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 Bostr.18351s0132.1.p
Organism
Boechera stricta
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Boechereae; Boechera
Family MYB
Protein Properties Length: 241aa    MW: 27838.7 Da    PI: 9.2336
Description MYB family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Bostr.18351s0132.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding56.66e-181461148
                          TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS-HHHHHHHHHHHT CS
       Myb_DNA-binding  1 rgrWTteEdellvdavkqlGggtWktIartmgkgRtlkqcksrwqkyl 48
                          +g+WT+eEde+lv ++k +G g+W++ +r  g+ R++k+c++rw +yl
  Bostr.18351s0132.1.p 14 KGAWTKEEDERLVSYIKSHGEGCWRSLPRAAGLLRCGKSCRLRWINYL 61
                          79******************************99************97 PP
2Myb_DNA-binding57.82.4e-1867111147
                           TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS-HHHHHHHHHHH CS
       Myb_DNA-binding   1 rgrWTteEdellvdavkqlGggtWktIartmgkgRtlkqcksrwqky 47 
                           rg++T +Edel+++++ +lG++ W++Ia++++ gRt++++k++w+++
  Bostr.18351s0132.1.p  67 RGNFTHDEDELIIKLHSLLGNK-WSLIAARLP-GRTDNEIKNYWNTH 111
                           89********************.*********.************97 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:1.10.10.607.3E-24564IPR009057Homeodomain-like
PROSITE profilePS5129417.094961IPR017930Myb domain
SuperFamilySSF466891.42E-2912108IPR009057Homeodomain-like
SMARTSM007172.2E-131363IPR001005SANT/Myb domain
PfamPF002493.0E-151461IPR001005SANT/Myb domain
CDDcd001671.29E-91661No hitNo description
PROSITE profilePS5129428.75162116IPR017930Myb domain
Gene3DG3DSA:1.10.10.606.3E-2865116IPR009057Homeodomain-like
SMARTSM007173.2E-1766114IPR001005SANT/Myb domain
PfamPF002499.6E-1767111IPR001005SANT/Myb domain
CDDcd001672.84E-1169112No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0009651Biological Processresponse to salt stress
GO:0009751Biological Processresponse to salicylic acid
GO:1900384Biological Processregulation of flavonol biosynthetic process
GO:0003677Molecular FunctionDNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 241 aa     Download sequence    Send to blast
MGRSPCCEKE HMNKGAWTKE EDERLVSYIK SHGEGCWRSL PRAAGLLRCG KSCRLRWINY  60
LRPDLKRGNF THDEDELIIK LHSLLGNKWS LIAARLPGRT DNEIKNYWNT HIKRKLLSKG  120
IDPSTHRAIN EAKFSDSKKT EDQIVKDVSF GIKFEKTEKS GDQKQNKRNL NGLVCKEERV  180
EYYPVVVKEE ICPDLNLELR ISPPSPWQYQ RERSPYTASR FYMGNGMECS SETAKCQDRG  240
*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1h8a_C3e-281211625128MYB TRANSFORMING PROTEIN
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtTranscription factor involved in the negative regulation of flavonol biosynthesis. Represses the early phenylpropanoid genes, phenylalanine ammonia-lyase (PAL), cinnamate 4-hydroxylase (C4H) and 4-coumarate-CoA ligase (4CL), as well as the flavonoid-specific genes, flavonoid 3'-hydroxylase (F3'H) and dihydroflavonol 4-reductase (DFR) (PubMed:24319076). Plays a role in seed germination inhibition. Negatively regulates the expression of the abscisic acid (ABA) signaling transcription factor ABI5 in seeds (PubMed:25053018). {ECO:0000269|PubMed:24319076, ECO:0000269|PubMed:25053018}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapBostr.18351s0132.1.p
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Induced by abscisic acid (ABA) and osmotic stress (PubMed:25053018). Induced by salt stress (PubMed:24319076, PubMed:25053018). {ECO:0000269|PubMed:24319076, ECO:0000269|PubMed:25053018}.
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_002886068.11e-150transcription factor MYB7 isoform X1
SwissprotQ423791e-147MYB7_ARATH; Transcription factor MYB7
TrEMBLD7L7N31e-148D7L7N3_ARALL; Uncharacterized protein
STRINGBostr.18351s0132.1.p1e-180(Boechera stricta)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM4282646
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G16720.11e-149myb domain protein 7
Publications ? help Back to Top
  1. Duarte JM, et al.
    Expression pattern shifts following duplication indicative of subfunctionalization and neofunctionalization in regulatory genes of Arabidopsis.
    Mol. Biol. Evol., 2006. 23(2): p. 469-78
    [PMID:16280546]
  2. Ding Y, et al.
    Four distinct types of dehydration stress memory genes in Arabidopsis thaliana.
    BMC Plant Biol., 2013. 13: p. 229
    [PMID:24377444]
  3. Zhou M, et al.
    Changing a conserved amino acid in R2R3-MYB transcription repressors results in cytoplasmic accumulation and abolishes their repressive activity in Arabidopsis.
    Plant J., 2015. 84(2): p. 395-403
    [PMID:26332741]
  4. Lotkowska ME, et al.
    The Arabidopsis Transcription Factor MYB112 Promotes Anthocyanin Formation during Salinity and under High Light Stress.
    Plant Physiol., 2015. 169(3): p. 1862-80
    [PMID:26378103]
  5. Zhou M, et al.
    LNK1 and LNK2 Corepressors Interact with the MYB3 Transcription Factor in Phenylpropanoid Biosynthesis.
    Plant Physiol., 2017. 174(3): p. 1348-1358
    [PMID:28483877]
  6. Mondal SK,Roy S
    Genome-wide sequential, evolutionary, organizational and expression analyses of phenylpropanoid biosynthesis associated MYB domain transcription factors in Arabidopsis.
    J. Biomol. Struct. Dyn., 2018. 36(6): p. 1577-1601
    [PMID:28490275]