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 XP_010558210.1
Organism
Tarenaya hassleriana
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Cleomaceae; Tarenaya
Family HSF
Protein Properties Length: 463aa    MW: 51039 Da    PI: 5.1375
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_010558210.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind1101.8e-34731652103
                     HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXXXXXXXX CS
    HSF_DNA-bind   2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgkkellek 96 
                     Fl+k++++++d++l+ +isw ++g sfvv+d+ efa+ +Lp+ Fkh+nf+SFvRQLn+YgF+k+++++         weF+++ F++gk +ll++
  XP_010558210.1  73 FLSKTFDLVDDPNLDPVISWGQTGLSFVVWDPVEFARVILPRSFKHNNFSSFVRQLNTYGFRKIDTDR---------WEFANEAFQRGKSHLLKN 158
                     9****************************************************************999.........****************** PP

                     XXXXXXX CS
    HSF_DNA-bind  97 ikrkkse 103
                     i+r++s+
  XP_010558210.1 159 IHRRRSS 165
                     ****987 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF467853.81E-3468162IPR011991Winged helix-turn-helix DNA-binding domain
SMARTSM004152.8E-5669162IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene3DG3DSA:1.10.10.101.8E-3670162IPR011991Winged helix-turn-helix DNA-binding domain
PRINTSPR000568.0E-187396IPR000232Heat shock factor (HSF)-type, DNA-binding
PfamPF004472.7E-3073162IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000568.0E-18111123IPR000232Heat shock factor (HSF)-type, DNA-binding
PROSITE patternPS004340112136IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000568.0E-18124136IPR000232Heat 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: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: 463 aa     Download sequence    Send to blast
MNPEKDNPPK PPPISTQPAS GSLYIETDMG FSASPLFSPL TGLEALSAGI CGGGETEMPQ  60
PLECLQGNPI PPFLSKTFDL VDDPNLDPVI SWGQTGLSFV VWDPVEFARV ILPRSFKHNN  120
FSSFVRQLNT YGFRKIDTDR WEFANEAFQR GKSHLLKNIH RRRSSQSQQA SSSCFFGSPP  180
EVRAEIEKLR KERKTLIAEV AELQQQQRGT ARDVDSVNER LQAAEQRQRQ MLSFLAKLFR  240
NPSFLECLRS HGEGRAFGPS SKTRRKFIKH QQHHQGSDLD SSPAGIQTLK HRADDFGSVE  300
VTTFLSTAEE GIPFRVGDVP LAERFSRQRA SSPGTEQQQE QYLDPKGKNS MNLPKESMSP  360
ECSASFPSPG WLESIAKQEE IWSMGFEASV SAMASSCNTE LWGDIINCDG PELGPVTTTA  420
GGLSDFCWDL GSEQLAVSGS EIGLSWATGG SSSLDDDALT KKD
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5d5u_B9e-24451622129Heat shock factor protein 1
5d5v_B9e-24451622129Heat shock factor protein 1
5d5v_D9e-24451622129Heat 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
PlantRegMapXP_010558210.1
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_010558210.10.0PREDICTED: heat stress transcription factor A-3-like
SwissprotQ8GYY11e-139HSFA3_ARATH; Heat stress transcription factor A-3
TrEMBLD7LWT01e-141D7LWT0_ARALL; AT-HSFA3
STRINGXP_010558210.10.0(Tarenaya hassleriana)
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-120heat 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]