ID   ZEST_DROVI              Reviewed;         618 AA.
AC   Q24762;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Regulatory protein zeste;
GN   Name=z;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1732733; DOI=10.1128/mcb.12.2.598-608.1992;
RA   Chen J.D., Chan C.S., Pirrotta V.;
RT   "Conserved DNA binding and self-association domains of the Drosophila zeste
RT   protein.";
RL   Mol. Cell. Biol. 12:598-608(1992).
CC   -!- FUNCTION: Involved in transvection phenomena (= synapsis-dependent gene
CC       expression), where the synaptic pairing of chromosomes carrying genes
CC       with which zeste interacts influences the expression of these genes.
CC       Zeste binds to DNA and stimulates transcription from a nearby promoter
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates forming complexes of several hundred monomers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; M76700; AAA29052.1; -; Genomic_DNA.
DR   PIR; A42020; A42020.
DR   AlphaFoldDB; Q24762; -.
DR   SMR; Q24762; -.
DR   STRING; 7244.FBpp0231194; -.
DR   eggNOG; ENOG502QR8W; Eukaryota.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR028002; Myb_DNA-bind_5.
DR   Pfam; PF13873; Myb_DNA-bind_5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           1..618
FT                   /note="Regulatory protein zeste"
FT                   /id="PRO_0000066576"
FT   DNA_BIND        66..146
FT                   /evidence="ECO:0000250"
FT   REGION          31..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  68102 MW;  3127180B10AFDC0B CRC64;
     MSAAGDAGAG AANGSNNVAV VQATVSVSGN ISVGDGSPNN NNNNNANGNT NGNSNNNGST
     AGSSKGQLPL TPRFTAEEKD VLYTLFHLHE EVIDIKHRKK QRNKYSVRDT WDKIVRDFNS
     HPHVSAMRNI KQIQKFWLNS RLRKQYPYRD GSASGGSAGL GKVGTVSASA QQQQQQQQQQ
     QQQQQQQHHD SVKVEPEYQI SPEASEHNPQ GEPFDEIEMD GNDVSEMEDD PLEAQQQQQQ
     QQQQQQQAAA QAQAEAQQQQ QQQSAVAEMQ KLQVSAAVAA ANASMLNTHR INVDSISAEK
     LTLNDLLHFK PARHDEIILQ IKHPTDATAT QIHTIPAQPQ QHTMATITAG GYNQQIISEI
     KPQQITLAQY QAQQHQQAQA RLRPGQAQQL AQQQLAAQQQ QLAVAAAAAH QQQNSSSAAA
     VVVQQHQQQQ QQQQHQQQQQ QQQVQQQQQQ QQQAAAAAAA VKMQLTGGTP TFTFSALPTV
     TAATSVPVTV PVPVTVPVTA APAAVSNVSV SGAGTLPTGA QQQLQLQQQQ QQQQQQQQQQ
     QQAGDSYEER INYFKVKEAE LRCKEQQLAT EAKKIELNKA QDELKYMREV HRLRVEELKM
     KIRILQKEEE QLQKCSST