ID Q9U9D0_DROME Unreviewed; 591 AA. AC Q9U9D0; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 124. DE SubName: Full=Zeste-white 5 {ECO:0000313|EMBL:AAD50986.1}; GN Name=dwg {ECO:0000313|FlyBase:FBgn0000520}; GN Synonyms=zw5 {ECO:0000313|EMBL:AAD50986.1}; GN ORFNames=CG2711 {ECO:0000313|FlyBase:FBgn0000520}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAD50986.1}; RN [1] {ECO:0000313|EMBL:AAD50986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Oregon R {ECO:0000313|EMBL:AAD50986.1}; RA Gaszner M., Vazquez J., Schedl P.; RT "The Zw5 protein, a component of the scs chromatin domain boundary, is able RT to block enhancer-promoter interaction."; RL Genes Dev. 0:0-0(1999). CC -!- INTERACTION: CC Q9U9D0; Q7JN06: BEAF-32; NbExp=4; IntAct=EBI-366837, EBI-134484; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF170448; AAD50986.1; -; mRNA. DR AlphaFoldDB; Q9U9D0; -. DR IntAct; Q9U9D0; 2. DR AGR; FB:FBgn0000520; -. DR FlyBase; FBgn0000520; dwg. DR VEuPathDB; VectorBase:FBgn0000520; -. DR HOGENOM; CLU_002678_94_15_1; -. DR ChiTaRS; dwg; fly. DR ExpressionAtlas; Q9U9D0; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:FlyBase. DR GO; GO:0003677; F:DNA binding; IDA:FlyBase. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR Gene3D; 3.40.1800.20; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8. DR InterPro; IPR012934; Znf_AD. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24404:SF49; RH47711P-RELATED; 1. DR PANTHER; PTHR24404; ZINC FINGER PROTEIN; 1. DR Pfam; PF07776; zf-AD; 1. DR Pfam; PF00096; zf-C2H2; 7. DR Pfam; PF13912; zf-C2H2_6; 1. DR SMART; SM00868; zf-AD; 1. DR SMART; SM00355; ZnF_C2H2; 8. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR PROSITE; PS51915; ZAD; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8. PE 1: Evidence at protein level; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU01263}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01263}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00042}. FT DOMAIN 11..92 FT /note="ZAD" FT /evidence="ECO:0000259|PROSITE:PS51915" FT DOMAIN 304..331 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 332..359 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 360..387 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 388..415 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 416..443 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 444..471 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 472..499 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT DOMAIN 500..527 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT REGION 100..122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..569 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 102..122 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263" FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263" SQ SEQUENCE 591 AA; 66251 MW; 1FEE341F27C2A950 CRC64; MNSKIAEVVV LNCRTCTRAC KLHKPLQEEI DLGSEGSTTL ASMLNYCTGL SFEPQDGAAM PQHICLHCLQ LLEQAFNFKR MVIDSDELLR LGLDEARCSS FHESQTHSPN QSQQHDQQQQ AFDSTEEYVM IEMLNEEQEN VANLDEELAE EDRRIFAMTV DEEEEFLTEE VDQDDELSEE EHQLAQSGDQ QEEHITMESV HEFQPAEVEY VTIKNEFETI VTEEDEFEVM NDSGAHDAIL DCQMIVIPAE GAIDEVIGEE TLEMEGDGRE EHLLPEAEDV CEDEDFLEES LDSAPPTAGE ALPYVCTVCQ KEFRQQCRLN QHMRSHVDEK QYECEECGKR LKHLRNYKEH MLTHTNVKPH QCSICGRFYR TTSSLAVHKR THAEKKPYNC DQCGRGYAAF DHLRRHKLTH TGERPYACDL CDKAYYDSSS LRQHKISHTG KKAFTCEICG VGLSQKSGYK KHMMVHSGVK AHKCDVCGHA FTFTSNLNAH VRLHSGEKPF KCEVCVKAFP TKKRLASHMR VHNKESPVTA TVAVQSINPP SRQAGAEGAT GGGATGGSPT GGGATGGSAT NLHITEVHEQ PVSTSKVVMV L //