ID   KLHDB_DROPE             Reviewed;         628 AA.
AC   B4GRJ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Kelch-like protein diablo {ECO:0000250|UniProtKB:Q9VUU5};
GN   Name=dbo {ECO:0000250|UniProtKB:Q9VUU5}; ORFNames=GL25213;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1] {ECO:0000312|EMBL:EDW40377.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479188; EDW40377.1; -; Genomic_DNA.
DR   RefSeq; XP_002021221.1; XM_002021185.1.
DR   AlphaFoldDB; B4GRJ2; -.
DR   SMR; B4GRJ2; -.
DR   STRING; 7234.FBpp0189320; -.
DR   EnsemblMetazoa; FBtr0190828; FBpp0189320; FBgn0162797.
DR   GeneID; 6596064; -.
DR   KEGG; dpe:6596064; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   HOGENOM; CLU_004253_14_2_1; -.
DR   OMA; NSWSPIV; -.
DR   PhylomeDB; B4GRJ2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008744; 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..628
FT                   /note="Kelch-like protein diablo"
FT                   /id="PRO_0000379950"
FT   DOMAIN          74..141
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          176..278
FT                   /note="BACK"
FT                   /evidence="ECO:0000255"
FT   REPEAT          325..371
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          373..419
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          420..466
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          468..513
FT                   /note="Kelch 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          515..560
FT                   /note="Kelch 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          561..607
FT                   /note="Kelch 6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  69213 MW;  21DA5F8A531486E5 CRC64;
     MGDLPGSTGG GSGPAAAGNA SGNSSSAGNT GLGVAGTTGV DRPPSPARLS HTSEKHPKVT
     LTELNMLRRH RELCDVVLNV GGRKIFAHRV ILSACSSYFC AMFTGELEES RQTEVTIRDI
     DENAMELLID FCYTAHIIVE ESNVQTLLPA ACLLQLVEIQ DICCEFLKRQ LDPTNCLGIR
     AFADTHSCRE LLRIADKFTQ HNFQEVMESE EFLLLPVGQL VDIICSDELN VRSEEQVFNA
     VMSWLKYNVA ERRQHLAQVL QHVRLPLLSP KFLVGTVGSD LLVRSDEACR DLVDEAKNYL
     LLPQERPLMQ GPRTRPRKPT RRGEVLFAVG GWCSGDAIAS VERFDPQTND WKMVAPMSKR
     RCGVGVAVLN DLLYAVGGHD GQSYLNSIER YDPQTNQWSC DVAPTTSCRT SVGVAVLDGF
     LYAVGGQDGV QCLNHVERYD PKENKWSKVA PMTTRRLGVA VAVLGGFLYA IGGSDGQCPL
     NTVERYDPRQ NKWVAVSPMS TRRKHLGCAV FNNYIYAVGG RDDCMELSSA ERYNPLTNTW
     SPIVAMTSRR SGVGLAVVNG QLYAVGGFDG SAYLKTIEVY DPETNQWRLC GCMNYRRLGG
     GVGVMRAPQT ENYMWCENSL KQHNNPPS