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 GSBRNA2T00130406001
Common NameGSBRNA2T00130406001
Organism
Brassica napus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica
Family ERF
Protein Properties Length: 496aa    MW: 56407.4 Da    PI: 6.2948
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
GSBRNA2T00130406001genomeGenoscopeView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP260.34.6e-19338388256
                  AP2   2 gykGVrwdkkrgrWvAeIrdpsengkr..krfslgkfgtaeeAakaaiaarkklege 56 
                          +y+GVr ++ +g+Wv+eIr+p     r  +r++lg+++ +e+Aa+a++aa  +++ge
  GSBRNA2T00130406001 338 CYRGVRKRS-WGKWVSEIRVP-----RtaRRIWLGSYDDPEKAARAYDAALFCIRGE 388
                          8*****888.**********9.....447*************************997 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
HamapMF_0001335.27633260IPR000544Octanoyltransferase
Gene3DG3DSA:3.90.1550.105.1E-7241257No hitNo description
SuperFamilySSF556812.07E-5844232No hitNo description
TIGRFAMsTIGR002144.5E-5774257IPR000544Octanoyltransferase
PROSITE profilePS5173360.67576261IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PfamPF030999.4E-9111207IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PROSITE patternPS013130118133IPR020605Octanoyltransferase, conserved site
ProDomPD0060862.0E-20122170No hitNo description
SuperFamilySSF541711.44E-19338396IPR016177DNA-binding domain
PROSITE profilePS5103221.957338395IPR001471AP2/ERF domain
PfamPF008478.0E-11338388IPR001471AP2/ERF domain
SMARTSM003801.7E-33338401IPR001471AP2/ERF domain
Gene3DG3DSA:3.30.730.102.2E-27338397IPR001471AP2/ERF domain
PRINTSPR003671.5E-8339350IPR001471AP2/ERF domain
CDDcd000184.91E-29339397No hitNo description
PRINTSPR003671.5E-8361377IPR001471AP2/ERF domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0006464Biological Processcellular protein modification process
GO:0009107Biological Processlipoate biosynthetic process
GO:0005634Cellular Componentnucleus
GO:0005737Cellular Componentcytoplasm
GO:0003677Molecular FunctionDNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0016415Molecular Functionoctanoyltransferase activity
Sequence ? help Back to Top
Protein Sequence    Length: 496 aa     Download sequence    Send to blast
MESLHLVETL LPGLHHHHPR TNANRNKVFR SVKVFFSNPR KCQCFDLHDK MVPYKKAWTW  60
QKRIVEEKKA LIDGNQDCPD TVILLQHSPV YTMGTGSSED YLNFDVKDAP FDVYRTERGG  120
EVTYHGPGQL VMYPIINLRN HEMDLHWYLR TLEEVVIRVL SSAFSIKASR LDGLTGVWVG  180
NQKVAAIGIR VSKWITYHGL ALNVTTDLTP FNSIVPCGIR DRQVGSIKCL LEDGEHGDLR  240
LIDIAHESLL KEFSEVFQLH IEKQTVSDLD ILKAEPFRRL DLQFADGDQC VMYDDQLKYN  300
IKLYSVSRTI FHLRDMMPPS TPKSPLLEEA HEDGRFKCYR GVRKRSWGKW VSEIRVPRTA  360
RRIWLGSYDD PEKAARAYDA ALFCIRGEKG VFNFPSSKKP ELPEGSVRPL SKLDIQTIAT  420
NHASSVVSVP SPATPIPETD QVSASPDASV STEIMEMADE HYLPVDASVE SIFSVEDLHL  480
DNFLMMDIDW IDDLV*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2qhs_A1e-415126830236Lipoyltransferase
2qht_A8e-425126010208Lipoyltransferase
2qhu_A8e-425126010208Lipoyltransferase
2qhv_A8e-425126010208Lipoyltransferase
Search in ModeBase
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Expressed in roots, leaves and flowers (PubMed:11602263, PubMed:23581459). Expressed in cauline leaves, stems and siliques (PubMed:23581459). {ECO:0000269|PubMed:11602263, ECO:0000269|PubMed:23581459}.
Functional Description ? help Back to Top
Source Description
UniProtCatalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity) (PubMed:11602263). Together with LIP1P is essential for de novo plastidial protein lipoylation during seed development. Acts redundantly with LIP2P2 (PubMed:23581459). {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:11602263, ECO:0000269|PubMed:23581459}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapGSBRNA2T00130406001
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAB0723900.0AB072390.1 Arabidopsis thaliana LIP2p mRNA for lipoyltransferase, complete cds.
GenBankAK2214890.0AK221489.1 Arabidopsis thaliana mRNA for putative protein, complete cds, clone: RAFL07-48-I03.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_013671053.10.0plastidial lipoyltransferase 2-like
RefseqXP_013730773.10.0plastidial lipoyltransferase 2-like
SwissprotQ948J91e-167LIP2P_ARATH; Octanoyltransferase LIP2p, chloroplastic
TrEMBLA0A3P6FH450.0A0A3P6FH45_BRAOL; Uncharacterized protein
STRINGBra011244.1-P0.0(Brassica rapa)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM719135
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT4G31060.17e-94ERF family protein
Publications ? help Back to Top
  1. Wada M,Yasuno R,Wada H
    Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids.
    FEBS Lett., 2001. 506(3): p. 286-90
    [PMID:11602263]
  2. Ewald R,Hoffmann C,Neuhaus E,Bauwe H
    Two redundant octanoyltransferases and one obligatory lipoyl synthase provide protein-lipoylation autonomy to plastids of Arabidopsis.
    Plant Biol (Stuttg), 2014. 16(1): p. 35-42
    [PMID:23581459]
  3. Ewald R, et al.
    Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis.
    Plant Physiol., 2014. 165(3): p. 978-990
    [PMID:24872381]
  4. Chalhoub B, et al.
    Plant genetics. Early allopolyploid evolution in the post-Neolithic Brassica napus oilseed genome.
    Science, 2014. 345(6199): p. 950-3
    [PMID:25146293]