ID W9J9Z8_FUSOX Unreviewed; 1020 AA.
AC W9J9Z8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=White collar 1 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOYG_01134 {ECO:0000313|EMBL:EWZ01525.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWZ01525.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWZ01525.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH717839; EWZ01525.1; -; Genomic_DNA.
DR AlphaFoldDB; W9J9Z8; -.
DR HOGENOM; CLU_007918_2_0_1; -.
DR OrthoDB; 728091at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR47429:SF7; GATA-FACTOR; 1.
DR PANTHER; PTHR47429; PROTEIN TWIN LOV 1; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT DOMAIN 363..385
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 532..602
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 669..721
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 873..902
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 111658 MW; CEACADA16CF73A37 CRC64;
MDGYYSPHQQ QQPPQQFQQP RMQQNQQNHM QHNMNDPTFY QGGDSLDDIV RDNQDKLYRR
QSMPQAFTTP MGQFQVNQQQ QQQGQRRMSS VGNGDMMTFG TDNADLNSYQ FNQPPMGGGF
PTINTSIGMD QMGNYMTSDP NDYSTISPDM MSSMMPSTFA SMSVGAQMAG NASSMNLYSP
SMSQFPQGQL TPQVPVGNDF SMDLSPDAGS MNTNQSNPPA TTPIPAPTNN AMDTIEDSGD
SMMNHQTFNN MNAGDSNQNL PALSRQVSIA SGSVVSPPQQ HSHGAMSSST VTHPTSTSVA
TTPSTGDAPR DSKEKTIYSK SGFDMLKALW LVATRKNPRI QLGAVDMSCA FVVCDVSMND
CPIIYVSDNF QNLTGYSRHE IVGQNCRFLQ APDGKVEAGS KREFVDDGAV YNLKKMVHEG
REVQQSLINY RKGGKPFLNL LTMIPIPWDT DEIRYFIGFQ IDLVECPDAI ASNQDLGGVK
VNYKHSDIGQ YIWTPPQSSQ WEPDNGQTLG VDDVSTLLQQ FSPKGLTSDW HKQSWDKMLL
ENTDDVVHVL SLKGLFLYLS PSCKKVLEYE AADLVGNSLS TVCHPSDIVP VTRELKDTTT
GNPVNIVFRI RRKHSGYTWF ESHGSLFVEQ GKGRKCIILV GRKRPVFALS RRNLEANGGI
GDSELWTKLS TSGLFLYVSS NIRSLLDLQP DSLVGTSIQD LMRKESRPEF GRTLEKARRG
KIVTCKHEVQ NRRGQVLQAQ TTLYPGDASE GQKPSFLLAQ TKLLKASSRN LAPASTGSRS
LAATPRSSNG TENHATGHIS QPAGGALAPG SQDAALASED NIFDELRTTK CSSWQFELRQ
MEKVNRILAE ELGGLLSSKK KRKRRKGVGN VVRDCANCHT RNTPEWRRGP SGQRDLCNSC
GLRWAKQTGR VSPRNSSRGA NTVNGDARSK KSNSPSSPLH KELSADNSKA QTPKGESGIN
PAQLTKQKIE NGTSAPSGAP SATGVKSSAG MPPLSHSSML GVGQASSMAS IREERETSQP
//
