ID   KLHDB_DROMO             Reviewed;         617 AA.
AC   B4L0G9;
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=GI11691;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1] {ECO:0000312|EMBL:EDW19138.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW19138.1};
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; CH933809; EDW19138.1; -; Genomic_DNA.
DR   RefSeq; XP_002008662.2; XM_002008626.2.
DR   AlphaFoldDB; B4L0G9; -.
DR   SMR; B4L0G9; -.
DR   STRING; 7230.FBpp0160908; -.
DR   PRIDE; B4L0G9; -.
DR   GeneID; 6582981; -.
DR   KEGG; dmo:Dmoj_GI11691; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   HOGENOM; CLU_004253_12_0_1; -.
DR   InParanoid; B4L0G9; -.
DR   OMA; NSWSPIV; -.
DR   PhylomeDB; B4L0G9; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
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; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..617
FT                   /note="Kelch-like protein diablo"
FT                   /id="PRO_0000379949"
FT   DOMAIN          73..140
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          175..277
FT                   /note="BACK"
FT                   /evidence="ECO:0000255"
FT   REPEAT          324..370
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          372..418
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          419..465
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          467..512
FT                   /note="Kelch 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          514..559
FT                   /note="Kelch 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          560..606
FT                   /note="Kelch 6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  68059 MW;  5C0EACB57248FA04 CRC64;
     MGDPLLPGST GLGSGGTAAA TGGTGTTGTG LGSGGTSGTE RPPSPARLTH TSEKHPKVTL
     TELNMLRRHR ELCDVVLNVG GRKIFAHRVI LSACSSYFCA MFTGELEESR QTEVTIRDID
     ENAMELLIDF CYTAHIIVEE SNVQTLLPAA CLLQLVEIQD ICCEFLKRQL DPTNCLGIRA
     FADTHSCREL LRIADKFTQH NFQEVMESEE FLLLPVGQLV DIICSDELNV RSEEQVFNAV
     MSWLKYNVAE RRQHLAQVLQ HVRLPLLSPK FLVGTVGSDL LVRSDEACRD LVDEAKNYLL
     LPQERPLMQG PRTRPRKPTR RGEVLFAVGG WCSGDAIASV ERFDPQTNDW KMVAPMSKRR
     CGVGVAVLND LLYAVGGHDG QSYLNSIERY DPQTNQWSCD VAPTTSCRTS VGVAVLDGFL
     YAVGGQDGVQ CLNHVERYDP KENKWSKVAP MTTRRLGVAV AVLSGHLYAI GGSDGQCPLN
     TVERYDPRQN KWVAVNPMST RRKHLGCAVF NNYIYAVGGR DDCMELSSAE RYNPLTNTWS
     PIVAMTSRRS GVGLAVVNGQ LYAVGGFDGS AYLKTIEVYD PETNQWRLCG CMNYRRLGGG
     VGVMRAPQTE NYMWCAK