PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID KZV28447.1
Organism
Dorcoceras hygrometricum
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae; Loxocarpinae; Dorcoceras
Family HSF
Protein Properties Length: 444aa    MW: 49591.8 Da    PI: 5.1445
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
KZV28447.1genomeCNUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind1124e-35291212103
                   HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXXXXXXXXXX CS
  HSF_DNA-bind   2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgkkellekik 98 
                   Fl+k++e+++d++l+ +isw  ng+sfvv+d+ efa+ +Lp+ Fkh+nf+SFvRQLn+YgF+k+++++         weF+++ F +gkk+ll++i 
    KZV28447.1  29 FLSKTFELVDDPSLDAIISWGPNGDSFVVWDPVEFARLILPRNFKHNNFSSFVRQLNTYGFRKIDTDK---------WEFTNEGFVRGKKHLLKNIS 116
                   9****************************************************************999.........******************** PP

                   XXXXX CS
  HSF_DNA-bind  99 rkkse 103
                   r+ks+
    KZV28447.1 117 RRKSA 121
                   **986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF467853.2E-3624118IPR011991Winged helix-turn-helix DNA-binding domain
SMARTSM004157.2E-5925118IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene3DG3DSA:1.10.10.105.0E-3725118IPR011991Winged helix-turn-helix DNA-binding domain
PRINTSPR000569.3E-192952IPR000232Heat shock factor (HSF)-type, DNA-binding
PfamPF004474.0E-3129118IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000569.3E-196779IPR000232Heat shock factor (HSF)-type, DNA-binding
PROSITE patternPS0043406892IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000569.3E-198092IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0009408Biological Processresponse to heat
GO:0010200Biological Processresponse to chitin
GO:0005634Cellular Componentnucleus
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 444 aa     Download sequence    Send to blast
MEDGTTGGFN LFELPQPLES LQGIQVPPFL SKTFELVDDP SLDAIISWGP NGDSFVVWDP  60
VEFARLILPR NFKHNNFSSF VRQLNTYGFR KIDTDKWEFT NEGFVRGKKH LLKNISRRKS  120
AQSSQLIGTS SVSQNDTSRG VLESEIGLLR RERSLMMMEV VELQKQHKGM IQHLEDVNEK  180
LKGAENRQKQ MVAFLAKMFQ NPDVLARLRQ AKERSSVTSP RTMRKFLKHQ QQEIGASDSS  240
LKGQIVKYKS ELPDLPKPSV TSAFFDPLLI EQLSHFPFQA EGDSESFGAK HVPLEMETIA  300
QVESAMINEL LLPADEPFEV PVLGSIDPLG KGKDTFSTSP QSNPDQNFVT FQKDKGKNIS  360
GFSMLGTESS FKQENAWSSG FGDTAGMSSS SSQFWSNPRN FDGGAFGFSD ELLAAWDIES  420
LKPGVGSSPN EDDPCEAKYE KKDP
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2ldu_A8e-272612317125Heat shock factor protein 1
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtTranscriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Involved in heat stress response. Activated by DREB2A under heat stress. {ECO:0000269|PubMed:17999647, ECO:0000269|PubMed:18261981}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapKZV28447.1
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat stress. {ECO:0000269|PubMed:17999647, ECO:0000269|PubMed:18261981}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_011101504.11e-139heat stress transcription factor A-3-like
SwissprotQ8GYY12e-92HSFA3_ARATH; Heat stress transcription factor A-3
TrEMBLA0A2Z7B4H50.0A0A2Z7B4H5_9LAMI; Uncharacterized protein
STRINGEMJ040671e-125(Prunus persica)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA87272025
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G03720.17e-95heat shock transcription factor A3
Publications ? help Back to Top
  1. Jung HS, et al.
    Subset of heat-shock transcription factors required for the early response of Arabidopsis to excess light.
    Proc. Natl. Acad. Sci. U.S.A., 2013. 110(35): p. 14474-9
    [PMID:23918368]
  2. Ding Y, et al.
    Four distinct types of dehydration stress memory genes in Arabidopsis thaliana.
    BMC Plant Biol., 2013. 13: p. 229
    [PMID:24377444]
  3. Nie S,Yue H,Xing D
    A Potential Role for Mitochondrial Produced Reactive Oxygen Species in Salicylic Acid-Mediated Plant Acquired Thermotolerance.
    Plant Physiol., 2016.
    [PMID:26099269]
  4. Hu Z, et al.
    Histone acetyltransferase GCN5 is essential for heat stress-responsive gene activation and thermotolerance in Arabidopsis.
    Plant J., 2015. 84(6): p. 1178-91
    [PMID:26576681]
  5. Song C,Chung WS,Lim CO
    Overexpression of Heat Shock Factor Gene HsfA3 Increases Galactinol Levels and Oxidative Stress Tolerance in Arabidopsis.
    Mol. Cells, 2016. 39(6): p. 477-83
    [PMID:27109422]
  6. Kim GD,Cho YH,Lee BH,Yoo SD
    STABILIZED1 Modulates Pre-mRNA Splicing for Thermotolerance.
    Plant Physiol., 2017. 173(4): p. 2370-2382
    [PMID:28223317]
  7. Song C,Lee J,Kim T,Hong JC,Lim CO
    VOZ1, a transcriptional repressor of DREB2C, mediates heat stress responses in Arabidopsis.
    Planta, 2018. 247(6): p. 1439-1448
    [PMID:29536220]