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 RrC1700_p1
Organism
Raphanus raphanistrum
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus
Family ERF
Protein Properties Length: 794aa    MW: 89863.6 Da    PI: 5.5433
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
RrC1700_p1genomeMSUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP260.63.7e-19636685255
         AP2   2 gykGVrwdkkrgrWvAeIrdpsengkr.krfslgkfgtaeeAakaaiaarkkleg 55 
                 +y+GVr+++ +g+W+AeIrdp+    + +r++lg+f tae+Aa a+++a++k++g
  RrC1700_p1 636 HYRGVRQRP-WGKWAAEIRDPK----KaARVWLGTFETAEDAALAYDRAALKFKG 685
                 7********.**********94....45************************987 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PfamPF033213.3E-19815556IPR004993GH3 family
Gene3DG3DSA:3.30.730.103.0E-32635694IPR001471AP2/ERF domain
PfamPF008471.0E-12636685IPR001471AP2/ERF domain
PROSITE profilePS5103224.803636693IPR001471AP2/ERF domain
SuperFamilySSF541717.19E-22636694IPR016177DNA-binding domain
CDDcd000184.29E-33636694No hitNo description
SMARTSM003804.0E-38636699IPR001471AP2/ERF domain
PRINTSPR003676.8E-11637648IPR001471AP2/ERF domain
PRINTSPR003676.8E-11659675IPR001471AP2/ERF domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0009816Biological Processdefense response to bacterium, incompatible interaction
GO:0009863Biological Processsalicylic acid mediated signaling pathway
GO:0010112Biological Processregulation of systemic acquired resistance
GO:0016046Biological Processdetection of fungus
GO:0018874Biological Processbenzoate metabolic process
GO:0034052Biological Processpositive regulation of plant-type hypersensitive response
GO:0044419Biological Processinterspecies interaction between organisms
GO:0071456Biological Processcellular response to hypoxia
GO:0003677Molecular FunctionDNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0052625Molecular Function4-aminobenzoate amino acid synthetase activity
GO:0052626Molecular Functionbenzoate amino acid synthetase activity
GO:0052627Molecular Functionvanillate amino acid synthetase activity
GO:0052628Molecular Function4-hydroxybenzoate amino acid synthetase activity
Sequence ? help Back to Top
Protein Sequence    Length: 794 aa     Download sequence    Send to blast
MKLVSNNNEK WEEKLKSLTF NVKQIQDNLL EEILTPNLKT EYLQRFHMDR FDKELFKKNV  60
PVVTYEDIKP YIDRVVNGES SDVMSARPIT GFLLSSGTSG GAQKMMPWNN KYLDNLTFAY  120
DLRMHVITKH VKGLEEGKGM MFLFTKQEAI TPSGLPARVA TSSYFKSDYF KNRPSNWYYS  180
YTSPDEVILC SNNTQSLYCH LLCGLLQRDE VVRMGSIFAS VMVRAIKFLE TYWEELCSNI  240
RTGRLSEWIT DLGCRSSVSL VLGGPRPDLA DTIETVCNQS SWEGIVKRLW PNTKYIETVV  300
TGSMGQYVPT LNYYCSDLPL VSTTYGSSET TFGINMDPLC KPEDVSYAFM PNMSFFEFIT  360
MDGDKRDVVD LQDVKLGCTY EPVVTNFSGL YRMRVGDILM VTGFYNKAPL FKFVRRENVV  420
LSIDGDKTNE EDLFKAVSQV KLVLESSDLM LVDFTSYADT STFPGHYVIY MEVKDKEGDN  480
KKKKYVELNE EVFSKCCSVM EDSLDNVYKR CRFKDGSVGP LEIRVVRQGM FDSLMDFFIS  540
QGASIGQYKT PRCIKSGKAV EFMDECVVAR YGKGLVPPET SAAENPSWNE SDVTAMISSL  600
SRAIEYPTAD GHDPVKQELD RSDQLQQDQD QPRKRHYRGV RQRPWGKWAA EIRDPKKAAR  660
VWLGTFETAE DAALAYDRAA LKFKGTKAKL NFPERVQGPS TTSYVASQSG TDHSPRGGSE  720
SMNSPPPQLG PSTTSSWPTN YNQDILQYAQ LLTSNNDDAL SYYTSSLFSQ QQQPFSTPSS  780
SSSSLASQQT QQQQ
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
4epm_A0.0157175784-substituted benzoates-glutamate ligase GH3.12
4eq4_A0.0157175784-substituted benzoates-glutamate ligase GH3.12
4eq4_B0.0157175784-substituted benzoates-glutamate ligase GH3.12
4eql_A0.0157175784-substituted benzoates-glutamate ligase GH3.12
4eql_B0.0157175784-substituted benzoates-glutamate ligase GH3.12
4ewv_A0.0157175784-substituted benzoates-glutamate ligase GH3.12
4ewv_B0.0157175784-substituted benzoates-glutamate ligase GH3.12
4l39_A0.0157175784-substituted benzoates-glutamate ligase GH3.12
4l39_B0.0157175784-substituted benzoates-glutamate ligase GH3.12
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtCatalyzes the conjugation of specific amino acids (e.g. Glu and possibly His, Lys, and Met) to their preferred acyl substrates (e.g. 4-substituted benzoates), in a magnesium ion- and ATP-dependent manner. Can use 4-substituted benzoates such as 4-aminobenzoate (pABA), 4-fluorobenzoate and 4-hydroxybenzoate (4-HBA), and, to a lesser extent, benzoate, vanillate and trans-cinnamate, but not 2-substituted benzoates and salicylic acid (SA), as conjugating acyl substrates. Involved in both basal and induced resistance in a SA-dependent manner. Confers resistance to virulent and avirulent pathogens (at least bacteria and oomycetes), and promotes SA glucosides accumulation. Required for the establishment of hyper-sensitive response (HR) upon incompatible interaction and subsequent systemic acquired resistance (SAR). {ECO:0000269|PubMed:10224270, ECO:0000269|PubMed:11846877, ECO:0000269|PubMed:16353557, ECO:0000269|PubMed:17468220, ECO:0000269|PubMed:17521413, ECO:0000269|PubMed:17918621, ECO:0000269|PubMed:18266921, ECO:0000269|PubMed:19189963}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By P.syringae pv. maculicola and pv. tomato. Induced by PAD4 locally at the infection site and in a salicylic acid-dependent manner systemically. {ECO:0000269|PubMed:17468220, ECO:0000269|PubMed:17521413, ECO:0000269|PubMed:17918621, ECO:0000269|PubMed:18266921}.
