ZGPAT_DROER
ID ZGPAT_DROER Reviewed; 513 AA.
AC B3N8L3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN ORFNames=GG10072;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954177; EDV58436.1; -; Genomic_DNA.
DR RefSeq; XP_001969377.1; XM_001969341.2.
DR AlphaFoldDB; B3N8L3; -.
DR SMR; B3N8L3; -.
DR STRING; 7220.FBpp0128618; -.
DR EnsemblMetazoa; FBtr0130126; FBpp0128618; FBgn0102384.
DR GeneID; 6541394; -.
DR KEGG; der:6541394; -.
DR eggNOG; KOG2185; Eukaryota.
DR HOGENOM; CLU_040504_1_0_1; -.
DR OMA; QYTRGIG; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; B3N8L3; -.
DR Proteomes; UP000008711; 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; Repressor; Transcription;
KW 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_0000385201"
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..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..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; 58696 MW; FE6FADC42C9D64AC CRC64;
MEEYEAQLLV VEQALENAAD EAQRQDLLAL KNNLQELLAL TRDTEDGAPT DELPQQGDDL
DDELQRLRSE LNDLEAAGSS QTALDEERQL ADLRTKYTAM VGEKCSAPHE HSWGTCYHNA
LICGVDDEVV MSSEGVLDAR LRVLFTNPTH REMLPCSYYL EGECRFDETK CRFSHGALVT
GSSIRKYNPP DFHKLCRSRP VFALLPDRLW HRGRVLCVNF VEQVCRVRLD GQDHKERERD
FKFEELYPLT TDQEEDDELS SEESNSSMNN ESSDEAESDM DDLEEARRAR MVELSLFTFK
PTERLGAWEE FTRGIGSKLM EKMGYIHGTG LGSDGRGIVT PVSAQILPQG RSLDACMELR
EAANGDKDYF SVERKLKRAQ RRQRKADEKA YVRESQRVDV FTFLNDSVLA PGESSQQGEQ
VAKKVKTNEL QQHSTKTLNV ETVRIADEIR RKQRDMAKVK QSLDRNSGDA QLQKRLQVQM
QSHKQELATL QAQERSLSKE QQTRKSKNKM FEF