PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Rsa1.0_00356.1_g00010.1
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: 519aa    MW: 58629.8 Da    PI: 6.7944
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Rsa1.0_00356.1_g00010.1genomeRGDView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP257.82.7e-18359409256
                      AP2   2 gykGVrwdkkrgrWvAeIrdpsengkr..krfslgkfgtaeeAakaaiaarkklege 56 
                              +y+GVr ++ +g+Wv+eIr+p     r  +r++lg+++ +e+Aa+a++aa  +++ge
  Rsa1.0_00356.1_g00010.1 359 CYRGVRKRS-WGKWVSEIRVP-----RtaRRIWLGSYDAPEKAARAYDAALFCIRGE 409
                              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_0001335.60531258IPR000544Octanoyltransferase
Gene3DG3DSA:3.90.1550.101.7E-7239255No hitNo description
SuperFamilySSF556816.79E-5942230No hitNo description
TIGRFAMsTIGR002142.5E-5871255IPR000544Octanoyltransferase
PROSITE profilePS5173361.00774259IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PfamPF030991.5E-8108205IPR004143Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
PROSITE patternPS013130116131IPR020605Octanoyltransferase, conserved site
ProDomPD0060861.0E-20120168No hitNo description
PfamPF008475.8E-11359409IPR001471AP2/ERF domain
PROSITE profilePS5103221.997359416IPR001471AP2/ERF domain
SuperFamilySSF541712.75E-19359418IPR016177DNA-binding domain
Gene3DG3DSA:3.30.730.103.0E-27359418IPR001471AP2/ERF domain
SMARTSM003806.5E-34359422IPR001471AP2/ERF domain
PRINTSPR003671.2E-8360371IPR001471AP2/ERF domain
CDDcd000181.34E-29360418No hitNo description
PRINTSPR003671.2E-8382398IPR001471AP2/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: 519 aa     Download sequence    Send to blast
MESLHRVETL LPGLHHHPRT KANRNRVFRS VKVFSNPRKC QCFDLHDKLV PYKKAWTWQK  60
RIVEEKKTLI DTNQDCPDTV ILLQHSPVYT MGTGSSEEYL NFDVKDAPFD VYRTERGGEV  120
TYHGPGQLVM YPIINLRNHE MDLHWYLRTL EEVVIRVLSS AFSIKASRLD GLTGVWVGDQ  180
KVAAIGIRVS KWITYHGLAL NVTTDLTPFN SIVPCGIRDR QVGSIKGLLE DGKVGDLRLI  240
DIAHESLLKE FSEVFKLQIE KETVSDPNIL LGSSDHMNTR SSSGSRTSFH LRYLFNARSQ  300
DLDQMSEIAV VLTRVSTSGK KRTSDFCNIP PVGGIYMMPP STPKSPLLEE AHEDGRFKCY  360
RGVRKRSWGK WVSEIRVPRT ARRIWLGSYD APEKAARAYD AALFCIRGEK GVFNFPTSEK  420
PQLPEGSVRP LSKNDIQTIA TNYASSVVSV PSPETDQVPS QVPSQVPASP DVSVATEIME  480
MADEHYLPVD ESAESIFSVE DLQLDSFFMM DIDWINDLV
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2qhs_A1e-414925830228Lipoyltransferase
2qht_A9e-424925810208Lipoyltransferase
2qhu_A9e-424925810208Lipoyltransferase
2qhv_A9e-424925810208Lipoyltransferase
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}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapRsa1.0_00356.1_g00010.1
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.
GenBankBT0249100.0BT024910.1 Arabidopsis thaliana At4g31050 mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_018466373.10.0PREDICTED: plastidial lipoyltransferase 2-like
RefseqXP_018468528.10.0PREDICTED: plastidial lipoyltransferase 2-like
SwissprotQ948J91e-168LIP2P_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
AT4G31060.14e-93ERF 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]