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 Sobic.002G136200.2.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum
Family BES1
Protein Properties Length: 597aa    MW: 67005.9 Da    PI: 4.7543
Description BES1 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Sobic.002G136200.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1DUF822119.54.6e-3761134376
                DUF822   3 sgrkptwkErEnnkrRERrRRaiaakiyaGLRaqGnyklpkraDnneVlkALcreAGwvvedDGttyrkgskpl 76 
                             r++  +E+E++k RER+RRai+ +i+aGLR++Gny l++raD+neV++AL+reAGwvv +DGtt++ +s+  
  Sobic.002G136200.2.p  61 PNRRRAREEKERTKMRERQRRAITGRILAGLRQHGNYSLRARADINEVIAALAREAGWVVLPDGTTFPSSSSSS 134
                           5799999*************************************************************877765 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PfamPF056871.0E-3362136IPR008540BES1/BZR1 plant transcription factor, N-terminal
SuperFamilySSF514454.7E-191153592IPR017853Glycoside hydrolase superfamily
Gene3DG3DSA:3.20.20.805.0E-208156590IPR013781Glycoside hydrolase, catalytic domain
PfamPF013738.2E-116162579IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77193207IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77214232IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77236257IPR001554Glycoside hydrolase, family 14
PROSITE patternPS005060240248IPR018238Glycoside hydrolase, family 14, conserved site
PRINTSPR008421.3E-8319328IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR007501.4E-77329351IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77402421IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77436452IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77453464IPR001554Glycoside hydrolase, family 14
PRINTSPR007501.4E-77471494IPR001554Glycoside hydrolase, family 14
PRINTSPR008421.3E-8474484IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR007501.4E-77511533IPR001554Glycoside hydrolase, family 14
PRINTSPR008421.3E-8562576IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR008421.3E-8577591IPR001371Glycoside 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: 597 aa     Download sequence    Send to blast
MQQAGPADDD EDEEMGVKEE EEDGDEEEED DDGYYMDPRS PAAATVVSTP GGGGGRAGGT  60
PNRRRAREEK ERTKMRERQR RAITGRILAG LRQHGNYSLR ARADINEVIA ALAREAGWVV  120
LPDGTTFPSS SSSSAAVAAQ VPDVAPRPPE RDFAGTPYVP VYVMLPLGVV NGNGEVVDAD  180
ELVGQLRVLK AAGVDGVMVD CWWGNVEAHR PQEYNWTGYR RLFQMIRELK LKLQVVMSFH  240
ECGGNVGDDI SIPLPHWVIE IGRSNPDIYF TDRAGRRNTE CLSWGIDKER VLQGRTAVEV  300
YFDFMRSFRV EFDEYFEDGI ISEIEIGLGA CGELRYPSYP AKHGWKYPGI GEFQCYDRYL  360
QKSLRKAAEA RGHTIWARGP DNAGHYNSEP NLTGFFCDGG DYDSYYGRFF LSWYSQTLVD  420
HADRVLMLAR LAFEGSNIAV KVSGVHWWYK TASHAAELTA GFYNPCNRDG YAPIAAVLKK  480
YDAALNFTCV ELRTMDQHEV YPEAFADPEG LVWQVLNAAW DAGIQVASEN ALPCYDRDGF  540
NKILENAKPL NDPDGRHLFG FTYLRLSNVL FERPNFFEFE RFVKRMHGEA VLDLQV*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1bfn_A1e-16315858911444BETA-AMYLASE
1bya_A1e-16315858911444BETA-AMYLASE
1byb_A1e-16315858911444BETA-AMYLASE
1byc_A1e-16315858911444BETA-AMYLASE
1byd_A1e-16315858911444BETA-AMYLASE
1q6c_A1e-16315858911444beta-amylase
1wdp_A1e-16315858911444Beta-amylase
Search in ModeBase
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Sbi.161540.0ovary
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
PlantRegMapSobic.002G136200.2.p
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
GenBankEU9569050.0EU956905.1 Zea mays clone 1577050 beta-amylase mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_002459849.20.0beta-amylase 2, chloroplastic
SwissprotO652580.0BAM2_ARATH; Beta-amylase 2, chloroplastic
TrEMBLA0A1W0W3Q20.0A0A1W0W3Q2_SORBI; Beta-amylase
STRINGORUFI09G21750.10.0(Oryza rufipogon)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MonocotsOGMP21413663
Representative plantOGRP4345912
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]