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Database: UniProt
Entry: A0A0D2JWX9_9EURO
LinkDB: A0A0D2JWX9_9EURO
Original site: A0A0D2JWX9_9EURO 
ID   A0A0D2JWX9_9EURO        Unreviewed;       963 AA.
AC   A0A0D2JWX9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=GATA-type domain-containing protein {ECO:0000259|PROSITE:PS50114};
GN   ORFNames=Z520_06162 {ECO:0000313|EMBL:KIX98082.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX98082.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX98082.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX98082.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN848072; KIX98082.1; -; Genomic_DNA.
DR   RefSeq; XP_016632205.1; XM_016776663.1.
DR   AlphaFoldDB; A0A0D2JWX9; -.
DR   STRING; 1442371.A0A0D2JWX9; -.
DR   GeneID; 27711908; -.
DR   VEuPathDB; FungiDB:Z520_06162; -.
DR   OrthoDB; 318925at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   InterPro; IPR013860; AreA_GATA.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071:SF333; NITROGEN REGULATORY PROTEIN AREA; 1.
DR   PANTHER; PTHR10071; TRANSCRIPTION FACTOR GATA FAMILY MEMBER; 1.
DR   Pfam; PF08550; DUF1752; 1.
DR   Pfam; PF00320; GATA; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT   DOMAIN          709..762
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50114"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..858
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  102526 MW;  B4B793D9AF1D5255 CRC64;
     MSSADEGERG GTAAATSRAT SAIQSPADHS HHSSASTSQP SSTLDDADFS TWSSSLGSHT
     VNTLSTGQSP SHLFSTDTSN KSSANFPAPT KAANPSLNPN LDLSTTDVLA RNESLLRDAV
     FPEWKDDAHS SDLDSPEEMQ KKDPLGTQIW KLYSRTKSRL PNQERMENLT WRMMAMNLRR
     REQQQAAYGN PAPVDSDRLS AATDRLPRAK QAQFKNPAPP SSAPSGIAQQ LRKSVDKSAE
     TEQAADPMNL DDFIVPSSVA SPAGMTSPAP SEAAGRPKTT QAPPIPITTR NKPQVQIPKN
     LPPSSMPQTS IPTHRTSEFE YVKKRVRKTS IDERRGNRKR PAEFSPQVPP LPGPHATNGT
     EMDTGVPDYV LDQTTAAQFP GQPNFQGSMS LHLDSFHLSD DPILTSAGPF QQNFAFSPAA
     SPMVTNGPFS NVYTQSSMGS SLNSADFYSP PQSGYPSAVS TPQPGHEVDG QGFYFDQSGH
     TRTMPFYPPH RGTHLMTPAA PQFAYGSNNE QVYSLMNGVP SAQTANGFSM QQHVDPSRVL
     VPEYGRRVSP GVSVAGNDNL FQFGADSDGE DDDANFAMIQ AEYGQISDPT LDLNSSLQWD
     PNVADYGNVQ RFGSGPGKQV RIGGAEMVNS PPDWGSSMLS RTHGSAASIS DIRNRDQDPR
     RQKIPRTTST PALSNQHMQS TGSSPGESGF SSRQPSRPGS PGPKSTDQNG VPTTCTNCFT
     QTTPLWRRNP EGHPLCNACG LFLKLHGVVR PLSLKTDVIK KRNRGSGNTV PMGSAATRAS
     KKASRKNSVQ QTPATTPTSG NAASEQNSAS PSSVQGSAHS GSVVTTPTSY PPGTTGGKPG
     VVPIAAAPPK PPVQPGPNMA RPVQVTPKRQ RRQSRASTNT LPIITGNSGP SNEAEMHDAS
     QSTPKVTQAP VTRAKAASMS STAGATTMAS VMQQGALLNS GVQTMGSGPH GNSQEWEWLT
     MSL
//
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