ZGPAT_DROAN
ID ZGPAT_DROAN Reviewed; 511 AA.
AC B3MPC0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN ORFNames=GF15731;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Transcription repressor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; CH902620; EDV32239.1; -; Genomic_DNA.
DR RefSeq; XP_001963018.1; XM_001962982.2.
DR AlphaFoldDB; B3MPC0; -.
DR SMR; B3MPC0; -.
DR STRING; 7217.FBpp0118923; -.
DR PRIDE; B3MPC0; -.
DR EnsemblMetazoa; FBtr0120431; FBpp0118923; FBgn0092755.
DR GeneID; 6498536; -.
DR KEGG; dan:6498536; -.
DR eggNOG; KOG2185; Eukaryota.
DR HOGENOM; CLU_040504_1_0_1; -.
DR InParanoid; B3MPC0; -.
DR OMA; QYTRGIG; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; B3MPC0; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR043560; ZGPAT.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR46297; PTHR46297; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..511
FT /note="Zinc finger CCCH-type with G patch domain-containing
FT protein"
FT /id="PRO_0000385200"
FT DOMAIN 311..357
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 157..180
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 254..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..280
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 58132 MW; F353D50C4B53160D CRC64;
MDEYEAQLLV VEQALENATD EHQRQELLAL KENLQELLSL TRGGTEDDAA TDDDSQNADN
LDNELERLKS ELNDMEATGA SKSNENEVQQ LADLRTKYSS MVGEKCSAPH EHSWGAISYH
NALICGVDDE VIINGDGALD ARLRVLFTNP THREMLPCSY YLEGECRFDE ARCRYSHGAL
VTGSSIRKYN PPDFHKLSRS CPVLAQLPDR LWHRGRVLCV NFVEQVCRVR LDGQDHKERE
RDFKFEELFP LTTDQEDELT SEDSSSVNDG SSDEEESDMD DLEAARRARM VELSLFTFKP
TEKLGAWEEY TRGIGSKLME KMGYIHGTGL GSDGRGIVTP VSAQILPKGR SLDACMELRE
AANGDKDYFS VERKLQRAQR RQKKANEKAY VRESQRTDVF SFLNSSVLGS DNKQQAEPEA
KKAKANDLQQ HSTKTLNVET VRIADDIRRK QRDIAKVQQS LDRNTGDVQL QKRLQAQMHN
QKQELATLQA QERSLSKEQQ TRKSKNKMFE F