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 DCAR_026406
Organism
Daucus carota
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; campanulids; Apiales; Apiineae; Apiaceae; Apioideae; Scandiceae; Daucinae; Daucus
Family MYB_related
Protein Properties Length: 778aa    MW: 84072.3 Da    PI: 8.7755
Description MYB_related family protein
Gene Model
Gene Model ID Type Source Coding Sequence
DCAR_026406genomeARS-USDAView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding408.9e-13556147
                     TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHT.....TTS-HHHHHHHHHHH CS
  Myb_DNA-binding  1 rgrWTteEdellvdavkqlGggtWktIartmg.....kgRtlkqcksrwqky 47
                     +++WT++E+e l+ +vk++G+g WktI          ++R+  ++k++w+++
      DCAR_026406  5 KQKWTADEEEALKAGVKKHGMGKWKTILVDPDfapslTHRSNIDLKDKWRNL 56
                     79****************************99999***************97 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5129414.026161IPR017930Myb domain
SuperFamilySSF466891.05E-14256IPR009057Homeodomain-like
Gene3DG3DSA:1.10.10.602.4E-12456IPR009057Homeodomain-like
SMARTSM007177.4E-8459IPR001005SANT/Myb domain
PfamPF002492.2E-7556IPR001005SANT/Myb domain
CDDcd116601.63E-19656No hitNo description
PROSITE profilePS5096819.898342424IPR000089Biotin/lipoyl attachment
SuperFamilySSF512305.1E-21361439IPR011053Single hybrid motif
PfamPF003641.3E-15361422IPR000089Biotin/lipoyl attachment
Gene3DG3DSA:2.40.50.1001.7E-29361442No hitNo description
TIGRFAMsTIGR013497.6E-160361777IPR006257Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
CDDcd068496.18E-22363422No hitNo description
PROSITE patternPS001890373402IPR0030162-oxo acid dehydrogenase, lipoyl-binding site
SuperFamilySSF470059.02E-12480524IPR004167E3-binding domain
Gene3DG3DSA:4.10.320.101.3E-19481530IPR004167E3-binding domain
PfamPF028173.7E-15485520IPR004167E3-binding domain
SuperFamilySSF527771.51E-78546777No hitNo description
PfamPF001989.4E-79546777IPR0010782-oxoacid dehydrogenase acyltransferase, catalytic domain
Gene3DG3DSA:3.30.559.101.1E-85546777IPR023213Chloramphenicol acetyltransferase-like domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006090Biological Processpyruvate metabolic process
GO:0005739Cellular Componentmitochondrion
GO:0009941Cellular Componentchloroplast envelope
GO:0045254Cellular Componentpyruvate dehydrogenase complex
GO:0003677Molecular FunctionDNA binding
GO:0004742Molecular Functiondihydrolipoyllysine-residue acetyltransferase activity
GO:0005507Molecular Functioncopper ion binding
Sequence ? help Back to Top
Protein Sequence    Length: 778 aa     Download sequence    Send to blast
MGNHKQKWTA DEEEALKAGV KKHGMGKWKT ILVDPDFAPS LTHRSNIDLK DKWRNLGISG  60
TAAGQASKEK SPVLAITNGS AALPAAQNTN AATQTASTAL VLVDANANGV PDDAKTPANA  120
VMIPTKRFHR SGVDALSQQK HEVPQNFRRA LSSNVRRLTA QKKLEKVEHR FKIKNTGSRI  180
PTPRQRGDAK AGTSKKPGLL DPNTLEGANS IASHRVADAD NKSFAAAEAV KESEDIKELT  240
EESWLILELK SAPGLLRHDH ALLVRWLSSD AISFANGRDD IVKLRRIGNA SQEMDGVCSN  300
YTSTTNCLNY NHSSINPSMV TSVGSKQIKS TTSNMKLQSL LVGSVLSRAH WDNIGELSLL  360
AQGNIARWLK KEGDQVSTGE VLCEVETDKA TVEMECMEEG YLAKIVHGDG AKEIKVGEII  420
AITVEDEGDI AKFKDYKPSM SEPEASPKET PVSTPPKEDV VEKPTSSPEQ KSSKPSAEKQ  480
TGSRIFASPL AKKLAEENNV SLSSIKGTGP DGNIVKADIE DYLASRGKEA SPKASKSEKP  540
AVSSTDYTDI PLSQIRKVTA SRLLLSKQTI PHYYLTVDTC VDKLMDLRAK LNALQEASGG  600
KRISVNDLVI KAAALALRKV PQCNSSWTNE YIRQYHNVNI NVAVQTDNGL FVPVIRDADK  660
KGLSKIGDEV KHLAQKAKEN NLKPEDYEGG TFTVSNLGGP FGVKQFCAII NPPQAGILAV  720
GSAEKRVIPG AGTDQYAFAS FMAVTLSCDH RVIDGAIGAE WLKAFKGYIE NPETMLL*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ct0_01e-119360777103647Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
6h55_A1e-119360777103647Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtThe pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). {ECO:0000269|PubMed:14764908}.
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_017219712.10.0PREDICTED: dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial-like
SwissprotQ8RWN90.0ODP22_ARATH; Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial
TrEMBLA0A164UT870.0A0A164UT87_DAUCS; Acetyltransferase component of pyruvate dehydrogenase complex
STRINGVIT_09s0002g01800.t010.0(Vitis vinifera)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G72740.24e-36MYB_related family protein
Publications ? help Back to Top
  1. Taylor NL,Heazlewood JL,Day DA,Millar AH
    Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis.
    Plant Physiol., 2004. 134(2): p. 838-48
    [PMID:14764908]
  2. Wienkoop S, et al.
    Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins.
    Rapid Commun. Mass Spectrom., 2004. 18(6): p. 643-50
    [PMID:15052571]
  3. Brugière S, et al.
    The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions.
    Phytochemistry, 2004. 65(12): p. 1693-707
    [PMID:15276431]
  4. Finkemeier I, et al.
    The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress.
    J. Biol. Chem., 2005. 280(13): p. 12168-80
    [PMID:15632145]
  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. 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]
  7. Carrie C,Venne AS,Zahedi RP,Soll J
    Identification of cleavage sites and substrate proteins for two mitochondrial intermediate peptidases in Arabidopsis thaliana.
    J. Exp. Bot., 2015. 66(9): p. 2691-708
    [PMID:25732537]
  8. Song L,Liu D
    Mutations in the three Arabidopsis genes that encode the E2 subunit of the mitochondrial pyruvate dehydrogenase complex differentially affect enzymatic activity and plant growth.
    Plant Cell Rep., 2015. 34(11): p. 1919-26
    [PMID:26194327]