ID A0A0M3QX44_DROBS Unreviewed; 1511 AA.
AC A0A0M3QX44;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=CG43980 {ECO:0000313|EMBL:ALC45219.1};
GN ORFNames=Dbus_chr3Lg2385 {ECO:0000313|EMBL:ALC45219.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC45219.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC45219.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC45219.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012525; ALC45219.1; -; Genomic_DNA.
DR SMR; A0A0M3QX44; -.
DR STRING; 30019.A0A0M3QX44; -.
DR OMA; WEPVPRV; -.
DR Proteomes; UP000494163; Chromosome 3l sequence.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR CDD; cd18491; BACK_ABTB2_like; 1.
DR CDD; cd18297; BTB_POZ_ABTB2-like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46071; ANKYRIN REPEAT AND BTB/POZ DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR46071:SF2; ANKYRIN REPEAT AND BTB_POZ DOMAIN-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50097; BTB; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT REPEAT 1063..1095
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1310..1376
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 85..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 164141 MW; AB36E1B30D70E981 CRC64;
MYCSKDCACG LCRELRSYKQ NAKKGPVVGA AQLPQQLPGK AKLKKLGAKA TPPSSLLGRM
LNENFILRRR GISLKNFQPQ SLRNSEMCQA QLQPRDIPRP PQTPSPTPIE EPQWAATQPR
RDRERDRAAN RNGNKKLGDQ EVKPNHKVVI YFGDSMNRTE QQPAAGVGVG VEVGVAVAGN
LLHSQLLQEM SQKLQVDKPL LEAEVEAIEF QSTPDQTTGA ETAVAEPDDE LPPYIESVQN
GVINIKIEGN YRRASALVQT VAKPTLAVVG QTKYDAIGAA NNNDKDEDDD DDDDDDDDDD
SDPGHNAETA SQSDSCDWGY VQEWRRAARR PPNFAGQQQQ PPTQTTGLPP VALQAQLQTA
AASTSQQQLP LNGLQVGGGV AVATPAPRIL KELAQQPNKA TPMPLLSSPL PQQQQAQPQQ
LTSPTGKGNL AQRSVAGPAR LTVQSTPVKS QPAQLSGSLQ SSPNRPTLGI PTAVTPGSQD
TPRAHQHEQF RAQQRVQECH SSSDENRSSG HASMSDTGGH SSSPAGGMTL GPLPEDRLAA
GVTNRSTRSR RHRGILPAGK APWSGSGLED IKLAIQQLTM RSQTSSSTYS SLSAGSESSE
PARRLGRYSS LETVITSTSA DEFVWVDSHN RLVELQHPPW SQQCIMRVLR HGRCKQQAQN
VSIEVISRLG YLLQRALVRI AREIQRFSAG LGLCSKQEVT GAFKVVLCSA LADSCSKACL
RAAAMFAVPG ESALKQSKSS RAALQLSVGS FFRWMSDARL GKFIHEYAAV YLCAGIENLL
EEIMLQCGSI GSVSSSAALD QSIASSGDFW GLLQPFAHLN AGRIASGSLA LPRWTSPFSL
ATCVGSIREL KEKAQRTQQE FQHTATLSNA ALSALFYFMR CSQLEHTELA AQNSTAGQAP
ANSGSQNVQE LCYERAYVVL PPLAEWLRVA SAHAEHRNGL MIDKDDILQL LLTGRAELLA
QAAQLLPPTT RYDTQNSGGL TALMIASIRN DEVALHALLD AGCDPNVEVP ATGIAGFPAI
QPDTQHWTAL CFAASRANYV ALRILLERGG KVEGGARSSE EKCTMTPLQL AAGTGNLEMV
ALLLAHGANA FLSTQQKDSV CFAGSAQKGC YCAISVAAAH GHRSCLRKLL THPVTPNTRD
VLSLEEMLAE GDVGVNARSA VTSKAGEDLL PLLNKTQIKR LQEAMYHSAE NNHLDITIEL
RKLGVPWTLH CWMHALSAAH ELRLDAVIDQ LLQDFLQVCP EDYSVQFVSE CLPLLFNILR
NKNEGTTLLL ADIFATCFGW EALQPLKEPQ MQPVQGSRID PKFVNNPELS DVTFRVEGKI
FYGHKIVLVT ASSRFQSMLS SKLSEASGAS GSTPTVQIND IRYHIFQLVM QFLYSGGCNA
LDVSHADVLE LMAAASFFQL DALLRYTEAR CSEMVDIDNV VAMYIHAKVY NANNLLEYCQ
CFLLQNMVAL LTYDDSVKRL LFAKKIPNHD VLAGLLHTLQ QRLKARKPSS VAGNLVNSFR
SSTNLTPVKK K
//
