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 PH01001239G0650
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; BOP clade; Bambusoideae; Arundinarodae; Arundinarieae; Arundinariinae; Phyllostachys
Family BES1
Protein Properties Length: 608aa    MW: 68799.8 Da    PI: 5.5593
Description BES1 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
PH01001239G0650genomeICBRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1DUF822124.11.8e-3849123276
           DUF822   2 gsgrkptwkErEnnkrRERrRRaiaakiyaGLRaqGnyklpkraDnneVlkALcreAGwvvedDGttyrkgskpl 76 
                      g +r++  +E+E++k+RER+RRai+a+i+aGLR++Gny+l++raD+neV++AL+reAGwvv +DGtt++ +s+ +
  PH01001239G0650  49 GVRRSRAREEKERTKLRERQRRAITARILAGLRRHGNYNLRARADINEVIAALAREAGWVVLPDGTTFPSSSQSQ 123
                      668899999************************************************************988876 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PfamPF056875.7E-3551123IPR008540BES1/BZR1 plant transcription factor, N-terminal
SuperFamilySSF514456.32E-185136573IPR017853Glycoside hydrolase superfamily
Gene3DG3DSA:3.20.20.806.6E-201139573IPR013781Glycoside hydrolase, catalytic domain
PfamPF013731.4E-110145559IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73176190IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73197215IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73219240IPR001554Glycoside hydrolase, family 14
PROSITE patternPS005060223231IPR018238Glycoside hydrolase, family 14, conserved site
PRINTSPR008423.9E-9302311IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR007501.7E-73312334IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73385404IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73419435IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73436447IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.7E-73454477IPR001554Glycoside hydrolase, family 14
PRINTSPR008423.9E-9457467IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR007501.7E-73491513IPR001554Glycoside hydrolase, family 14
PRINTSPR008423.9E-9542556IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR008423.9E-9557571IPR001371Glycoside hydrolase, family 14B, plant
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0000272Biological Processpolysaccharide catabolic process
GO:0009570Cellular Componentchloroplast stroma
GO:0016161Molecular Functionbeta-amylase activity
Sequence ? help Back to Top
Protein Sequence    Length: 608 aa     Download sequence    Send to blast
MQRLQASEDE EEEMGVKEEE EGDDYSDDEH AGRYLASPGA MLPVVSGGGV RRSRAREEKE  60
RTKLRERQRR AITARILAGL RRHGNYNLRA RADINEVIAA LAREAGWVVL PDGTTFPSSS  120
QSQVADVVPR PPERDFAGTA YVPVYVMLPL GVVNGNGEVV DADGLVGQLR VLKAAGVDGV  180
MVDCWWGNVE AHRPQEYNWT GYKRLFRMIR ELKLKLQVVM SFHECGGNVG DDVSIPLPHW  240
VTETGRSNPD IYFTDKAGRR NMECLSWGID KERVLQGRTA VEVYFDYMRN FRVEFDEYFE  300
DGIISEIEIG LGACGELRYP SYPAKHGWKY PGIGEFQCYD RYFQKSLRKA AEARGHTIWA  360
RAPDNAGHYN SEPNLTGFFC DGGDYDSYYG RFFLNWYSQI LVDHADRVLM LARLAFEGSN  420
IAVKVSGVHW WYKSASHAAE LTAGFYNPCN RDGYAPIAAV LKKHGAALNF TCAELRTMDQ  480
HEVFPEAFAD PEGLVLNAAW DAGIPVASEN ALPCYDRDGF NKILENAKPL NDPDGRHLLG  540
FTYLRLSKVL FERPNFLEFE RFVKRMHGEA VLDLQRWCIL TKEADCMELE KLLKIVEDWM  600
KSFCTSK*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1bfn_A1e-15614156911444BETA-AMYLASE
1bya_A1e-15614156911444BETA-AMYLASE
1byb_A1e-15614156911444BETA-AMYLASE
1byc_A1e-15614156911444BETA-AMYLASE
1byd_A1e-15614156911444BETA-AMYLASE
1q6c_A1e-15614156911444beta-amylase
1wdp_A1e-15614156911444Beta-amylase
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtLow beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapPH01001239G0650
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Slightly by cold stress. {ECO:0000269|PubMed:16297066}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAK0703000.0AK070300.1 Oryza sativa Japonica Group cDNA clone:J023048N01, full insert sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_015696458.10.0PREDICTED: LOW QUALITY PROTEIN: beta-amylase 2, chloroplastic-like
SwissprotO652580.0BAM2_ARATH; Beta-amylase 2, chloroplastic
TrEMBLA0A0E0QVA70.0A0A0E0QVA7_ORYRU; Beta-amylase
STRINGORUFI09G21750.10.0(Oryza rufipogon)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MonocotsOGMP21413663
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G45880.10.0beta-amylase 7
Publications ? help Back to Top
  1. Smith AM,Zeeman SC,Smith SM
    Starch degradation.
    Annu Rev Plant Biol, 2005. 56: p. 73-98
    [PMID:15862090]
  2. Lundmark M,Cavaco AM,Trevanion S,Hurry V
    Carbon partitioning and export in transgenic Arabidopsis thaliana with altered capacity for sucrose synthesis grown at low temperature: a role for metabolite transporters.
    Plant Cell Environ., 2006. 29(9): p. 1703-14
    [PMID:16913860]
  3. Li J, et al.
    Catalytically-inactive beta-amylase BAM4 required for starch breakdown in Arabidopsis leaves is a starch-binding-protein.
    Arch. Biochem. Biophys., 2009. 489(1-2): p. 92-8
    [PMID:19664588]
  4. Andriotis VM,Pike MJ,Kular B,Rawsthorne S,Smith AM
    Starch turnover in developing oilseed embryos.
    New Phytol., 2010. 187(3): p. 791-804
    [PMID:20546137]
  5. Monroe JD, et al.
    Arabidopsis β-Amylase2 Is a K+-Requiring, Catalytic Tetramer with Sigmoidal Kinetics.
    Plant Physiol., 2017. 175(4): p. 1525-1535
    [PMID:29066669]