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 GSBRNA2T00108159001
Common NameGSBRNA2T00108159001
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 HSF
Protein Properties Length: 387aa    MW: 41514.9 Da    PI: 6.0899
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
GSBRNA2T00108159001genomeGenoscopeView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind384.5e-1212111285
                          HHHHHHHHHCTGGGTTTSEES.SSSSEEEES-HHHHHHHTHHHHST.T--HHHHHHHHHHTTEEE---SSBTTTT..............X CS
         HSF_DNA-bind   2 Flkklyeiledeelkelisws.engnsfvvldeeefakkvLpkyFk.hsnfaSFvRQLnmYgFkkvkdeekksks..............k 75 
                          F ++lye ++d++l+ +isw+ +++nsf+v+d  +f +++Lpk  +  +nf+ Fv  L   gF ++++ e+                  +
  GSBRNA2T00108159001  12 FFMELYENVNDHSLDAIISWTnNSNNSFIVWDVPRFCTRILPKSVEfGKNFSEFVSELRHHGFLRIDHLETLMGLgfltlvgvtekdstR 101
                          8999*****************7778*****************97762479**************99998865333555555555443322 PP

                          TTSEEEEESX CS
         HSF_DNA-bind  76 ekiweFkhks 85 
                          + + +F+++ 
  GSBRNA2T00108159001 102 DATSKFENPI 111
                          5566666665 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM004151.2E-58129IPR000232Heat shock factor (HSF)-type, DNA-binding
SuperFamilySSF467858.3E-12981IPR011991Winged helix-turn-helix DNA-binding domain
Gene3DG3DSA:1.10.10.109.7E-1310110IPR011991Winged helix-turn-helix DNA-binding domain
PfamPF004479.6E-1212116IPR000232Heat shock factor (HSF)-type, DNA-binding
SuperFamilySSF529495.12E-792227No hitNo description
Gene3DG3DSA:3.40.630.101.7E-51214385No hitNo description
SuperFamilySSF531875.34E-39226385No hitNo description
PfamPF008832.7E-38230385IPR000819Peptidase M17, leucyl aminopeptidase, C-terminal
PRINTSPR004818.3E-22310327IPR011356Peptidase M17, leucine aminopeptidase/peptidase B
PRINTSPR004818.3E-22334355IPR011356Peptidase M17, leucine aminopeptidase/peptidase B
PRINTSPR004818.3E-22372386IPR011356Peptidase M17, leucine aminopeptidase/peptidase B
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0006508Biological Processproteolysis
GO:0005634Cellular Componentnucleus
GO:0005737Cellular Componentcytoplasm
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0004177Molecular Functionaminopeptidase activity
GO:0008235Molecular Functionmetalloexopeptidase activity
GO:0030145Molecular Functionmanganese ion binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 387 aa     Download sequence    Send to blast
MAHRSATGSY SFFMELYENV NDHSLDAIIS WTNNSNNSFI VWDVPRFCTR ILPKSVEFGK  60
NFSEFVSELR HHGFLRIDHL ETLMGLGFLT LVGVTEKDST RDATSKFENP ILNKLDAHVS  120
GLLDLVSSEE DFAGKPGKSA SSPAAFQDLG EAVATIAKAS QSSSVAVALS SHDNESKLSS  180
VSALELDCRY KSESKKPSLS SVDIIGFGTG PELENKLKYA EDVSYGVIFG RELINSPANV  240
LTPAVISDEA SKVASTYSDV FSANILNEEQ CRELKMGSYL AVASASAKAN PPFFIHLVYR  300
PPSGSVRTKH VLIGKGLTFD SDGYNIKAGP GSSINLMKFD MGGSAAILCA AKAIGEIKHP  360
GVEAHFIVAV CENMISGTGM RHGDVK*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
4ksi_A1e-1018738544370Leucine aminopeptidase 1, chloroplastic
Search in ModeBase
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Bna.28901e-83leaf| microspore| root| seed
Functional Description ? help Back to Top
Source Description
UniProtPresumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (Probable). Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin (PubMed:22493451). Possesses Cys-Gly dipeptidase activity. In addition, can cleave Cys-Leu and Leu-Cys dipeptides (PubMed:25716890). {ECO:0000269|PubMed:22493451, ECO:0000269|PubMed:25716890, ECO:0000305|PubMed:1555602}.; FUNCTION: Functions as molecular chaperone to protect proteins from heat-induced damage. {ECO:0000269|PubMed:22493451}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapGSBRNA2T00108159001
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_013633876.10.0PREDICTED: leucine aminopeptidase 1-like
SwissprotP301841e-155AMPL1_ARATH; Leucine aminopeptidase 1
TrEMBLA0A078GC190.0A0A078GC19_BRANA; BnaA01g18590D protein
STRINGBo4g145450.10.0(Brassica oleracea)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G77570.18e-20Winged helix-turn-helix transcription repressor DNA-binding
