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 Brast02G382000.2.p
Organism
Brachypodium stacei
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; BOP clade; Pooideae; Brachypodieae; Brachypodium
Family NAC
Protein Properties Length: 747aa    MW: 81626.8 Da    PI: 6.5123
Description NAC family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Brast02G382000.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1NAM35.62.7e-112715418128
                 NAM  18 yLkkkvegkk...leleevikevdiykvePwdLpk.........kvkaeekewyfFskrdkkya.tgkrknra.....tksgyWkatgkdk 90 
                          L++k+ g k    +   +i+e++ y+++P dL +         + +++  +wyf ++++ +++  g+r++r      +++g W++  k+k
  Brast02G382000.2.p  27 LLRHKAVGGKpfpRSHRPFIHEANPYSSHPADLVRgrahapgtdRGDGRGGDWYFCFPSKYQETvAGRRAKRRsrtvgAQDGCWHSESKKK 117
                         5666655444443222235**************744566665432223444998755555444436777777535555669********** PP

                 NAM  91 evlskkgelvglkktLvfykgrapkgektdWvmheyrl 128
                         ++ + +  ++     +   ++ + k ++t W+m e +l
  Brast02G382000.2.p 118 PIQD-RAYVTPFSYKMKVLENAKFKHQRTGWCMAEIQL 154
                         ***9.677777788888888999999*********987 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5100512.91710168IPR003441NAC domain
SuperFamilySSF1019414.84E-1626168IPR003441NAC domain
PfamPF023651.2E-428153IPR003441NAC domain
PfamPF006961.2E-9230372IPR001048Aspartate/glutamate/uridylate kinase
SuperFamilySSF536337.72E-42230475IPR001048Aspartate/glutamate/uridylate kinase
Gene3DG3DSA:3.40.1160.103.6E-14230278IPR001048Aspartate/glutamate/uridylate kinase
PROSITE patternPS003240231239IPR018042Aspartate kinase, conserved site
Gene3DG3DSA:3.40.1160.103.6E-14318379IPR001048Aspartate/glutamate/uridylate kinase
PfamPF006961.0E-11384445IPR001048Aspartate/glutamate/uridylate kinase
Gene3DG3DSA:3.40.1160.108.4E-21384477IPR001048Aspartate/glutamate/uridylate kinase
SuperFamilySSF550212.67E-5482550No hitNo description
SuperFamilySSF550214.2E-7560636No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0008652Biological Processcellular amino acid biosynthetic process
GO:0003677Molecular FunctionDNA binding
GO:0004072Molecular Functionaspartate kinase activity
Sequence ? help Back to Top
Protein Sequence    Length: 747 aa     Download sequence    Send to blast
MSAPNSPTSE QLQTLTPDLR PSVFARLLRH KAVGGKPFPR SHRPFIHEAN PYSSHPADLV  60
RGRAHAPGTD RGDGRGGDWY FCFPSKYQET VAGRRAKRRS RTVGAQDGCW HSESKKKPIQ  120
DRAYVTPFSY KMKVLENAKF KHQRTGWCMA EIQLEENVEL VLCRVYRSPR PSSAARGERG  180
APAPPLIDQI SPCAGRISPA SGGSGAMSEL GKGWMIRCQS GAAAAAAADT VMKFGGSSIP  240
SAEGMKEAAS IVLSFPEGTP APVVVLSAMG KTTTNLLMAA DNALRWRTHK AWEIRELDAV  300
QELHLSTVDA LGLDRSIISG SLDELKQLLK HVALDHTLTP KTRDIILSHG ELMSTTIFSA  360
YLNKLGEGAQ QLQEWEWSAI SNVGSGGSDL AAISIARELR ARKIVVWKDV NGLFTCDPNV  420
FESALPLPYL NFNEATALGF FAAQSMELAL EIGIPVIVKS LYNPQAPGTM LTKTREMNES  480
ELTRIMLTSN LTMLDIKSTG AVDRSRFVTK AFSIFTKFGI SVDHAVISQC EVLIILVPSK  540
LLSHESIQMK LDVVIEELQQ IAAVHALSHR SFISLIGTAE MSTTILEKAF GALTRINVKT  600
QMSSHGSSKV MNIFLVVNDN EATNCVEALH SEFVEKYLSE VHGADSEHNS SLVPVSSSVA  660
ASSGDKRKPD DEHRTQCLDT ETDDYHMDMR VLSGNFDNTL TFIAEEDFTN DVEAVVVEHW  720
SLFAGEEEGV YVAPHTYQFL EGVTAP*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2cdq_A1e-11923163530484ASPARTOKINASE
2cdq_B1e-11923163530484ASPARTOKINASE
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtInvolved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
Cis-element ? help Back to Top
SourceLink
PlantRegMapBrast02G382000.2.p
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_003562409.11e-142aspartokinase 1, chloroplastic
SwissprotQ9LYU81e-118AK1_ARATH; Aspartokinase 1, chloroplastic
TrEMBLA0A3B6SLB91e-156A0A3B6SLB9_WHEAT; Uncharacterized protein
Publications ? help Back to Top
  1. Yoshioka Y,Kurei S,Machida Y
    Identification of a monofunctional aspartate kinase gene of Arabidopsis thaliana with spatially and temporally regulated expression.
