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_016651918.1
Organism
Prunus mume
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Amygdaleae; Prunus
Family HSF
Protein Properties Length: 466aa    MW: 52099.9 Da    PI: 5.2754
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_016651918.1genomeBGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind113.41.5e-351051962102
                     HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXXXXXXXX CS
    HSF_DNA-bind   2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgkkellek 96 
                     Fl+k++++++d++l+++isw + gnsfvv+d+ ef++ +Lp+ Fkh+nf+SFvRQLn+YgF+kv++++         weF ++ Fk+gk++ll+k
  XP_016651918.1 105 FLSKTFDLVDDPSLDSIISWGSGGNSFVVWDPLEFSRLILPRNFKHNNFSSFVRQLNTYGFRKVDTDK---------WEFGNEAFKRGKRHLLKK 190
                     9****************************************************************999.........****************** PP

                     XXXXXX CS
    HSF_DNA-bind  97 ikrkks 102
                     i+r+ks
  XP_016651918.1 191 IQRRKS 196
                     ****98 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM004158.2E-56101194IPR000232Heat shock factor (HSF)-type, DNA-binding
SuperFamilySSF467851.36E-34101194IPR011991Winged helix-turn-helix DNA-binding domain
Gene3DG3DSA:1.10.10.108.6E-37102194IPR011991Winged helix-turn-helix DNA-binding domain
PfamPF004471.9E-30105194IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000566.2E-18105128IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000566.2E-18143155IPR000232Heat shock factor (HSF)-type, DNA-binding
PROSITE patternPS004340144168IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000566.2E-18156168IPR000232Heat 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: 466 aa     Download sequence    Send to blast
MNPKDESYPK SPPTSAELNP ENPFRPEMSE PLLGSQSIPS FTSPLMEFEA FCALNPSESS  60
WSSGAFEFDE KAPTATSSFM DAGGAEHVAV PQPLECLQDS PVPPFLSKTF DLVDDPSLDS  120
IISWGSGGNS FVVWDPLEFS RLILPRNFKH NNFSSFVRQL NTYGFRKVDT DKWEFGNEAF  180
KRGKRHLLKK IQRRKSPQSL QVGPSAEAGR PRLEGDIETL RKERSMLMQE VGDLQQEQLG  240
TVHHMKVVKE RLQSAEQRQK QMVSFLSKLL QNPAFLARLQ QKTGQKGIDS PRMKRKFVKQ  300
HQHELGKSDS CMQGQIVKYQ PAWRNLSVVP EVNPVVPIEQ SPDNLSQVMA GKLGLVAESK  360
PYQFADVASD ELNLSAEPAV MRGVIKTPEE EGEGASSMGA EDPFQKGKSV LSPEQEVNPE  420
YHVCFQEDFG KNKMFPELFS PGIDSMIKQE DIWSMGFDVS AGLNPC
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2ldu_A7e-2410019915125Heat shock factor protein 1
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1187193LKKIQRR
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_016651918.1
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_016651918.10.0PREDICTED: heat stress transcription factor A-3 isoform X4
SwissprotQ8GYY15e-92HSFA3_ARATH; Heat stress transcription factor A-3
TrEMBLA0A251NAA00.0A0A251NAA0_PRUPE; Uncharacterized protein
STRINGXP_008241431.10.0(Prunus mume)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G03720.14e-94heat 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]