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
//