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 462865514
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; PACMAD clade; Chloridoideae; Eragrostideae; Eragrostidinae; Eragrostis
Family FAR1
Protein Properties Length: 372aa    MW: 40057.4 Da    PI: 6.7863
Description FAR1 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
462865514genomeTefView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1FAR135.24.1e-1134824090
       FAR1 40 kreeekkktekerrtraetrtgCkaklkvkkekdgkwevtkleleHnHela 90
                r++e+  ++ e+ tr+etr++C a++k++++ dg +++++++ +HnH la
  462865514 34 DRRTESP-DHVESFTRPETRCQCPARMKISLR-DGFYYIYEFVADHNHILA 82
               3333333.467888******************.***************997 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PfamPF031011.7E-73682IPR004330FAR1 DNA binding domain
SuperFamilySSF516952.88E-30196362IPR017946PLC-like phosphodiesterase, TIM beta/alpha-barrel domain
Gene3DG3DSA:3.20.20.1901.0E-22197363IPR017946PLC-like phosphodiesterase, TIM beta/alpha-barrel domain
PROSITE profilePS5170427.915198372IPR030395Glycerophosphodiester phosphodiesterase domain
PfamPF030092.5E-16203361IPR030395Glycerophosphodiester phosphodiesterase domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006629Biological Processlipid metabolic process
GO:0008081Molecular Functionphosphoric diester hydrolase activity
Sequence ? help Back to Top
Protein Sequence    Length: 372 aa     Download sequence    Send to blast
MAPPIVPTPS IAAAVNSSSN SSVMSDLPGV REKDRRTESP DHVESFTRPE TRCQCPARMK  60
ISLRDGFYYI YEFVADHNHI LATAEEAHHL RSQRKITEAQ LASIEDAKAV GISNKAAFEQ  120
MAKEAGGMEN LGFTRVDMKN KLYSKSYDPS AEYLQFIENL DFSVDGFLTD FPPTASGAVA  180
CLAHSKGNPL PPPERPRPLI ISHNGASGVF PGSTDLAYQQ AMKDGADIID CTVQMSKDGI  240
AFCMPSADLG SCTTAGSAFI SKGSTVHQIQ NKSGIFSFDL SWSEIQTLKP DLVGPFAQSG  300
LKRNPAAKNA GKFMTLPGFL DMAKASNVSG ILIDIEHAAY LATRGLGVVD AVTGALTKAG  360
YDKETKQRKP MQ
Cis-element ? help Back to Top
SourceLink
PlantRegMap462865514
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_022683599.11e-128glycerophosphodiester phosphodiesterase GDPDL7
SwissprotQ9LVN08e-88GPDL7_ARATH; Glycerophosphodiester phosphodiesterase GDPDL7
TrEMBLA0A1D6H2W41e-125A0A1D6H2W4_MAIZE; Glycerophosphodiester phosphodiesterase GDPDL3
TrEMBLA0A2S3GLX71e-124A0A2S3GLX7_9POAL; Uncharacterized protein
TrEMBLA0A2T7F2W51e-124A0A2T7F2W5_9POAL; Uncharacterized protein
STRINGPavir.Aa03117.1.p1e-127(Panicum virgatum)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT4G38180.14e-13FAR1-related sequence 5
Publications ? help Back to Top
  1. Lalanne E, et al.
    SETH1 and SETH2, two components of the glycosylphosphatidylinositol anchor biosynthetic pathway, are required for pollen germination and tube growth in Arabidopsis.
    Plant Cell, 2004. 16(1): p. 229-40
    [PMID:14671020]
  2. Hayashi S, et al.
    The glycerophosphoryl diester phosphodiesterase-like proteins SHV3 and its homologs play important roles in cell wall organization.
    Plant Cell Physiol., 2008. 49(10): p. 1522-35
    [PMID:18718934]
  3. Cheng Y, et al.
    Characterization of the Arabidopsis glycerophosphodiester phosphodiesterase (GDPD) family reveals a role of the plastid-localized AtGDPD1 in maintaining cellular phosphate homeostasis under phosphate starvation.
    Plant J., 2011. 66(5): p. 781-95
    [PMID:21323773]
  4. Ge W, et al.
    Proteomic analyses of apoplastic proteins from germinating Arabidopsis thaliana pollen.
    Biochim. Biophys. Acta, 2011. 1814(12): p. 1964-73
    [PMID:21798377]