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 RrC1538_p3
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus
Family ERF
Protein Properties Length: 496aa    MW: 56050.8 Da    PI: 6.923
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
RrC1538_p3genomeMSUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP258.61.5e-18337387256
         AP2   2 gykGVrwdkkrgrWvAeIrdpsengkr.krfslgkfgtaeeAakaaiaarkklege 56 
                 +y+GVr ++ +g+Wv+eIr+p+    + +r++lg+++ +e+Aa+a++aa  +++ge
  RrC1538_p3 337 CYRGVRKRS-WGKWVSEIRVPR----TgRRIWLGSYDAPEKAARAYDAALFCIRGE 387
                 8*****888.**********95....25*************************997 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
HamapMF_0001334.89531269IPR000544Octanoyltransferase
Gene3DG3DSA:3.90.1550.104.7E-7045240No hitNo description
SuperFamilySSF556811.91E-5747236No hitNo description
TIGRFAMsTIGR002141.1E-5476235IPR000544Octanoyltransferase
PROSITE profilePS5173358.18280270IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PfamPF030992.7E-8114211IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PROSITE patternPS013130122137IPR020605Octanoyltransferase, conserved site
ProDomPD0060866.0E-20126174No hitNo description
SMARTSM003806.9E-35337400IPR001471AP2/ERF domain
SuperFamilySSF541719.15E-20337395IPR016177DNA-binding domain
PROSITE profilePS5103222.089337394IPR001471AP2/ERF domain
Gene3DG3DSA:3.30.730.101.6E-27337395IPR001471AP2/ERF domain
PfamPF008472.7E-11337387IPR001471AP2/ERF domain
PRINTSPR003671.1E-8338349IPR001471AP2/ERF domain
CDDcd000182.16E-30338394No hitNo description
PRINTSPR003671.1E-8360376IPR001471AP2/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: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
MESLHRVETL LSGLHHHHPR TNSNRNRVPR SVEILNTANH VNPRKCQCFD LYDQLVPYKK  60
AWTWQKTLVE EKKTLIDRNQ DCPDTVILLQ HSPVYTMGTG SSEEYLNFDV KDAPFDVYRT  120
ERGGEVTYHG PGQLVMYPII NLRNHEMDLH WYLRRLEEVV IRVLSSAFSI RASRLDGLTG  180
VWVGNQKVAA IGIRASKWIT YHGLALNVTT DLAPFDSIVP CGIRERRVES VKGLLAVADG  240
EQGKVGDLRL IDVAHESLLK EFSEVFQLHI EKQTVSDPNV PGEASTLRYL LNGHMSWIKI  300
VSIKKVRSAS VVDMMPPSTP KSPLFSSSLE EDQRFKCYRG VRKRSWGKWV SEIRVPRTGR  360
RIWLGSYDAP EKAARAYDAA LFCIRGEKGV FNFPSDKKPQ LPEGSVRPLS KHDIQTIATE  420
YSLSAASVPS SPTTTTPVAT DQVPAFPDAS VSTEIIEMAN ERYLPVDTAA ESMYSVEDLE  480
LDSFLMMDID WINNLD
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2qhs_A4e-385527730236Lipoyltransferase
2qht_A3e-385526810207Lipoyltransferase
2qhu_A3e-385526810207Lipoyltransferase
2qhv_A3e-385526810207Lipoyltransferase
Search in ModeBase
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}.
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_018449533.10.0PREDICTED: plastidial lipoyltransferase 2-like isoform X1
SwissprotQ948J91e-172LIP2P_ARATH; Octanoyltransferase LIP2p, chloroplastic
TrEMBLA0A3P5Z2M80.0A0A3P5Z2M8_BRACM; 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
AT4G31060.12e-89ERF 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]