PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID MDP0000485895
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Malus
Family HSF
Protein Properties Length: 85aa    MW: 9631.98 Da    PI: 10.2853
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
MDP0000485895genomeGDRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind422.5e-1317584090
                   THHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXX CS
   HSF_DNA-bind 40 vLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgk 90
                   +Lpk+Fk +nf+SF+ QLn+YgF kv+ ++         weF+++ F+  k
  MDP0000485895 17 LLPKHFKDNNFSSFILQLNTYGFIKVDPDR---------WEFANERFQGRK 58
                   79*************************999.........********8654 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM004154.3E-5166IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000565.2E-71729IPR000232Heat shock factor (HSF)-type, DNA-binding
SuperFamilySSF467851.63E-101756IPR011991Winged helix-turn-helix DNA-binding domain
PfamPF004473.5E-101758IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene3DG3DSA:1.10.10.104.0E-141756IPR011991Winged helix-turn-helix DNA-binding domain
PRINTSPR000565.2E-73042IPR000232Heat 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: 85 aa     Download sequence    Send to blast
MLGKASLFRT CTNSPGLLPK HFKDNNFSSF ILQLNTYGFI KVDPDRWEFA NERFQGRKRW  60
ATIIRAQGES EVAKFISDAT TRCG*
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).
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: DNA-binding capacity is reduced by HSBP in vitro. {ECO:0000269|PubMed:20388662}.
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_009361628.13e-19PREDICTED: heat stress transcription factor A-2-like
RefseqXP_009361629.13e-19PREDICTED: heat stress transcription factor A-2-like
SwissprotO818211e-16HFA1B_ARATH; Heat stress transcription factor A-1b
TrEMBLA0A498KFB62e-17A0A498KFB6_MALDO; Uncharacterized protein
STRINGXP_009361628.11e-18(Pyrus x bretschneideri)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF16123393
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G16820.25e-19heat shock factor 3
Publications ? help Back to Top
  1. Hsu SF,Jinn TL
    AtHSBP functions in seed development and the motif is required for subcellular localization and interaction with AtHSFs.
    Plant Signal Behav, 2010. 5(8): p. 1042-4
    [PMID:20657173]
  2. Bechtold U, et al.
    Arabidopsis HEAT SHOCK TRANSCRIPTION FACTORA1b overexpression enhances water productivity, resistance to drought, and infection.
    J. Exp. Bot., 2013. 64(11): p. 3467-81
    [PMID:23828547]
  3. Guan Q,Yue X,Zeng H,Zhu J
    The protein phosphatase RCF2 and its interacting partner NAC019 are critical for heat stress-responsive gene regulation and thermotolerance in Arabidopsis.
    Plant Cell, 2014. 26(1): p. 438-53
    [PMID:24415771]