ID   HSF_CRYNJ               Reviewed;         783 AA.
AC   Q5KMX8; Q55X04;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Heat shock transcription factor {ECO:0000303|PubMed:17040492};
DE            Short=HSTF {ECO:0000305};
DE   AltName: Full=Heat shock factor protein {ECO:0000305};
DE            Short=HSF {ECO:0000305};
GN   Name=HSF1 {ECO:0000303|PubMed:17040492};
GN   OrderedLocusNames=CNB00120 {ECO:0000312|EMBL:AAW41451.1};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684 {ECO:0000312|Proteomes:UP000002149};
RN   [1] {ECO:0000312|Proteomes:UP000002149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565 {ECO:0000312|Proteomes:UP000002149};
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
RN   [2] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH SSA1, AND SUBCELLULAR LOCATION.
RX   PubMed=17040492; DOI=10.1111/j.1365-2958.2006.05422.x;
RA   Zhang S., Hacham M., Panepinto J., Hu G., Shin S., Zhu X., Williamson P.R.;
RT   "The Hsp70 member, Ssa1, acts as a DNA-binding transcriptional co-activator
RT   of laccase in Cryptococcus neoformans.";
RL   Mol. Microbiol. 62:1090-1101(2006).
CC   -!- FUNCTION: DNA-binding transcription factor that specifically binds heat
CC       shock promoter elements (HSE) and activates transcription
CC       (PubMed:17040492). Together with its coregulator SSA1, activates
CC       expression of laccase LAC1 during glucose starvation (PubMed:17040492).
CC       {ECO:0000269|PubMed:17040492}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Homotrimerization increases the
CC       affinity of HSF1 to DNA (By similarity). Interacts with transcriptional
CC       coregulator SSA1 on chromatin (PubMed:17040492).
CC       {ECO:0000250|UniProtKB:P10961, ECO:0000269|PubMed:17040492}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17040492}.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000255|RuleBase:RU004020}.
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   EMBL; AE017342; AAW41451.1; -; Genomic_DNA.
DR   RefSeq; XP_568758.1; XM_568758.1.
DR   AlphaFoldDB; Q5KMX8; -.
DR   SMR; Q5KMX8; -.
DR   STRING; 5207.AAW41451; -.
DR   PaxDb; Q5KMX8; -.
DR   EnsemblFungi; AAW41451; AAW41451; CNB00120.
DR   GeneID; 3255945; -.
DR   KEGG; cne:CNB00120; -.
DR   VEuPathDB; FungiDB:CNB00120; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_015858_1_0_1; -.
DR   InParanoid; Q5KMX8; -.
DR   OMA; AQMFLNS; -.
DR   OrthoDB; 1154048at2759; -.
DR   Proteomes; UP000002149; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 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; PTHR10015; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..783
FT                   /note="Heat shock transcription factor"
FT                   /id="PRO_0000452016"
FT   DNA_BIND        78..168
FT                   /evidence="ECO:0000250|UniProtKB:P10961"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..333
FT                   /note="Involved in trimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P22121"
FT   REGION          350..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  81501 MW;  596C577352079DF7 CRC64;
     MTTNLYAIAG PSKPTTPTST PSPRSEPPSP LKSLTSLPTN PLNSHGTSTP NTLTNQLSST
     GIGISKPGLS VDENGEVMKV PAFLNKLYTM VSDPEVDDLI YWGESGDSFF VPNAELFGRE
     LLPRWFKHSN FSSFVRQLNM YGFHKVPHLQ SGALKNETPI ELWEFANPYF KRGQPQLLTK
     VTRKNNRPSN SGVGPSSSVG GSGAGGGMST RSASAAAASG SASGQIQQAI SQGHEAGNHS
     TSGKYLITDG TTPGSVPPSH TSAGPLIAPQ TLDLSAINSG IAAIRQTQAS IATDLRKLQA
     SNEALWRQAY ETQEKQRKHE ETIDLIVSFL ERLFGTEGEG LKGLKEAMRR GVGVRRDRDG
     REGRDSRDSR FAEDDDGGQK KRRRVGIDRM IEGGTGDGTG EHGEIESPTS DDRLVEIGSN
     SEYSIPSVKR TSSSSHPISL GQLGSSRFTA LPSEDPSPSA SGPGSTSYEG LHTTQTNARG
     AGADVNVTDP TLGMNHLSPL SDTDPLLPSS SNALAPYSSH LPFPSSNSNQ SNSFNPSNPS
     SAWASNPSQP LLSPTSAAAA AHAYNLDPSL LQTTIGSLLQ SPAAAQMFLN SLSASAQGQA
     LASHSHPHNP SPLNPNPNGN ASTSASASAH GMNTGGMGTG SGTKDVDPTL ALFSPLPSHS
     SLTSQSNDLL KSYSDALTVG EGVDNLQESI DSLVRSMGLD LPNGGSSVGV DVGDGAGVGT
     ETGEGDGEFN VDEFLQGLAK EGEEEGEREV EGDGGVSSSG AGAGAENGRK EDVIAQSGLK
     SES