch-like protein diablo {ECO:0000250|UniProtKB:Q9VUU5};
GN   Name=dbo {ECO:0000250|UniProtKB:Q9VUU5}; ORFNames=GD14575;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1] {ECO:0000312|EMBL:EDX10601.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC       protein ligase complex which mediates the ubiquitination and subsequent
CC       proteasomal degradation of target proteins. May have a role in synapse
CC       differentiation and growth (By similarity).
CC       {ECO:0000250|UniProtKB:Q9VUU5, ECO:0000250|UniProtKB:Q9Y2M5}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9Y2M5}.
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DR   EMBL; CM000363; EDX10601.1; -; Genomic_DNA.
DR   RefSeq; XP_016032031.1; XM_016171543.1.
DR   AlphaFoldDB; B4QLQ2; -.
DR   SMR; B4QLQ2; -.
DR   STRING; 7240.B4QLQ2; -.
DR   EnsemblMetazoa; FBtr0354299; FBpp0318704; FBgn0186255.
DR   GeneID; 6738203; -.
DR   HOGENOM; CLU_004253_14_2_1; -.
DR   OMA; NSWSPIV; -.
DR   PhylomeDB; B4QLQ2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000304; Chromosome 3l.
DR   Bgee; FBgn0186255; Expressed in embryo and 3 other tissues.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; ISS:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:EnsemblMetazoa.
DR   Gene3D; 2.120.10.80; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR017096; BTB-kelch_protein.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 6.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF50965; SSF50965; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   3: Inferred from homology;
KW   Actin-binding; Kelch repeat; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..623
FT                   /note="Kelch-like protein diablo"
FT                   /id="PRO_0000379953"
FT   DOMAIN          72..139
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          174..276
FT                   /note="BACK"
FT                   /evidence="ECO:0000255"
FT   REPEAT          323..369
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          371..417
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          418..464
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          466..511
FT                   /note="Kelch 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          513..558
FT                   /note="Kelch 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          559..605
FT                   /note="Kelch 6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   623 AA;  68995 MW;  89A3BD2812587167 CRC64;
     MGDLPGSGST AQPRDAAVTG TGGNSTAGGG SSVGSTAVDR PPSPARLSHT SEKHPKVTLT
     ELNMLRRHRE LCDVVLNVGG RKIFAHRVIL SACSSYFCAM FTGELEESRQ TEVTIRDIDE
     NAMELLIDFC YTAHIIVEES NVQTLLPAAC LLQLVEIQDI CCEFLKRQLD PTNCLGIRAF
     ADTHSCRELL RIADKFTQHN FQEVMESEEF LLLPVGQLVD IICSDELNVR SEEQVFNAVM
     SWLKYNVAER RQHLAQVLQH VRLPLLSPKF LVGTVGSDLL VRSDEACRDL VDEAKNYLLL
     PQERPLMQGP RTRPRKPTRR GEVLFAVGGW CSGDAIASVE RFDPQTNDWK MVAPMSKRRC
     GVGVAVLNDL LYAVGGHDGQ SYLNSIERYD PQTNQWSCDV APTTSCRTSV GVAVLDEFLY
     AVGGQDGVQC LNHVERYDPK ENKWSKVAPM TTRRLGVAVA VLGGFLYAIG GSDGQCPLNT
     VERYDPRHNK WVAVSPMSTR RKHLGCAVFN NYIYAVGGRD DCMELSSAER YNPLTNTWSP
     IVAMTSRRSG VGLAVVNGQL YAVGGFDGSA YLKTIEVYDP ETNQWRLCGC MNYRRLGGGV
     GVMRAPQTEN YMWCENSFKQ PNS