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Database: UniProt
Entry: A0A151J329_9HYME
LinkDB: A0A151J329_9HYME
Original site: A0A151J329_9HYME 
ID   A0A151J329_9HYME        Unreviewed;       622 AA.
AC   A0A151J329;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Kelch-like protein diablo {ECO:0000256|ARBA:ARBA00013699};
GN   ORFNames=ALC57_11418 {ECO:0000313|EMBL:KYN16336.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN16336.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN16336.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN16336.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN16336.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00043912}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; KQ980368; KYN16336.1; -; Genomic_DNA.
DR   RefSeq; XP_018367909.1; XM_018512407.1.
DR   RefSeq; XP_018367910.1; XM_018512408.1.
DR   AlphaFoldDB; A0A151J329; -.
DR   STRING; 471704.A0A151J329; -.
DR   GeneID; 108764267; -.
DR   OrthoDB; 5472491at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd18458; BACK_KLHL19_KEAP1; 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; IPR047098; KEAP1_BACK.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR24412:SF35; ACTIN-BINDING PROTEIN IPP; 1.
DR   PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 5.
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; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   4: Predicted;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          74..141
FT                   /note="BTB"
FT                   /evidence="ECO:0000259|PROSITE:PS50097"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  70178 MW;  07047B74850FFF32 CRC64;
     MDGEKDCQRK KEARDDAPSP GAIPFASGEE TDWEGMLNTE RQRGDLGDMT FCMANYLKET
     MKMMFMMRSH HMLTDVILEV GTELFHAHKV ILAAASPYFK AMFTGGLKEC EMTRVKLQGV
     CPTTMARLMY FMYTGQIRVT EITVCSLLSA ATMFQVSNVI DACSVFLERQ LDPTNAIGIA
     NFAEQHGCHD LYHKANQFIV QHFNQICQEE EFLQLSAIQL VTLIRKDELN VQEEREVYNA
     VLKWVKYNEE ARRPKMEHIL HAVRCQYLTP NFLREQMKNC DVLKKVPACR EYLAQIFKDL
     TLHKKPVVKE RTPNTRRVIY IAGGFFKHSL DVLEGYNADD KAWTQHAKLI VPRSGLGGAF
     LKGMFYAVGG RHNSPGSRYD SDWVDRYNPM TDQWRPCSPM SVPRNRVGVA VMDGLLYAVG
     GSAGVEYHNS VECYDPDQDT WTSVKSMHIK RLGVGVAVVN RLLYAIGGFD GKDRLSSVEC
     YHPENDEWTM VSPMKCSRSG AGVASLGQYI YVIGGYDGKS QLNSVERYDT EHDIWENVSS
     VTIARSALSV TILDGKLYAM GGYDGTTFLN IVEIYDPVQD QWAQGVPMTS GRSGHASAVS
     YYQCPIHCDH LDYNISLEKP PS
//
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