ID A0A6I8UFW3_DROPS Unreviewed; 589 AA.
AC A0A6I8UFW3;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Transcription factor grauzone {ECO:0000313|RefSeq:XP_001354861.3};
GN Name=LOC4815381 {ECO:0000313|RefSeq:XP_001354861.3};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001354861.3};
RN [1] {ECO:0000313|RefSeq:XP_001354861.3}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001354861.3};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001354861.3};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_001354861.3; XM_001354825.4.
DR AlphaFoldDB; A0A6I8UFW3; -.
DR KEGG; dpo:4815381; -.
DR InParanoid; A0A6I8UFW3; -.
DR Proteomes; UP000001819; Chromosome X.
DR ExpressionAtlas; A0A6I8UFW3; baseline.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1800.20; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR InterPro; IPR039970; TF_Grauzone.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23225:SF2; AT09679P-RELATED; 1.
DR PANTHER; PTHR23225; ZINC FINGER PROTEIN; 1.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00868; zf-AD; 2.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 1..80
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
FT DOMAIN 310..337
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 338..366
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 373..395
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 402..430
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 431..458
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 517..544
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 545..573
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 141..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 589 AA; 67780 MW; FA289BE369585F96 CRC64;
MICRLCLRTI NPSNAVFLFE TNETLAETTL VKMIAKFLQL EITPDDSIST SVCTECCEHL
EDFNTFWQLV EQKQGTLKKE FLTVDVDCVA MKWTGEIDVD VNIDELPLVA VEMDEKPLDM
HNLSLLGSVL DVNVDSVEVP QAPPGDIKIQ PTDYLSEEDG HPSHIEATDS EFECEPVPEE
NTSDDEPLVK LQDKLKPKRR SHPRTTKTRE DTCSLGAQEL NYLLGRGDGE GSKGRRRKAP
GQRIPTEVQE SELQAALERK PKGCSRAQLA KRYEEVIASY MNADCDLCEF SAKYLSELKV
HFLEAHQREF YIKCCNKVFT RASKLMDHIR KHVNPKLFTC SICQKTLNSQ DYLATHIETV
HNKVEKLDKV LQFPCSKCER TFSSERRLAN HLAKHDTATL EHICHICHKN FANVHRLRRH
IQSIHEDLHR HVCDICGKKF KFKPSFERHL REHQGVVAPA MQCPVCGVWL KNEHSLRLHR
FTHDSTNTAC PHCSKTCNSR TALRAHIKYA HKLTTSFQCT YCEKTFKQQR NLDEHLAIHT
GLQLYNCPHC PKECRSRSNM YVHIKQRHAE EWLTAKMARS HNPQFKPHA
//