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_018464053.10.0PREDICTED: 4-substituted benzoates-glutamate ligase GH3.12
SwissprotQ9LYU40.0GH312_ARATH; 4-substituted benzoates-glutamate ligase GH3.12
TrEMBLA0A0D3B0X80.0A0A0D3B0X8_BRAOL; Uncharacterized protein
TrEMBLA0A3P6A9G50.0A0A3P6A9G5_BRAOL; Uncharacterized protein
STRINGBo3g009110.10.0(Brassica oleracea)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM554322
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G13330.19e-56related to AP2 6l
Publications ? help Back to Top
  1. Warren RF,Merritt PM,Holub E,Innes RW
    Identification of three putative signal transduction genes involved in R gene-specified disease resistance in Arabidopsis.
    Genetics, 1999. 152(1): p. 401-12
    [PMID:10224270]
  2. van der Biezen EA,Freddie CT,Kahn K,Parker JE,Jones JD
    Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR genes and confers downy mildew resistance through multiple signalling components.
    Plant J., 2002. 29(4): p. 439-51
    [PMID:11846877]
  3. Xiao S, et al.
    The atypical resistance gene, RPW8, recruits components of basal defence for powdery mildew resistance in Arabidopsis.
    Plant J., 2005. 42(1): p. 95-110
    [PMID:15773856]
  4. McDowell JM,Williams SG,Funderburg NT,Eulgem T,Dangl JL
    Genetic analysis of developmentally regulated resistance to downy mildew (Hyaloperonospora parasitica) in Arabidopsis thaliana.
    Mol. Plant Microbe Interact., 2005. 18(11): p. 1226-34
    [PMID:16353557]
  5. Nobuta K, et al.
    The GH3 acyl adenylase family member PBS3 regulates salicylic acid-dependent defense responses in Arabidopsis.
    Plant Physiol., 2007. 144(2): p. 1144-56
    [PMID:17468220]
  6. Jagadeeswaran G, et al.
    Arabidopsis GH3-LIKE DEFENSE GENE 1 is required for accumulation of salicylic acid, activation of defense responses and resistance to Pseudomonas syringae.
    Plant J., 2007. 51(2): p. 234-46
    [PMID:17521413]
  7. Lee MW,Lu H,Jung HW,Greenberg JT
    A key role for the Arabidopsis WIN3 protein in disease resistance triggered by Pseudomonas syringae that secrete AvrRpt2.
    Mol. Plant Microbe Interact., 2007. 20(10): p. 1192-200
    [PMID:17918621]
  8. Wang L, et al.
    The genetic network controlling the Arabidopsis transcriptional response to Pseudomonas syringae pv. maculicola: roles of major regulators and the phytotoxin coronatine.
    Mol. Plant Microbe Interact., 2008. 21(11): p. 1408-20
    [PMID:18842091]
  9. Okrent RA,Brooks MD,Wildermuth MC
    Arabidopsis GH3.12 (PBS3) conjugates amino acids to 4-substituted benzoates and is inhibited by salicylate.
    J. Biol. Chem., 2009. 284(15): p. 9742-54
    [PMID:19189963]
  10. Chen Z,Zheng Z,Huang J,Lai Z,Fan B
    Biosynthesis of salicylic acid in plants.
    Plant Signal Behav, 2009. 4(6): p. 493-6
    [PMID:19816125]
  11. Okrent RA,Wildermuth MC
    Evolutionary history of the GH3 family of acyl adenylases in rosids.
    Plant Mol. Biol., 2011. 76(6): p. 489-505
    [PMID:21594748]
  12. Westfall CS, et al.
    Structural basis for prereceptor modulation of plant hormones by GH3 proteins.
    Science, 2012. 336(6089): p. 1708-11
    [PMID:22628555]
  13. Round A, et al.
    Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography.
    Acta Crystallogr. D Biol. Crystallogr., 2013. 69(Pt 10): p. 2072-80
    [PMID:24100325]
  14. Mackelprang R,Okrent RA,Wildermuth MC
    Preference of Arabidopsis thaliana GH3.5 acyl amido synthetase for growth versus defense hormone acyl substrates is dictated by concentration of amino acid substrate aspartate.
    Phytochemistry, 2017. 143: p. 19-28
    [PMID:28743075]