ID A0A195CUZ8_9HYME Unreviewed; 738 AA.
AC A0A195CUZ8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Kelch-like protein 10 {ECO:0000313|EMBL:KYN04498.1};
GN ORFNames=ALC62_04723 {ECO:0000313|EMBL:KYN04498.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN04498.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN04498.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN04498.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN04498.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; KQ977276; KYN04498.1; -; Genomic_DNA.
DR RefSeq; XP_018393600.1; XM_018538098.1.
DR AlphaFoldDB; A0A195CUZ8; -.
DR STRING; 456900.A0A195CUZ8; -.
DR GeneID; 108772548; -.
DR OrthoDB; 5472491at2759; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR CDD; cd18450; BACK_KLHL10; 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; IPR000210; BTB/POZ_dom.
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 PRINTS; PR00501; KELCHREPEAT.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; Kelch motif; 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:UP000078542};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 103..172
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 659..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 83200 MW; 35538F9BFCAF880B CRC64;
MAARLGAIGT RVCEENEYEN CWQLSGSGEA EEAIGSSGPR ASTYSRHRAH VDYAITAGIS
RLLKQSRRKQ SARIRKCMCL PSNYALVEFP VVWSELRANQ QLCDGVIRCT EDQVFPVHRA
ILSAVSPYFK ALFTNSLKGG KTETTEVVIS VPGEIFSLIL DYAYTGTCNV NADNVEQLLP
LADQFEVLGI IQLCCQFLLQ ELRPENCLGI FKFARHYFCH DLEKQGRKYI RHHFKRILQE
SAEFKDLLSD ELEAILRDDE LNVKNEEIVF DAVKTWVEAR VEERRVYLPR LLECIRYGLM
SHKYFINNIV NWKLVEKDEA CQQILFPVNA YLTEQELKQN GEIDLKNPIA RPRVPYEILF
AIGGWSAGSP TSFVETYDTR ADRWFLSVNT DVTPRAYHGL CVLNNLIYMI GGFDGNEHFN
TVRCFDPTTK TWRERACMYH ARCYVSVCTH GGKIYALGGY NGRTRMSSGE RYEPQRNQWE
MIPSMHRQRS DASAAALNDK IYIVGGFNGQ EVLDSAEVFD VETNQWTNID SMISPRSGVS
LVAFRDSLYA LGGFSGVARL SSGERYTPNH SDQWHEISEM FSPRSNFATV ILDDMIFVIG
GYNGSSTIAH VECYDADYNE WYDASPMNLS RSALSACVIA GLANAREYSY LGKARDLGQG
QATSKNQEKS DQSGEGSTGT NVIISAQDDE QMDISESMPV VGPTDGMADG IGNFYEEENG
NDEKEMQSEL LYVVNELD
//