Publications ? help Back to Top
  1. Sokolenko A, et al.
    The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts.
    Curr. Genet., 2002. 41(5): p. 291-310
    [PMID:12185496]
  2. Tamaoki M, et al.
    Transcriptome analysis of O3-exposed Arabidopsis reveals that multiple signal pathways act mutually antagonistically to induce gene expression.
    Plant Mol. Biol., 2003. 53(4): p. 443-56
    [PMID:15010611]
  3. Rajjou L, et al.
    The effect of alpha-amanitin on the Arabidopsis seed proteome highlights the distinct roles of stored and neosynthesized mRNAs during germination.
    Plant Physiol., 2004. 134(4): p. 1598-613
    [PMID:15047896]
  4. Shimaoka T, et al.
    Isolation of intact vacuoles and proteomic analysis of tonoplast from suspension-cultured cells of Arabidopsis thaliana.
    Plant Cell Physiol., 2004. 45(6): p. 672-83
    [PMID:15215502]
  5. Bartling D,Weiler EW
    Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants.
    Eur. J. Biochem., 1992. 205(1): p. 425-31
    [PMID:1555602]
  6. Job C,Rajjou L,Lovigny Y,Belghazi M,Job D
    Patterns of protein oxidation in Arabidopsis seeds and during germination.
    Plant Physiol., 2005. 138(2): p. 790-802
    [PMID:15908592]
  7. Dixon DP,Skipsey M,Grundy NM,Edwards R
    Stress-induced protein S-glutathionylation in Arabidopsis.
    Plant Physiol., 2005. 138(4): p. 2233-44
    [PMID:16055689]
  8. Rajjou L, et al.
    Proteomic investigation of the effect of salicylic acid on Arabidopsis seed germination and establishment of early defense mechanisms.
    Plant Physiol., 2006. 141(3): p. 910-23
    [PMID:16679420]
  9. Hricová A,Quesada V,Micol JL
    The SCABRA3 nuclear gene encodes the plastid RpoTp RNA polymerase, which is required for chloroplast biogenesis and mesophyll cell proliferation in Arabidopsis.
    Plant Physiol., 2006. 141(3): p. 942-56
    [PMID:16698900]
  10. Chibani K, et al.
    Proteomic analysis of seed dormancy in Arabidopsis.
    Plant Physiol., 2006. 142(4): p. 1493-510
    [PMID:17028149]
  11. Espagne C,Martinez A,Valot B,Meinnel T,Giglione C
    Alternative and effective proteomic analysis in Arabidopsis.
    Proteomics, 2007. 7(20): p. 3788-99
    [PMID:17828791]
  12. Scranton MA,Yee A,Park SY,Walling LL
    Plant leucine aminopeptidases moonlight as molecular chaperones to alleviate stress-induced damage.
    J. Biol. Chem., 2012. 287(22): p. 18408-17
    [PMID:22493451]
  13. 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]
  14. Kumar S,Kaur A,Chattopadhyay B,Bachhawat AK
    Defining the cytosolic pathway of glutathione degradation in Arabidopsis thaliana: role of the ChaC/GCG family of γ-glutamyl cyclotransferases as glutathione-degrading enzymes and AtLAP1 as the Cys-Gly peptidase.
    Biochem. J., 2015. 468(1): p. 73-85
    [PMID:25716890]