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KLHDB_DROWI
ID   KLHDB_DROWI             Reviewed;         679 AA.
AC   B4MXW3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Kelch-like protein diablo {ECO:0000250|UniProtKB:Q9VUU5};
GN   Name=dbo {ECO:0000250|UniProtKB:Q9VUU5}; ORFNames=GK15757;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1] {ECO:0000312|EMBL:EDW76882.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW76882.1};
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; CH963876; EDW76882.1; -; Genomic_DNA.
DR   RefSeq; XP_002065896.2; XM_002065860.2.
DR   AlphaFoldDB; B4MXW3; -.
DR   SMR; B4MXW3; -.
DR   STRING; 7260.FBpp0244900; -.
DR   PRIDE; B4MXW3; -.
DR   EnsemblMetazoa; FBtr0421713; FBpp0379805; FBgn0217760.
DR   eggNOG; KOG4441; Eukaryota.
DR   HOGENOM; CLU_004253_12_0_1; -.
DR   InParanoid; B4MXW3; -.
DR   OMA; NSWSPIV; -.
DR   OrthoDB; 731760at2759; -.
DR   PhylomeDB; B4MXW3; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007798; 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..679
FT                   /note="Kelch-like protein diablo"
FT                   /id="PRO_0000379955"
FT   DOMAIN          101..168
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          203..305
FT                   /note="BACK"
FT                   /evidence="ECO:0000255"
FT   REPEAT          352..398
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          400..446
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          447..493
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          495..540
FT                   /note="Kelch 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          542..587
FT                   /note="Kelch 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          588..634
FT                   /note="Kelch 6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  73991 MW;  8B8E942F80035C59 CRC64;
     MGDLPGGGGG AAGGAGAAGG GGGGGNGAAG SSSSGGGASG SGGGGPGSSG LPTTNGLGVA
     GTAGPNVDRP PSPARLSHTS EKHPKVTLTE LNMLRRHREL CDVVLNVGGR KIFAHRVILS
     ACSSYFCAMF TGELEESRQT EVTIRDIDEN AMELLIDFCY TAHIIVEESN VQTLLPAACL
     LQLVEIQDIC CEFLKRQLDP TNCLGIRAFA DTHSCRELLR IADKFTQHNF QEVMESEEFL
     LLPVSQLVDI ICSDELNVRS EEQVFNAVMS WLKYNVAERR QHLAQVLQHV RLPLLSPKFL
     VGTVGSDLLV RSDEACRDLV DEAKNYLLLP QERPLMQGPR TRPRKPTRRG EVLFAVGGWC
     SGDAIASVER FDPQTNDWKM VAPMSKRRCG VGVAVLNDLL YAVGGHDGQS YLNSIERYDP
     QTNQWSCDVA PTTSCRTSVG VAVLDGFLYA VGGQDGVQCL NHVERYDPKD NKWGKVAPMT
     TRRLGVAVAV LGGYLYAIGG SDGQCPLNTV ERYDPRQNKW VAVNPMSTRR KHLGCAVFNN
     YIYAVGGRDD CMELSSAERY NPLTNTWSPI VAMTSRRSGV GLAVVNGQLY AVGGFDGSAY
     LKTIEVYDPE TNQWRLCGCM NYRRLGGGVG VMRAPQTENY MWCDNNSSNN NNNNYNLKHQ
     QQQPQQQQQQ QQQQTQQQL
 
 
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