ID A0A3B0K577_DROGU Unreviewed; 1291 AA.
AC A0A3B0K577;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Blast:Zinc finger protein 768 {ECO:0000313|EMBL:SPP80776.1};
GN ORFNames=DGUA_6G005705 {ECO:0000313|EMBL:SPP80776.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP80776.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OUUW01000005; SPP80776.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0K577; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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; 1.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24388:SF54; C2H2 FINGER DOMAIN TRANSCRIPTION FACTOR CRZA; 1.
DR PANTHER; PTHR24388; ZINC FINGER PROTEIN; 1.
DR Pfam; PF07776; zf-AD; 1.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 18..116
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
FT DOMAIN 219..247
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 278..305
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 472..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..875
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 1291 AA; 144464 MW; D06CEA077D533A0F CRC64;
MERFAFKIDA ALKANLYKIC RLCGIDNPSK VQILPPNEAN IIDLDDPSLS QKVLELIGFT
VGLKTPTFGS IQQRPLQVTV DDKMPQTMCS ICVDKINDFY EFREMCYATN KQTRNLLGLP
QLEPLKLICS QSMVKAEPQV PGKRGRKRKT DESFLKAKIT EMPDVKKEPL AWRKKQRLQQ
TQTQQYQQLL VTKTEPEIKD EPMDPENRLR LPGKKGRKAI CSVCGEKFAS KEMADEHKSA
VHVPSIPRYI CNACNQTHHN PTDIRAHQLW HKLSKTPYKC PLCDSYVANN YAFTRHLREH
TPQTPVQLLV LDRECPLCKK TFITNFFYNT HRCAIRKRKC GGCNRTLNTE VAFLRHAPVC
SKIYLSHSKH IMPEEANTES QMCIKNEVEE VDSSGCPTSV IPPDFFINED MQPVVVLERL
ASPLLRAFSA EPQNTLGASR STSSERVSSK NYLKRVDQLL KSTMSTLVSI KHEPEVHIND
TMQTATVQPE SEPEEEEPAS FSDFHAANDD SDEEEAEAAT MAASIDDNVP SVSVKQEPRD
NAYENQSHVK QEPLKLKLKI TNNHGKLNSS LIDEAGQSKS NKKKKKRKHK EREKEAESQP
TAQDLPMVSI KQERIDAENV PDGNQRSTDF QPQATVMTSI PMAHLESSFT TERDEAMTQC
PEPEKDVKPN RMELDRLMQI THVASGVDIA EEAMPLDKAV EATPDEPLPA DDTFIMPPKA
KSAKPTARKS TGGATRRPPS AEDASPRETT APLLQIVAVE SGEAVSFKMP ADIRIKPEPR
NRGYADDERE DKPTQEINHN EKIDEENAFI NSLDFNNMIV KQEKDLDISD QTGNGSDPGA
MHQSHNGLER GSESEDSDGE DSPSEADEAE EAMEEDEGER IYREIELPLL EPEKEGEADK
QQSEKQSEES IQVQEAQSEN LELEMPMETP VVVGWVEQPA VEESIQVQQA PSENLELDMP
METAVVVGGV EQPTVELVQS QETPTANAPE EMRPQLSTLQ VLGELDSLLE VTGLIGEVDP
PQEASKDLEE IKPPLNTLDV VEEIHQALEN LDAVGDMEPL VEIPEGLVQI EPPLDTPNIL
SAQEPVNAFD FVITDICSQA AEIPEIAYVQ SQNIPNLSSS PPNPEPLENA DTEHDSSDCQ
ADTLLEIIVN APKDNETQAL PFNFETGTAI CDEEQQNVLN HELSEQQAPL DGNVEQSAEA
EEKILAVEEE LCLQLEEQEE ELPGPSARPN EETENRINEQ QQEMDLEGQR QPRCQLDDDS
NINEIAENNN NANIERELQD DSNVPQENVS P
//
