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 BGIOSGA002288-PA
Common NameOsI_00597
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; BOP clade; Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa
Family bZIP
Protein Properties Length: 384aa    MW: 41044.5 Da    PI: 10.2787
Description bZIP family protein
Gene Model
Gene Model ID Type Source Coding Sequence
BGIOSGA002288-PAgenomeRISView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1bZIP_137.16.9e-12290350262
                       XXXCHHHCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH CS
            bZIP_1   2 kelkrerrkqkNReAArrsRqRKkaeieeLeekvkeLeaeNkaLkkeleelkkevaklkse 62 
                       ke  r +r+ +NR++A+  R+RKka++ eLe k+k Le  N +L +++++l++e  +l++ 
  BGIOSGA002288-PA 290 KEQNRLKRLLRNRVSAQQARERKKAYMTELEAKAKDLELRNAELEQRVSTLQNENNTLRQI 350
                       78899***************************************************99986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS513849.95812130IPR017927Ferredoxin reductase-type FAD-binding domain
SuperFamilySSF633802.69E-1953132IPR017938Riboflavin synthase-like beta-barrel
PfamPF009701.8E-1655129IPR008333Oxidoreductase, FAD-binding domain
CDDcd061832.78E-8264218No hitNo description
PRINTSPR004062.1E-197986IPR001834NADH:cytochrome b5 reductase (CBR)
Gene3DG3DSA:2.40.30.101.1E-1681117No hitNo description
PRINTSPR004062.1E-19115129IPR001834NADH:cytochrome b5 reductase (CBR)
SuperFamilySSF523431.1E-28117219No hitNo description
Gene3DG3DSA:3.40.50.801.3E-39118224No hitNo description
PRINTSPR004062.1E-19138157IPR001834NADH:cytochrome b5 reductase (CBR)
PfamPF001752.0E-24139224IPR001433Oxidoreductase FAD/NAD(P)-binding
PRINTSPR004062.1E-19176187IPR001834NADH:cytochrome b5 reductase (CBR)
SMARTSM003381.6E-13289353IPR004827Basic-leucine zipper domain
PfamPF001701.7E-10290351IPR004827Basic-leucine zipper domain
PROSITE profilePS5021712.185291354IPR004827Basic-leucine zipper domain
SuperFamilySSF579591.88E-11294351No hitNo description
Gene3DG3DSA:1.20.5.1703.9E-16294353No hitNo description
CDDcd147046.17E-22294344No hitNo description
PROSITE patternPS000360296311IPR004827Basic-leucine zipper domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0055114Biological Processoxidation-reduction process
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0016491Molecular Functionoxidoreductase activity
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 384 aa     Download sequence    Send to blast
MAALLLRRLA GTHRGRVPLA AAAAVTGGAA LFCASSPPTI ALMEEKGEDA AAKVALNPDK  60
WLEFKLQEKA TVSHNSQLFR YTPISDPDSK GYFDLLIKVY PDGKMSQYFA SLKPGDVVEV  120
KGPIEKLRYS PNMKKQIGMI AGGTGITPML QVVRAILKNP DDNTQVSLIY ANVSPDDILL  180
KRELDRLASS YPNFKVFYTV DKPSNDWRGG VGYISKDMAL KGVESDEEIR RVPEMGGGGG  240
SASSGAGADE RQGKEDGKQQ GGGGGGAAAA GGGQEQAPPA RKRGRSAGDK EQNRLKRLLR  300
NRVSAQQARE RKKAYMTELE AKAKDLELRN AELEQRVSTL QNENNTLRQI LKNTTAHAGK  360
RGGGGGGKGG DGGGGGKKHH FTKS
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2eix_A7e-60552185200NADH-cytochrome b5 reductase
2eix_B7e-60552185200NADH-cytochrome b5 reductase
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1365373GGKGGDGGG
2367376KGGDGGGGGK
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Os.531990.0callus| flower| leaf| panicle| root| stem
Expression -- Microarray ? help Back to Top
Source ID E-value
GEO329813470.0
Functional Description ? help Back to Top
Source Description
UniProtDesaturation and elongation of fatty acids. {ECO:0000250}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankCT8418870.0CT841887.1 Oryza rufipogon (W1943) cDNA clone: ORW1943C105P06, full insert sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_015621896.11e-145NADH-cytochrome b5 reductase-like protein
SwissprotP832911e-100NB5R2_ARATH; NADH-cytochrome b5 reductase-like protein
TrEMBLA2WL860.0A2WL86_ORYSI; Uncharacterized protein
STRINGORUFI01G05070.11e-147(Oryza rufipogon)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G11260.11e-32bZIP family protein
Publications ? help Back to Top
  1. Kruft V,Eubel H,Jänsch L,Werhahn W,Braun HP
    Proteomic approach to identify novel mitochondrial proteins in Arabidopsis.
    Plant Physiol., 2001. 127(4): p. 1694-710
    [PMID:11743114]
  2. Peltier JB, et al.
    Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications.
    J. Biol. Chem., 2004. 279(6): p. 4768-81
    [PMID:14593120]
  3. Tamaoki M, et al.
    Transcriptome analysis of O3-exposed Arabidopsis reveals that multiple signal pathways act mutually antagonistically to induce gene expression.
    Plant Mol. Biol., 2003. 53(4): p. 443-56
    [PMID:15010611]
  4. Tasseva G,de Virville JD,Cantrel C,Moreau F,Zachowski A
    Changes in the endoplasmic reticulum lipid properties in response to low temperature in Brassica napus.
    Plant Physiol. Biochem., 2004. 42(10): p. 811-22
    [PMID:15596101]
  5. Noir S,Bräutigam A,Colby T,Schmidt J,Panstruga R
    A reference map of the Arabidopsis thaliana mature pollen proteome.
    Biochem. Biophys. Res. Commun., 2005. 337(4): p. 1257-66
    [PMID:16242667]
  6. Bayer EM, et al.
    Arabidopsis cell wall proteome defined using multidimensional protein identification technology.
    Proteomics, 2006. 6(1): p. 301-11
    [PMID:16287169]
  7. Kumar R,Wallis JG,Skidmore C,Browse J
    A mutation in Arabidopsis cytochrome b5 reductase identified by high-throughput screening differentially affects hydroxylation and desaturation.
    Plant J., 2006. 48(6): p. 920-32
    [PMID:17227547]
  8. Jiang Y,Yang B,Harris NS,Deyholos MK
    Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots.
    J. Exp. Bot., 2007. 58(13): p. 3591-607
    [PMID:17916636]
  9. Jamet E, et al.
    Recent advances in plant cell wall proteomics.
    Proteomics, 2008. 8(4): p. 893-908
    [PMID:18210371]
  10. Tan YF,O'Toole N,Taylor NL,Millar AH
    Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function.
    Plant Physiol., 2010. 152(2): p. 747-61
    [PMID:20018591]
  11. Duncan O, et al.
    Multiple lines of evidence localize signaling, morphology, and lipid biosynthesis machinery to the mitochondrial outer membrane of Arabidopsis.
    Plant Physiol., 2011. 157(3): p. 1093-113
    [PMID:21896887]
  12. Aryal UK,Krochko JE,Ross AR
    Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry.
    J. Proteome Res., 2012. 11(1): p. 425-37
    [PMID:22092075]