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 Pavir.2NG236800.1.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; Panicodae; Paniceae; Panicinae; Panicum
Family BES1
Protein Properties Length: 584aa    MW: 65886.1 Da    PI: 4.9406
Description BES1 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Pavir.2NG236800.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1DUF822119.64.3e-3753127680
               DUF822   6 kptwkErEnnkrRERrRRaiaakiyaGLRaqGnyklpkraDnneVlkALcreAGwvvedDGttyrkgskpleeae 80 
                          +++++E E++k+RER+RRai+ +i+aGLR++Gny+l++raD+neV++AL+reAGw+v +DGtt++ +s p+ +a+
  Pavir.2NG236800.1.p  53 RRRAREEERTKLRERQRRAITGRILAGLRQHGNYCLRARADINEVIAALAREAGWIVLPDGTTFPTSSPPPAAAQ 127
                          5789*************************************************************9998884444 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PfamPF056875.4E-3453126IPR008540BES1/BZR1 plant transcription factor, N-terminal
SuperFamilySSF514454.09E-191140579IPR017853Glycoside hydrolase superfamily
Gene3DG3DSA:3.20.20.802.5E-208143577IPR013781Glycoside hydrolase, catalytic domain
PfamPF013733.5E-116149567IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78180194IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78201219IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78223244IPR001554Glycoside hydrolase, family 14
PROSITE patternPS005060227235IPR018238Glycoside hydrolase, family 14, conserved site
PRINTSPR008422.3E-8306315IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR007508.5E-78316338IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78389408IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78423439IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78440451IPR001554Glycoside hydrolase, family 14
PRINTSPR007508.5E-78458481IPR001554Glycoside hydrolase, family 14
PRINTSPR008422.3E-8461471IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR007508.5E-78498520IPR001554Glycoside hydrolase, family 14
PRINTSPR008422.3E-8549563IPR001371Glycoside hydrolase, family 14B, plant
PRINTSPR008422.3E-8564578IPR001371Glycoside hydrolase, family 14B, plant
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0000272Biological Processpolysaccharide catabolic process
GO:0016161Molecular Functionbeta-amylase activity
Sequence ? help Back to Top
Protein Sequence    Length: 584 aa     Download sequence    Send to blast
MQQAEDEDEE MGVKEEDGDE EEEDDGCFYM DPCPVSAASP TGSGGVGRAN PGRRRAREEE  60
RTKLRERQRR AITGRILAGL RQHGNYCLRA RADINEVIAA LAREAGWIVL PDGTTFPTSS  120
PPPAAAQVPD VAPRPPERDF AGTPYVPVYV MLPLGVVNVN GEVVDADELV GQLRVLKAAG  180
VDGVMVDCWW GNVEAHRPQE YNWTGYKRLF QMIRELKLKL QVVMSFHECG GNVGDDVSIP  240
LPHWVTEIGR SNPDIYFTDR AGRRNTECLS WGIDKERVLQ GRTAVEVYFD FMRSFRVEFD  300
EYFEDGIISE IEIGLGACGE LRYPSYPAKH GWKYPGIGEF QCYDRYLQKN LRRAAEARGH  360
TIWARGPGNA GHYNSEPNLT GFFCDGGDYD SYYGRFFLNW YSQMLVDHAD RVLMLARLAF  420
EGSSIAVKVS GVHWWYKTAS HAAELTAGFY NPCNRDGYAP IAAVLKKYDA ALNFTCVELR  480
TMDQHEVYPE AFADPEGLVW QVLNAAWDAG IQVASENALP CYDRDGFNKI LENAKPLNDP  540
DGRHLFGFTY LRLSKVLFER RNFFEFERFV KRMHGEAVLD LQV*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1bya_A1e-16214557611444BETA-AMYLASE
1byb_A1e-16214557611444BETA-AMYLASE
1byc_A1e-16214557611444BETA-AMYLASE
1byd_A1e-16214557611444BETA-AMYLASE
Search in ModeBase
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Pvr.347370.0callus| leaf| root
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
PlantRegMapPavir.2NG236800.1.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
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]