ZGPAT_DROSE
ID ZGPAT_DROSE Reviewed; 513 AA.
AC B4HWD7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN ORFNames=GM17832;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480818; EDW52332.1; -; Genomic_DNA.
DR RefSeq; XP_002036409.1; XM_002036373.1.
DR AlphaFoldDB; B4HWD7; -.
DR SMR; B4HWD7; -.
DR STRING; 7238.B4HWD7; -.
DR EnsemblMetazoa; FBtr0200817; FBpp0199309; FBgn0172739.
DR GeneID; 6611892; -.
DR KEGG; dse:6611892; -.
DR HOGENOM; CLU_040504_1_0_1; -.
DR OMA; QYTRGIG; -.
DR PhylomeDB; B4HWD7; -.
DR Proteomes; UP000001292; 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..513
FT /note="Zinc finger CCCH-type with G patch domain-containing
FT protein"
FT /id="PRO_0000385207"
FT DOMAIN 312..358
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 155..178
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 252..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 58675 MW; 6D7AA0CEFD99CE67 CRC64;
MEEYEAQLLV VEQALENAAD DAQRQELLAL KNNLQELLAL TRDTGDEAPT DELPQQGNDL
DDELQRLKSE LSDLEAAGSS QTALDEERQL ADLRTKYTAM VGEKCSAPHE HSWGTCYHNA
LICGVDDEVV INSEGVLDAR LRVLFTNPTH REMLPCSYYL EGECRFDEAK CRFSHGALVT
GSSIRKYNPP DFHKLSRSRP VFALLPDRLW HRGRVLCVNF VEQVCRVRLD GQDHKERERD
FKFEELYPLT TDQDEDDELS SEESTSSMRD ASSDEAESDM DDLEEARRAR MVELSLFTYK
PTDRLGAWEE FTRGIGSKLM EKMGYIHGTG LGSEGRGIVT PVSAQILPQG RSLDACMELR
EAANGDKDYF SVERKLKRAQ RRQRKADEKA YVRESQRVDV FTFLNDRVLG PGESTQQSEQ
VAKKAKNNEL QQHSTKTLNV ETVRIADEIR RKQRDMAKVK QSLERNSGDA QLQKRLQVQM
QSHKQELATL QAQERSLSKE QQTRKSKNKM FEF