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 Tp57577_TGAC_v2_mRNA31100
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; Trifolieae; Trifolium
Family MYB
Protein Properties Length: 345aa    MW: 39830.9 Da    PI: 6.6
Description MYB family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Tp57577_TGAC_v2_mRNA31100genomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding49.31.1e-151461148
                               TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS-HHHHHHHHHHHT CS
            Myb_DNA-binding  1 rgrWTteEdellvdavkqlGggtWktIartmgkgRtlkqcksrwqkyl 48
                               +g+W++eEde l d+++++G  +W+  ++  g+ R++k+c++rw ++l
  Tp57577_TGAC_v2_mRNA31100 14 KGAWSKEEDECLSDYIHKHGHSNWRQLPKLAGLARCGKSCRLRWVNHL 61
                               79*******************************************996 PP

2Myb_DNA-binding23.61.2e-0768121248
                                SSS-HHHHHHHHHHHHHTTTT.-HHHHHHHHT......TTS-HHHHHHHHHHHT CS
            Myb_DNA-binding   2 grWTteEdellvdavkqlGgg.tWktIartmg......kgRtlkqcksrwqkyl 48 
                                g+ T eEde ++++++ lG++     I+   g      + R++k+c++rw ++l
  Tp57577_TGAC_v2_mRNA31100  68 GNYTREEDEMIIKLHHHLGNRyIIVIISVFHGyylntgLARCGKSCRLRWVNHL 121
                                789******************85555555555666699*************996 PP

3Myb_DNA-binding537.7e-17128172248
                                SSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS-HHHHHHHHHHHT CS
            Myb_DNA-binding   2 grWTteEdellvdavkqlGggtWktIartmgkgRtlkqcksrwqkyl 48 
                                g+ T eEde ++++++ lG++ W++Ia++++ gRt+ ++k++w++yl
  Tp57577_TGAC_v2_mRNA31100 128 GNYTREEDEMIIKLHHHLGNR-WSLIAEKLP-GRTDHEIKNYWHSYL 172
                                789******************.*********.************997 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5129421.749965IPR017930Myb domain
SMARTSM007174.2E-121363IPR001005SANT/Myb domain
PfamPF002493.1E-141461IPR001005SANT/Myb domain
Gene3DG3DSA:1.10.10.602.0E-221574IPR009057Homeodomain-like
SuperFamilySSF466891.97E-221591IPR009057Homeodomain-like
CDDcd001674.14E-91661No hitNo description
PROSITE profilePS500907.8462121IPR017877Myb-like domain
SMARTSM007172.4E-566123IPR001005SANT/Myb domain
PfamPF002493.1E-668121IPR001005SANT/Myb domain
Gene3DG3DSA:1.10.10.601.2E-1575128IPR009057Homeodomain-like
SuperFamilySSF466895.06E-22108178IPR009057Homeodomain-like
PROSITE profilePS5129425.284122176IPR017930Myb domain
SMARTSM007171.9E-16126174IPR001005SANT/Myb domain
PfamPF002491.4E-15128172IPR001005SANT/Myb domain
CDDcd001672.44E-11129172No hitNo description
Gene3DG3DSA:1.10.10.602.8E-24129176IPR009057Homeodomain-like
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0003677Molecular FunctionDNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 345 aa     Download sequence    Send to blast
MVRGPFYDKN GVKKGAWSKE EDECLSDYIH KHGHSNWRQL PKLAGLARCG KSCRLRWVNH  60
LKPNLKHGNY TREEDEMIIK LHHHLGNRYI IVIISVFHGY YLNTGLARCG KSCRLRWVNH  120
LKPNLKHGNY TREEDEMIIK LHHHLGNRWS LIAEKLPGRT DHEIKNYWHS YLKKCLKSKE  180
YKMLDLKLKP CDNIVEENDT HHFVAPKSPI SNVGKDFLYI LESSTLPMPA AETSPEDNSP  240
SSTNGRGIEE DTAAQWLALE AFNGDFWTEP FIIEDTLPED KSPSSTSSRG IEKDNADLWL  300
AFEAFSGDFW TEPFIIEDTY TTNEISNKDI DLLISDFYDG SYMF*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1h88_C1e-30141746157MYB PROTO-ONCOGENE PROTEIN
1h89_C1e-30141746157MYB PROTO-ONCOGENE PROTEIN
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtTranscription factor involved in cold-regulation of CBF genes and in the development of freezing tolerance. May be part of a complex network of transcription factors controlling the expression of CBF genes and other genes in response to cold stress. Binds to the MYB recognition sequences in the promoters of CBF1, CBF2 and CBF3 genes (PubMed:17015446). Involved in drought and salt tolerance. May enhance expression levels of genes involved in abscisic acid (ABA) biosynthesis and signaling, as well as those encoding stress-protective proteins (PubMed:19161942). {ECO:0000269|PubMed:17015446, ECO:0000269|PubMed:19161942}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapTp57577_TGAC_v2_mRNA31100
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By nitrogen, salicylic acid, NaCl and abscisic acid (ABA). {ECO:0000269|PubMed:16463103, ECO:0000269|PubMed:18541146, ECO:0000269|PubMed:9839469}.
UniProtINDUCTION: Induced by abscisic acid (ABA) and drought stress (PubMed:19161942). Induced by salt stress (PubMed:19161942). {ECO:0000269|PubMed:19161942}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
SwissprotQ9LTC48e-33MYB15_ARATH; Transcription factor MYB15
SwissprotQ9S9K96e-33MYB3_ARATH; Transcription factor MYB3
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF3134817
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G22640.13e-35myb domain protein 3
Publications ? help Back to Top
  1. Schnaubelt D, et al.
    Low glutathione regulates gene expression and the redox potentials of the nucleus and cytosol in Arabidopsis thaliana.
    Plant Cell Environ., 2015. 38(2): p. 266-79
    [PMID:24329757]
  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. Ma X, et al.
    CYCLIN-DEPENDENT KINASE G2 regulates salinity stress response and salt mediated flowering in Arabidopsis thaliana.
    Plant Mol. Biol., 2015. 88(3): p. 287-99
    [PMID:25948280]
  4. 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]
  5. Wada T,Hayashi N,Tominaga-Wada R
    Root hair formation at the root-hypocotyl junction in CPC-LIKE MYB double and triple mutants of Arabidopsis.
    Plant Signal Behav, 2015. 10(11): p. e1089372
    [PMID:26339713]
  6. Wada T,Tominaga-Wada R
    CAPRICE family genes control flowering time through both promoting and repressing CONSTANS and FLOWERING LOCUS T expression.
    Plant Sci., 2015. 241: p. 260-5
    [PMID:26706076]
  7. Song L, et al.
    A transcription factor hierarchy defines an environmental stress response network.
    Science, 2017.
    [PMID:27811239]
  8. 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]
  9. 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]
  10. Kim SH, et al.
    Phosphorylation of the transcriptional repressor MYB15 by mitogen-activated protein kinase 6 is required for freezing tolerance in Arabidopsis.
    Nucleic Acids Res., 2017. 45(11): p. 6613-6627
    [PMID:28510716]
  11. Chezem WR,Memon A,Li FS,Weng JK,Clay NK
    SG2-Type R2R3-MYB Transcription Factor MYB15 Controls Defense-Induced Lignification and Basal Immunity in Arabidopsis.
    Plant Cell, 2017. 29(8): p. 1907-1926
    [PMID:28733420]
  12. Pal S, et al.
    TransDetect Identifies a New Regulatory Module Controlling Phosphate Accumulation.
    Plant Physiol., 2017. 175(2): p. 916-926
    [PMID:28827455]