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 Pta003932
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Acrogymnospermae; Pinidae; Pinales; Pinaceae; Pinus; Pinus
Family Whirly
Protein Properties Length: 259aa    MW: 28678.8 Da    PI: 9.0372
Description Whirly family protein
Gene Model
Gene Model ID Type Source Coding Sequence
gnl|UG|Pta#S24904783PU_unrefUnigeneView CDS
PUT-157a-Pinus_taeda-20875PU_refplantGDBView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Whirly167.24.3e-52792162139
     Whirly   2 vyktkaalkvkavrptfealdsgnlklkraGglllelanataerkydWekkqsfalsatevaelvdlaskesceffhdpaakgsneGkvrkalkvePlpd 101
                +yk+kaal +++++p++++ldsg ++l+++G ++le+a+a+++r+ydW+kkq fals+ e+++l+++ +ke+ceffhdp+ ++s++Gk++k+lkv  l d
  Pta003932  79 LYKGKAALGIQPKAPEYTTLDSGGIRLSKEGCVFLEFAPAVGTRQYDWSKKQIFALSVLELGTLLSFDPKEPCEFFHDPFLGKSEAGKIQKVLKVGMLQD 178
                7*************************************************************************************************** PP

     Whirly 102 GsGlfvnlsvtnslvkgnesfsvPvskaefavlrsllv 139
                  G+f+nl v+   ++ +es+ +P++k+ef+v++s+++
  Pta003932 179 AGGYFFNLRVSDRTLNIDESLFMPITKGEFSVMQSAFN 216
                ***********************************996 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS512575116No hitNo description
Gene3DG3DSA:2.30.31.103.1E-6968238IPR009044ssDNA-binding transcriptional regulator
SuperFamilySSF544473.84E-6272256IPR009044ssDNA-binding transcriptional regulator
PfamPF085362.5E-5179214IPR013742Plant transcription factor
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0003677Molecular FunctionDNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 259 aa     Download sequence    Send to blast
MLRFHGLGTH FLGAACARPI QPLRTASISS RSFLKVVKAS FNDDSSQSHS FSSSPDHSAV  60
TQPGFLRGQP SKIYVKYTLY KGKAALGIQP KAPEYTTLDS GGIRLSKEGC VFLEFAPAVG  120
TRQYDWSKKQ IFALSVLELG TLLSFDPKEP CEFFHDPFLG KSEAGKIQKV LKVGMLQDAG  180
GYFFNLRVSD RTLNIDESLF MPITKGEFSV MQSAFNFILP YLMGWHAYMN SEKPNESGHL  240
TSASPSIGKK AELEWDVPF
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1l3a_A8e-767225737220p24: plant transcriptional regulator PBF-2
1l3a_B8e-767225737220p24: plant transcriptional regulator PBF-2
1l3a_C8e-767225737220p24: plant transcriptional regulator PBF-2
1l3a_D8e-767225737220p24: plant transcriptional regulator PBF-2
Search in ModeBase
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Pta.105790.0root| xylem
Functional Description ? help Back to Top
Source Description
UniProtSingle-stranded DNA-binding protein that functions in both chloroplasts and nucleus. In chloroplasts, maintains plastid genome stability by preventing break-induced and short homology-dependent illegitimate recombinations. In nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo. {ECO:0000269|PubMed:14960277, ECO:0000269|PubMed:17217467, ECO:0000269|PubMed:19666500, ECO:0000269|PubMed:19669906, ECO:0000269|PubMed:20551348, ECO:0000269|PubMed:21911368}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By salicylic acid (SA) and infection by H.parasitica. {ECO:0000269|PubMed:14960277, ECO:0000269|PubMed:19669906}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqNP_172893.18e-81ssDNA-binding transcriptional regulator
RefseqXP_018447906.19e-81PREDICTED: single-stranded DNA-binding protein WHY1, chloroplastic
SwissprotQ9M9S37e-82WHY1_ARATH; Single-stranded DNA-binding protein WHY1, chloroplastic
TrEMBLA9NQE81e-119A9NQE8_PICSI; Uncharacterized protein
STRINGAT1G14410.13e-80(Arabidopsis thaliana)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G14410.18e-84ssDNA-binding transcriptional regulator
Publications ? help Back to Top
  1. Lepage É,Zampini É,Brisson N
    Plastid genome instability leads to reactive oxygen species production and plastid-to-nucleus retrograde signaling in Arabidopsis.
    Plant Physiol., 2013. 163(2): p. 867-81
    [PMID:23969600]
  2. Carella P,Wilson DC,Cameron RK
    Some things get better with age: differences in salicylic acid accumulation and defense signaling in young and mature Arabidopsis.
    Front Plant Sci, 2014. 5: p. 775
    [PMID:25620972]
  3. Zampini É,Lepage É,Tremblay-Belzile S,Truche S,Brisson N
    Organelle DNA rearrangement mapping reveals U-turn-like inversions as a major source of genomic instability in Arabidopsis and humans.
    Genome Res., 2015. 25(5): p. 645-54
    [PMID:25800675]
  4. Ren Y,Li Y,Jiang Y,Wu B,Miao Y
    Phosphorylation of WHIRLY1 by CIPK14 Shifts Its Localization and Dual Functions in Arabidopsis.
    Mol Plant, 2017. 10(5): p. 749-763
    [PMID:28412544]
  5. Karpinska B,Alomrani SO,Foyer CH
    Inhibitor-induced oxidation of the nucleus and cytosol in Arabidopsis thaliana: implications for organelle to nucleus retrograde signalling.
    Philos. Trans. R. Soc. Lond., B, Biol. Sci., 2018.
    [PMID:28808105]
  6. Huang D,Lin W,Deng B,Ren Y,Miao Y
    Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis.
    Int J Mol Sci, 2018.
    [PMID:29112140]
  7. Guan Z,Wang W,Yu X,Lin W,Miao Y
    Comparative Proteomic Analysis of Coregulation of CIPK14 and WHIRLY1/3 Mediated Pale Yellowing of Leaves in Arabidopsis.
    Int J Mol Sci, 2018.
    [PMID:30065159]