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 GSBRNA2T00039973001
Common NameGSBRNA2T00039973001
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: 455aa    MW: 51267.3 Da    PI: 5.6153
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
GSBRNA2T00039973001genomeGenoscopeView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP260.44e-19297347256
                  AP2   2 gykGVrwdkkrgrWvAeIrdpsengkr..krfslgkfgtaeeAakaaiaarkklege 56 
                          +y+GVr ++ +g+Wv+eIr+p     r  +r++lg+++ +e+Aa+a++aa  +++ge
  GSBRNA2T00039973001 297 CYRGVRKRS-WGKWVSEIRVP-----RtaRRIWLGSYDDPEKAARAYDAALFCIRGE 347
                          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_0001335.00931261IPR000544Octanoyltransferase
Gene3DG3DSA:3.90.1550.104.1E-7239237No hitNo description
SuperFamilySSF556811.49E-5842231No hitNo description
TIGRFAMsTIGR002141.2E-5670232IPR000544Octanoyltransferase
PROSITE profilePS5173359.8574262IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PfamPF030998.6E-9109205IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PROSITE patternPS013130116131IPR020605Octanoyltransferase, conserved site
ProDomPD0060865.0E-20120168No hitNo description
PfamPF008477.1E-11297347IPR001471AP2/ERF domain
Gene3DG3DSA:3.30.730.102.2E-27297356IPR001471AP2/ERF domain
PROSITE profilePS5103221.957297354IPR001471AP2/ERF domain
SMARTSM003801.1E-33297360IPR001471AP2/ERF domain
SuperFamilySSF541719.81E-20297356IPR016177DNA-binding domain
PRINTSPR003671.3E-8298309IPR001471AP2/ERF domain
CDDcd000181.52E-29298356No hitNo description
PRINTSPR003671.3E-8320336IPR001471AP2/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: 455 aa     Download sequence    Send to blast
MESLHRVETL LSGLHHCPRT SANRNRVFRS VKVFSNPRKC QCFDLHDKLV PYNKAWTWQK  60
RIVEEKKTLI DRNQDCPDTV ISLQHDPVYT MGTGSSEDYL NFDVKDAPFD VYRTERGGEV  120
TYHGPGQLVM YPIINLRNHE MDLHWYLRTL EEVVINVLSS AFSIKASRVD GLTGVWVGNQ  180
KVAAIGIRVS KWITYHGLAL NVTTDLTPFN SIVPCGIRDR QVGSIKGLLG DGEHGTVGDL  240
RLIDIAHESL LKEFSEVFQL QIEKETVADP YILDMMPPST PKSPLLEEAH EDGRFKCYRG  300
VRKRSWGKWV SEIRVPRTAR RIWLGSYDDP EKAARAYDAA LFCIRGEKGV FNFPTSEKPQ  360
LPEGSVRPLS KLDIQTIATN YASSVVSVPS TTIPIPATDQ VSASPDVAVS TEIMEMADEH  420
YLPVDASVES IFSVEDLQLD NFLMMDIDWI DDLV*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2qhs_A2e-394926130228Lipoyltransferase
2qht_A9e-404926110208Lipoyltransferase
2qhu_A9e-404926110208Lipoyltransferase
2qhv_A9e-404926110208Lipoyltransferase
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
PlantRegMapGSBRNA2T00039973001
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_009127279.10.0PREDICTED: plastidial lipoyltransferase 2
SwissprotQ948J91e-169LIP2P_ARATH; Octanoyltransferase LIP2p, chloroplastic
TrEMBLA0A078GNW40.0A0A078GNW4_BRANA; BnaA01g06090D 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
AT4G31060.12e-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]