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 Cla021884
Organism
Citrullus lanatus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Citrullus
Family Whirly
Protein Properties Length: 336aa    MW: 37742.2 Da    PI: 8.8266
Description Whirly family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Cla021884genomeICuGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Whirly176.74.8e-55962061111
     Whirly   1 svyktkaalkvkavrptfealdsgnlklkraGglllelanataerkydWekkqsfalsatevaelvdlaskesceffhdpaakgsneGkvrkalkvePlp 100
                s+yk+kaal+v+++ p+f+ ldsg++k++r+G++ll++a+a+++r+ydW++kq+f+ls+te+++lv l+++esceffhdp +++s+eGkvrk lkvePlp
  Cla021884  96 SIYKGKAALTVEPRPPEFTPLDSGAFKISREGFVLLQFAPAAGVRQYDWSRKQVFSLSVTELGSLVALGPRESCEFFHDPYKGKSDEGKVRKILKVEPLP 195
                7*************************************************************************************************** PP

     Whirly 101 dGsGlfvnlsv 111
                dGsG+f+nls 
  Cla021884 196 DGSGHFFNLSK 206
                *********85 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:2.30.31.101.1E-5487207IPR009044ssDNA-binding transcriptional regulator
SuperFamilySSF544475.18E-4989206IPR009044ssDNA-binding transcriptional regulator
PfamPF085364.1E-5197207IPR013742Plant transcription factor
SuperFamilySSF544476.98E-20265336IPR009044ssDNA-binding transcriptional regulator
Gene3DG3DSA:2.30.31.103.8E-14266317IPR009044ssDNA-binding transcriptional regulator
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006281Biological ProcessDNA repair
GO:0032211Biological Processnegative regulation of telomere maintenance via telomerase
GO:0045893Biological Processpositive regulation of transcription, DNA-templated
GO:0045910Biological Processnegative regulation of DNA recombination
GO:0009508Cellular Componentplastid chromosome
GO:0009570Cellular Componentchloroplast stroma
GO:0003697Molecular Functionsingle-stranded DNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0003723Molecular FunctionRNA binding
GO:0042162Molecular Functiontelomeric DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 336 aa     Download sequence    Send to blast
MLRLQWLSSS LVPSFNSELS PETVSNCKLG SLNSFRPLLT LTTTRKPSPK CQYSWNTQQQ  60
QQQSAFEPGS QTDSFASQTR AGAAAALPPR FFVGHSIYKG KAALTVEPRP PEFTPLDSGA  120
FKISREGFVL LQFAPAAGVR QYDWSRKQVF SLSVTELGSL VALGPRESCE FFHDPYKGKS  180
DEGKVRKILK VEPLPDGSGH FFNLSKSCIE TFMIHLRLNV NAEFCFMDVQ LKRGYMLPPT  240
IDPVNCIDAR GSLFPTYIFC SILMHKGVQN KLINVDESIY IPITKAEYTV LVEAFKFILP  300
HLMGWHTIAN TITRPEDSSR VNNANPRYGG DFEWNR
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
4koo_A5e-73843122168Single-stranded DNA-binding protein WHY1, chloroplastic
4koo_B5e-73843122168Single-stranded DNA-binding protein WHY1, chloroplastic
4koo_C5e-73843122168Single-stranded DNA-binding protein WHY1, chloroplastic
4koo_D5e-73843122168Single-stranded DNA-binding protein WHY1, chloroplastic
Search in ModeBase
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 -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankLN6818212e-50LN681821.1 Cucumis melo genomic scaffold, anchoredscaffold00040.
GenBankLN7132572e-50LN713257.1 Cucumis melo genomic chromosome, chr_3.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_008456468.11e-129PREDICTED: single-stranded DNA-binding protein WHY1, chloroplastic-like
SwissprotQ9M9S32e-72WHY1_ARATH; Single-stranded DNA-binding protein WHY1, chloroplastic
TrEMBLA0A1S3C3B01e-128A0A1S3C3B0_CUCME; single-stranded DNA-binding protein WHY1, chloroplastic-like
STRINGXP_008456468.11e-129(Cucumis melo)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF64163251
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G14410.12e-74ssDNA-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]