PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID AA19G00216
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Aethionemeae; Aethionema
Family HSF
Protein Properties Length: 384aa    MW: 43852.4 Da    PI: 5.1105
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
AA19G00216genomeVEGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind108.93.8e-34551462102
                   HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXXXXXXXXXX CS
  HSF_DNA-bind   2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgkkellekik 98 
                   Fl+k+++++++++l+ +isw ++g sfvv+++ efa+ +Lp+ Fkh+nf+SFvRQLn+YgF+k+++++         weF+++ F +gkk+ll++i+
    AA19G00216  55 FLSKTFDLVDEPSLDPIISWGQTGASFVVWEPMEFARIILPRNFKHNNFSSFVRQLNTYGFRKIDTDR---------WEFANECFLRGKKHLLKNIH 142
                   9****************************************************************999.........******************** PP

                   XXXX CS
  HSF_DNA-bind  99 rkks 102
                   r++s
    AA19G00216 143 RRRS 146
                   *986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF467851.43E-3450144IPR011991Winged helix-turn-helix DNA-binding domain
SMARTSM004151.1E-5651144IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene3DG3DSA:1.10.10.103.4E-3652144IPR011991Winged helix-turn-helix DNA-binding domain
PRINTSPR000567.7E-185578IPR000232Heat shock factor (HSF)-type, DNA-binding
PfamPF004474.6E-3055144IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000567.7E-1893105IPR000232Heat shock factor (HSF)-type, DNA-binding
PROSITE patternPS00434094118IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000567.7E-18106118IPR000232Heat 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: 384 aa     Download sequence    Send to blast
MIQMSAERDD VSKSKSSIPN SLYVDTDMGF SGSPLTSPLA PMPLDILQGN PIPPFLSKTF  60
DLVDEPSLDP IISWGQTGAS FVVWEPMEFA RIILPRNFKH NNFSSFVRQL NTYGFRKIDT  120
DRWEFANECF LRGKKHLLKN IHRRRSLQSQ QLCTSTSQGS PTEVVGGEIE KLRKERQALM  180
EEVVELQQQH RGTTHHMDTV NQRLKAAEQR QKQMLSFLAK LFQNPGFLER LKNQKLEAEQ  240
GGSLRRKLIK TRSNSPTEGQ IVKYEADEWE KLLKSDQELI GQGSSNIVTD QRGKKIMNPE  300
EDMMNSDYLM SFSSPRELDD NVKEEEIWSM GFNDPIQDLS SSNVWGTPME FSLPDISWEQ  360
VAGASRESGF DWPNPGDDNM PTKD
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2ldu_A1e-245214417120Heat shock factor protein 1
5d5u_B1e-245214426129Heat shock factor protein 1
5d5v_B1e-245214426129Heat shock factor protein 1
5d5v_D1e-245214426129Heat 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
PlantRegMapAA19G00216
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_002873110.11e-177heat stress transcription factor A-3
SwissprotQ8GYY11e-173HSFA3_ARATH; Heat stress transcription factor A-3
TrEMBLD7LWT01e-175D7LWT0_ARALL; AT-HSFA3
STRINGscaffold_600303.11e-176(Arabidopsis lyrata)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM109502529
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G03720.11e-167heat 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]