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 Itr_sc000862.1_g00006.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea
Family NF-YC
Protein Properties Length: 142aa    MW: 14844.1 Da    PI: 10.6676
Description NF-YC family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Itr_sc000862.1_g00006.1genomeKazusaView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1NF-YC24.36.6e-08311051993
                    NF-YC  19 helPlarikkilkadedvkmisaeaPvllskacelfileltlrswlhaeenkrrtlkksdiaaavtrtdifdflv 93 
                               ++P+ ri + lka +  +++ aeaPv l+   e++  e+   + + a++nk++ +   +i+ av + +    l+
  Itr_sc000862.1_g00006.1  31 LQFPVGRIARFLKAGKYAERVGAEAPVYLAVVLEYLAAEVLELAGNAARDNKKNRIVPRQIQLAVRNDEELSKLL 105
                              589*************************************999*********************99887665444 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM004148.7E-7210130IPR002119Histone H2A
Gene3DG3DSA:1.10.20.102.1E-5914129IPR009072Histone-fold
PfamPF001251.2E-131896IPR007125Histone H2A/H2B/H3
CDDcd000744.75E-6420127No hitNo description
PRINTSPR006204.7E-492143IPR002119Histone H2A
SuperFamilySSF471133.29E-4124127IPR009072Histone-fold
PRINTSPR006204.7E-495065IPR002119Histone H2A
PRINTSPR006204.7E-496578IPR002119Histone H2A
PRINTSPR006204.7E-497993IPR002119Histone H2A
PfamPF162118.0E-1999132IPR032454Histone H2A, C-terminal domain
PRINTSPR006204.7E-49107125IPR002119Histone H2A
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0000786Cellular Componentnucleosome
GO:0005634Cellular Componentnucleus
GO:0003677Molecular FunctionDNA binding
GO:0046982Molecular Functionprotein heterodimerization activity
Sequence ? help Back to Top
Protein Sequence    Length: 142 aa     Download sequence    Send to blast
MSSGGGAGKG GAGRGKAKAT KSVSRSSKVG LQFPVGRIAR FLKAGKYAER VGAEAPVYLA  60
VVLEYLAAEV LELAGNAARD NKKNRIVPRQ IQLAVRNDEE LSKLLGDVTI ANGGVLPNIH  120
QTLLPKKAGS GKGEIDFASQ EF
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1eqz_A4e-5771342127PROTEIN (HISTONE H2A)
1eqz_E4e-5771342127PROTEIN (HISTONE H2A)
1hq3_A4e-5771342127HISTONE H2A-IV
1hq3_E4e-5771342127HISTONE H2A-IV
1tzy_A4e-5771342127Histone H2A-IV
1tzy_E4e-5771342127Histone H2A-IV
2aro_A4e-5771342127Histone H2A-IV
2aro_E4e-5771342127Histone H2A-IV
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtVariant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation (By similarity). {ECO:0000250}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_020204559.16e-81histone H2AX
RefseqXP_028226627.16e-81histone H2AX-like
SwissprotQ9S9K71e-80H2AXB_ARATH; Probable histone H2AXb
TrEMBLA0A151R5971e-79A0A151R597_CAJCA; Histone H2A
TrEMBLA0A445LGF93e-79A0A445LGF9_GLYSO; Histone H2A (Fragment)
STRINGXP_008451417.12e-79(Cucumis melo)
STRINGXP_004148883.12e-79(Cucumis sativus)
STRINGXP_004171385.12e-79(Cucumis sativus)
STRINGGLYMA19G42760.11e-79(Glycine max)
STRINGXP_007147093.11e-79(Phaseolus vulgaris)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA16469
Publications ? help Back to Top
  1. Friesner JD,Liu B,Culligan K,Britt AB
    Ionizing radiation-dependent gamma-H2AX focus formation requires ataxia telangiectasia mutated and ataxia telangiectasia mutated and Rad3-related.
    Mol. Biol. Cell, 2005. 16(5): p. 2566-76
    [PMID:15772150]
  2. Ebbs ML,Bender J
    Locus-specific control of DNA methylation by the Arabidopsis SUVH5 histone methyltransferase.
    Plant Cell, 2006. 18(5): p. 1166-76
    [PMID:16582009]
  3. Yi H,Sardesai N,Fujinuma T,Chan CW,Gelvin SB
    Constitutive expression exposes functional redundancy between the Arabidopsis histone H2A gene HTA1 and other H2A gene family members.
    Plant Cell, 2006. 18(7): p. 1575-89
    [PMID:16751347]
  4. Sanchez-Moran E,Santos JL,Jones GH,Franklin FC
    ASY1 mediates AtDMC1-dependent interhomolog recombination during meiosis in Arabidopsis.
    Genes Dev., 2007. 21(17): p. 2220-33
    [PMID:17785529]
  5. Charbonnel C,Gallego ME,White CI
    Xrcc1-dependent and Ku-dependent DNA double-strand break repair kinetics in Arabidopsis plants.
    Plant J., 2010. 64(2): p. 280-90
    [PMID:21070408]
  6. Lang J, et al.
    Plant γH2AX foci are required for proper DNA DSB repair responses and colocalize with E2F factors.
    New Phytol., 2012. 194(2): p. 353-63
    [PMID:22339405]
  7. Qi Y,Zhang Y,Baller JA,Voytas DF
    Histone H2AX and the small RNA pathway modulate both non-homologous end-joining and homologous recombination in plants.
    Mutat. Res., 2016. 783: p. 9-14
    [PMID:26687994]
  8. Ryu TH,Kim JK,Kim JI,Kim JH
    Transcriptome-based biological dosimetry of gamma radiation in Arabidopsis using DNA damage response genes.
    J Environ Radioact, 2018. 181: p. 94-101
    [PMID:29128690]
  9. Lai J, et al.
    The Transcriptional Coactivator ADA2b Recruits a Structural Maintenance Protein to Double-Strand Breaks during DNA Repair in Plants.
    Plant Physiol., 2018. 176(4): p. 2613-2622
    [PMID:29463775]