ID KLHDB_AEDAE Reviewed; 589 AA.
AC Q16RL8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Kelch-like protein diablo {ECO:0000250|UniProtKB:Q9VUU5};
GN Name=dbo {ECO:0000250|UniProtKB:Q9VUU5}; ORFNames=AAEL010911;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT37050.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(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; CH477704; EAT37050.1; -; Genomic_DNA.
DR RefSeq; XP_001661146.1; XM_001661096.1.
DR AlphaFoldDB; Q16RL8; -.
DR SMR; Q16RL8; -.
DR STRING; 7159.Q16RL8; -.
DR PaxDb; 7159-AAEL010911-PA; -.
DR EnsemblMetazoa; AAEL010911-RA; AAEL010911-PA; AAEL010911.
DR GeneID; 5574073; -.
DR KEGG; aag:5574073; -.
DR VEuPathDB; VectorBase:AAEL010911; -.
DR eggNOG; KOG4441; Eukaryota.
DR HOGENOM; CLU_004253_12_0_1; -.
DR InParanoid; Q16RL8; -.
DR OMA; CAVFNNL; -.
DR OrthoDB; 5472491at2759; -.
DR PhylomeDB; Q16RL8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008820; Chromosome 3.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd18459; BACK_KLHL20; 1.
DR CDD; cd18249; BTB_POZ_KLHL20_KLEIP; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 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 PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR PANTHER; PTHR24412:SF451; KELCH-LIKE PROTEIN 20; 1.
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; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 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..589
FT /note="Kelch-like protein diablo"
FT /id="PRO_0000379942"
FT DOMAIN 41..108
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 143..245
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REPEAT 292..338
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 340..386
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 387..433
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 435..480
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 482..527
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 528..574
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 66025 MW; 0357BA91DEB903F1 CRC64;
MGDVLISDRP PSPARLSHTS EKHPRVTLTE LNVLRRHREL CDVVINVSGR KIFAHRVILS
ACSPYFRAMF TGELEESRQT EVTIRDIDEN AMELLIDFCY TSHIVVEESN VQTLLPAACL
LQLAEIQDIC CEFLKRQLDP TNCLGIRAFA DTHSCRELLR IADKFTQHNF QEVMESEEFL
LLPVGQLVDI ICSDELNVRS EEQVFNAVMA WLKYNVAERR QHLAQVLQHV RMPLLSPKFL
VGTVGSDLLV RSDEACRDLV DEAKNYLLLP QERPLMQGPR TRPRKPTRRG EVLFAVGGWC
SGDAIASVER FDPETADWKM VAPMSKRRCG VGVAVLNDLL YAVGGHDGQS YLNSIERYDP
QTNQWSCDVA PTTSCRTSVG VAVLDGFLYA VGGQDGVQCL NHVERYDPKE NKWSKVAPMT
TRRLGVAVAV LGGYLYAIGG SDGQCPLNTV ERYDPRQNKW CAVSPMSTRR KHLGCAVFNN
FIYAVGGRDD CMELSSAERY NPHTNSWSPI VAMTSRRSGV GLAVVNGQLY AVGGFDGTAY
LKTIEVYDPE TNQWRLCGCM NYRRLGGGVG VMRAPQTENY MWIRKDSVV
//
