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 Migut.E00236.1.p
Common NameLOC105974677, MIMGU_mgv1a007753mg
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Phrymaceae; Erythranthe
Family Trihelix
Protein Properties Length: 397aa    MW: 44330.4 Da    PI: 5.8587
Description Trihelix family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Migut.E00236.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1trihelix77.91.5e-2476160286
          trihelix   2 WtkqevlaLiearremeerlrrgklkkplWeevskkmrergferspkqCkekwenlnkrykkikegekkrtsessstcpyfdqle 86 
                       W ++e++aLi +r+e++  ++++k++k+lW+ +s kmre+gf rsp++C++kw+nl k++kk k++++++    s ++  ++++e
  Migut.E00236.1.p  76 WVQEETRALILLRKEIDMMFNTSKSNKHLWDNISLKMREKGFDRSPTMCTDKWRNLLKEFKKAKQNNQDGGGSGSAKMNCYKEIE 160
                       **********************************************************************888888999999987 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:1.10.10.602.2E-467137IPR009057Homeodomain-like
PROSITE profilePS500908.33968132IPR017877Myb-like domain
SMARTSM007176.9E-572134IPR001005SANT/Myb domain
CDDcd122032.85E-2674139No hitNo description
PfamPF138373.2E-1875162No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0005634Cellular Componentnucleus
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0042802Molecular Functionidentical protein binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 397 aa     Download sequence    Send to blast
MYMSEKPQPQ PESAIDFYTG DKQEAPHHSS NMIIHHIAAA DATSSGGDES AAAAAANNSA  60
NHPSSSLAPK KRAETWVQEE TRALILLRKE IDMMFNTSKS NKHLWDNISL KMREKGFDRS  120
PTMCTDKWRN LLKEFKKAKQ NNQDGGGSGS AKMNCYKEIE EILRERSKNG PTWKSSEDGG  180
GGGGPKVDDS FMQFADKGID DTSLTFGPVE ANGRSTLNLE RRLDHEGHPL AITAAEVVVA  240
SGASPWNWRE TPRSGEQTNT YDGRVITVKL GDFTKRIGID GSADGIKEAI KSAFGLRTKR  300
AFWLEDDDNV VRTLDRDMPL GNYTLHVDEG LTIKVCFYEE TGPMPVHAED KTFYNEDDFR  360
DFLSRRRWTC LREYNGFRNI DSMEELCPGV IYRGVN*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2jmw_A2e-3970158186DNA binding protein GT-1
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtProbable transcription factor that binds specifically to the core DNA sequence 5'-GGTTAA-3'. May act as a molecular switch in response to light signals. {ECO:0000269|PubMed:10437822, ECO:0000269|PubMed:15044016, ECO:0000269|PubMed:7866025}.
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00640PBMTransfer from MDP0000164819Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMapMigut.E00236.1.p
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieveRetrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_012855256.10.0PREDICTED: trihelix transcription factor GT-4-like
SwissprotQ9FX531e-155TGT1_ARATH; Trihelix transcription factor GT-1
TrEMBLA0A022Q4L30.0A0A022Q4L3_ERYGU; Uncharacterized protein
STRINGMigut.E00236.1.p0.0(Erythranthe guttata)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA51132136
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G13450.11e-156Trihelix family protein
Publications ? help Back to Top
  1. Le Gourrierec J,Li YF,Zhou DX
    Transcriptional activation by Arabidopsis GT-1 may be through interaction with TFIIA-TBP-TATA complex.
    Plant J., 1999. 18(6): p. 663-8
    [PMID:10417717]