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Database: UniProt
Entry: C1G0D1_PARBD
LinkDB: C1G0D1_PARBD
Original site: C1G0D1_PARBD 
ID   C1G0D1_PARBD            Unreviewed;       659 AA.
AC   C1G0D1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=HSF-type DNA-binding domain-containing protein {ECO:0000259|PROSITE:PS00434};
GN   ORFNames=PADG_00321 {ECO:0000313|EMBL:EEH44032.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH44032.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH44032.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH44032.2,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000256|RuleBase:RU004020}.
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DR   EMBL; KN275957; EEH44032.2; -; Genomic_DNA.
DR   RefSeq; XP_010755781.1; XM_010757479.1.
DR   AlphaFoldDB; C1G0D1; -.
DR   STRING; 502780.C1G0D1; -.
DR   GeneID; 22580178; -.
DR   KEGG; pbn:PADG_00321; -.
DR   VEuPathDB; FungiDB:PADG_00321; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_031225_0_0_1; -.
DR   InParanoid; C1G0D1; -.
DR   OMA; SALWEFK; -.
DR   OrthoDB; 1117127at2759; -.
DR   Proteomes; UP000001628; 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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR027725; HSF_fam.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10015:SF396; FLOCCULATION SUPPRESSION PROTEIN; 1.
DR   PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT   DOMAIN          167..191
FT                   /note="HSF-type DNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00434"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..659
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   659 AA;  71597 MW;  A3FB62988E5813BC CRC64;
     MNRIQEPPSR SPFSGPTDVS NKSRTIPVLS SSISPSDHPQ GDPMDLSPSS PATMAPPGNN
     NGDSPETEHA GGASNNNTNS NTNSNTINHS TNGAAPASTM IGGDSGHALN QPIGAAAAAQ
     QPKVVQTAFI HKLYSMLQDP GIQHLISWSS TNESFVMSPS QDFAKVLAQY FKHTNVSSFV
     RQLNMYGFHK VSDVFHTGSP DSQMWEFKHG NGNFKKGDVA GLREIRRRAS RQTLIHRDSF
     SGHKPNASQP GTPAEPTPDS SDSRVIDSRL LNTEHNIFEL YSRLSRVEEN YSMLASRCQA
     LTESLVRCHQ WSNSMSHFVM SLVPDPENAI HRDAANMQRE VSRQLDAIRS LENPHESLLS
     GRQPYFGSMT LHSGPPLSPR QMPQDDNRRS SMAQPPVPVH LSVSPRRYGS IGAANTSPDY
     NRSHIPTHYS ATTATHQLHP LSAVSSAPGT NLGRRHTSAD IREHWASTTT NNTYPFGSIN
     PNHPSSSSQW PPSPQRTGPP NNPVHNPMSM SMSMNMNMNP VPNAGDHQHV RDVLAKYEMG
     GPRRQASSRH PTPPLPPIAI DPVAANTNTN NNNNNNTATT TPPHAPPHAS SSSSSTLNPE
     SGWSIGGPKF PRPTDSSLPA TRRSSMASNV HSLLNPTATA ERPDEDDGAG EDRKRKRLQ
//
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