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 TRIUR3_12546-P1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; BOP clade; Pooideae; Triticodae; Triticeae; Triticinae; Triticum
Family WRKY
Protein Properties Length: 308aa    MW: 34655.6 Da    PI: 9.2149
Description WRKY family protein
Gene Model
Gene Model ID Type Source Coding Sequence
TRIUR3_12546-P1genomeBGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1WRKY72.17.3e-23244296251
                      --SS-EEEEEEE--TT-SS-EEEEEE-ST...T---EEEEEE-SSSTTEEEEE CS
             WRKY   2 dDgynWrKYGqKevkgsefprsYYrCtsa...gCpvkkkversaedpkvveit 51 
                      dDg++WrKYGqK++ g++fpr+YYrCt++   gC ++++v+rs+ d  v+++t
  TRIUR3_12546-P1 244 DDGFSWRKYGQKDILGAKFPRGYYRCTYRnaqGCAATRQVQRSDADLAVFDVT 296
                      8***************************98889****************9998 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF568011.96E-647108No hitNo description
Gene3DG3DSA:3.40.50.9808.6E-451109No hitNo description
Gene3DG3DSA:2.20.25.807.6E-21241297IPR003657WRKY domain
SuperFamilySSF1182902.88E-19241296IPR003657WRKY domain
SMARTSM007749.3E-30243303IPR003657WRKY domain
PROSITE profilePS5081119.244244296IPR003657WRKY domain
PfamPF031062.1E-20244297IPR003657WRKY domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 308 aa     Download sequence    Send to blast
MADDCVRSRQ SSSEAMKFLV ESGGAEGNAG PSYRNVLAKD TGLLQSPPGV DCLWDLFRAS  60
VEKYPSNPML GHRPVVDGKV GDYAWMTYRE VCDVVIKLAA AMSNSGVKQI WVYGNSFESF  120
LIAVINPNQQ ALENWAGQNG ITGNLEELCE NAKIKEHFIA ELAKAAKEKK LKGFEFIRAV  180
HLDAVPFDME RDLITPTYKK KRPQMLKYYQ GAIDALYKSS KKGLPRWTKK FRIPDDANLE  240
YTPDDGFSWR KYGQKDILGA KFPRGYYRCT YRNAQGCAAT RQVQRSDADL AVFDVTLNLS  300
CKRKKESS
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5w3x_B1e-172452961869Disease resistance protein RRS1
5w3x_D1e-172452961869Disease resistance protein RRS1
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtActivation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankDQ9006878e-56DQ900687.1 Hordeum vulgare clone BAC 455J22, complete sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_003564297.15e-59long chain acyl-CoA synthetase 4
SwissprotQ9T0A06e-48LACS4_ARATH; Long chain acyl-CoA synthetase 4
TrEMBLM7ZZ020.0M7ZZ02_TRIUA; Long chain acyl-CoA synthetase 4
STRINGTRIUR3_12546-P10.0(Triticum urartu)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G24110.18e-34WRKY DNA-binding protein 30
Publications ? help Back to Top
  1. Shockey JM,Fulda MS,Browse JA
    Arabidopsis contains nine long-chain acyl-coenzyme a synthetase genes that participate in fatty acid and glycerolipid metabolism.
    Plant Physiol., 2002. 129(4): p. 1710-22
    [PMID:12177484]
  2. Fulda M,Shockey J,Werber M,Wolter FP,Heinz E
    Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation.
    Plant J., 2002. 32(1): p. 93-103
    [PMID:12366803]
  3. Shockey JM,Fulda MS,Browse J
    Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases.
    Plant Physiol., 2003. 132(2): p. 1065-76
    [PMID:12805634]
  4. Zhao L,Katavic V,Li F,Haughn GW,Kunst L
    Insertional mutant analysis reveals that long-chain acyl-CoA synthetase 1 (LACS1), but not LACS8, functionally overlaps with LACS9 in Arabidopsis seed oil biosynthesis.
    Plant J., 2010. 64(6): p. 1048-58
    [PMID:21143684]
  5. Jessen D, et al.
    Combined activity of LACS1 and LACS4 is required for proper pollen coat formation in Arabidopsis.
    Plant J., 2011. 68(4): p. 715-26
    [PMID:21790813]
  6. Jessen D,Roth C,Wiermer M,Fulda M
    Two activities of long-chain acyl-coenzyme A synthetase are involved in lipid trafficking between the endoplasmic reticulum and the plastid in Arabidopsis.
    Plant Physiol., 2015. 167(2): p. 351-66
    [PMID:25540329]
  7. Fulda M,Heinz E,Wolter FP
    Brassica napus cDNAs encoding fatty acyl-CoA synthetase.
    Plant Mol. Biol., 1997. 33(5): p. 911-22
    [PMID:9106514]