    Genes Genet. Syst., 2001. 76(3): p. 189-98
    [PMID:11569502]
  2. Mas-Droux C, et al.
    A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase.
    Plant Cell, 2006. 18(7): p. 1681-92
    [PMID:16731588]
  3. Curien G,Laurencin M,Robert-Genthon M,Dumas R
    Allosteric monofunctional aspartate kinases from Arabidopsis.
    FEBS J., 2007. 274(1): p. 164-76
    [PMID:17140415]
  4. Jander G,Joshi V
    Aspartate-Derived Amino Acid Biosynthesis in Arabidopsis thaliana.
    Arabidopsis Book, 2009. 7: p. e0121
    [PMID:22303247]
  5. Van Bochaute P,Novoa A,Ballet S,Rognes SE,Angenon G
    Regulatory mechanisms after short- and long-term perturbed lysine biosynthesis in the aspartate pathway: the need for isogenes in Arabidopsis thaliana.
    Physiol Plant, 2013. 149(4): p. 449-60
    [PMID:23556418]
  6. Clark TJ,Lu Y
    Analysis of Loss-of-Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate-Derived Amino Acid Contents.
    Plant Physiol., 2015. 168(4): p. 1512-26
    [PMID:26063505]
  7. Khare D, et al.
    Root avoidance of toxic metals requires the GeBP-LIKE 4 transcription factor in Arabidopsis thaliana.
    New Phytol., 2017. 213(3): p. 1257-1273
    [PMID:27768815]
  8. Rognes SE,Lea PJ,Miflin BJ
    S-adenosylmethionine--a novel regulator of aspartate kinase.
    Nature, 1980. 287(5780): p. 357-9
    [PMID:6252474]
  9. Ghislain M,Frankard V,Vandenbossche D,Matthews BF,Jacobs M
    Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana.
    Plant Mol. Biol., 1994. 24(6): p. 835-51
    [PMID:8204822]
  10. Ben-Tzvi Tzchori I,Perl A,Galili G
    Lysine and threonine metabolism are subject to complex patterns of regulation in Arabidopsis.
    Plant Mol. Biol., 1996. 32(4): p. 727-34
    [PMID:8980524]
  11. Frankard V,Vauterin M,Jacobs M
    Molecular characterization of an Arabidopsis thaliana cDNA coding for a monofunctional aspartate kinase.
    Plant Mol. Biol., 1997. 34(2): p. 233-42
    [PMID:9207839]
  12. Tang G,Zhu-Shimoni JX,Amir R,Zchori IB,Galili G
    Cloning and expression of an Arabidopsis thaliana cDNA encoding a monofunctional aspartate kinase homologous to the lysine-sensitive enzyme of Escherichia coli.
    Plant Mol. Biol., 1997. 34(2): p. 287-93
    [PMID:9207844]
  13. Zhu-Shimoni JX,Galili G
    Expression of an arabidopsis aspartate Kinase/Homoserine dehydrogenase gene is metabolically regulated by photosynthesis-related signals but not by nitrogenous compounds
    Plant Physiol., 1998. 116(3): p. 1023-8
    [PMID:9501134]