PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID KHN14288.1
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; Phaseoleae; Glycine; Soja
Family MYB_related
Protein Properties Length: 390aa    MW: 43457.9 Da    PI: 10.4321
Description MYB_related family protein
Gene Model
Gene Model ID Type Source Coding Sequence
KHN14288.1genomeTCUHKView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding36.79.5e-1296147147
                      TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHT.....TTS-HHHHHHHHHHH CS
  Myb_DNA-binding   1 rgrWTteEdellvdavkqlGggtWktIartmg.....kgRtlkqcksrwqky 47 
                      +++WT+eE++ l+ +v ++G g W+tI +          R+  ++k++w+++
       KHN14288.1  96 KQKWTAEEEQALKAGVVKHGVGKWRTILKDPEfsgvlYLRSNVDLKDKWRNL 147
                      79***********************************88***********96 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS512949.52391149IPR017930Myb domain
SuperFamilySSF466893.24E-1693162IPR009057Homeodomain-like
Gene3DG3DSA:1.10.10.601.9E-1395147IPR009057Homeodomain-like
SMARTSM007171.7E-795150IPR001005SANT/Myb domain
PfamPF002492.7E-896147IPR001005SANT/Myb domain
CDDcd116601.34E-1997147No hitNo description
SMARTSM005262.4E-10209274IPR005818Linker histone H1/H5, domain H15
SuperFamilySSF467854.19E-15209288IPR011991Winged helix-turn-helix DNA-binding domain
Gene3DG3DSA:1.10.10.106.6E-13210279IPR011991Winged helix-turn-helix DNA-binding domain
PROSITE profilePS5150424.418211279IPR005818Linker histone H1/H5, domain H15
PfamPF005389.6E-8214272IPR005818Linker histone H1/H5, domain H15
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006334Biological Processnucleosome assembly
GO:0006357Biological Processregulation of transcription from RNA polymerase II promoter
GO:0009651Biological Processresponse to salt stress
GO:0009723Biological Processresponse to ethylene
GO:0009733Biological Processresponse to auxin
GO:0009737Biological Processresponse to abscisic acid
GO:0009739Biological Processresponse to gibberellin
GO:0009751Biological Processresponse to salicylic acid
GO:0009753Biological Processresponse to jasmonic acid
GO:0046686Biological Processresponse to cadmium ion
GO:0000786Cellular Componentnucleosome
GO:0005730Cellular Componentnucleolus
GO:0003691Molecular Functiondouble-stranded telomeric DNA binding
GO:0033613Molecular Functionactivating transcription factor binding
GO:0042803Molecular Functionprotein homodimerization activity
GO:0070491Molecular Functionrepressing transcription factor binding
GO:1990841Molecular Functionpromoter-specific chromatin binding
Sequence ? help Back to Top
Protein Sequence    Length: 390 aa     Download sequence    Send to blast
MYLLNAHAVG SLVRLGHLAR DANKSGTLNH QSNPNQFIFL QFQLRFLPLF RSLSLFSHYF  60
LADISQIPLL GFRRTNQNSI VLAESVFDLH AMGAPKQKWT AEEEQALKAG VVKHGVGKWR  120
TILKDPEFSG VLYLRSNVDL KDKWRNLSVM ANGWSSREKS RLSVRRVHQV PRQDENSMAI  180
TPVVPSDEEI VDVKPLQVSR DIVHIPGPKR SNLSLDKLIM EAITSLKENG GSNKTAIAAF  240
IEDQYWALPG LKSMLSAKLK FLTASGKLIK VNRKYRIAPI AAYSDRRRNS SMLYLKGRQK  300
ASMKIDRDET NILTRSQIDL ELEKIRSMTP QEAAAFAARA VAEAEAAIAE AEEAAKEAEA  360
AEADAEAAQA FADATTKSAK GRKSPKRIHT
Functional Description ? help Back to Top
Source Description
UniProtBinds preferentially double-stranded telomeric repeats. {ECO:0000269|PubMed:19102728}.
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00607ChIP-seqTransfer from AT1G49950Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMapKHN14288.1
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieveRetrieve
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankBT0983180.0BT098318.1 Soybean clone JCVI-FLGm-23G7 unknown mRNA.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_006597673.20.0telomere repeat-binding factor 1 isoform X1
RefseqXP_028204580.10.0telomere repeat-binding factor 1-like isoform X1
SwissprotQ8VWK44e-96TRB1_ARATH; Telomere repeat-binding factor 1
TrEMBLA0A445GT910.0A0A445GT91_GLYSO; Telomere repeat-binding factor 1 isoform A
TrEMBLI1MG870.0I1MG87_SOYBN; Uncharacterized protein
STRINGGLYMA15G14320.40.0(Glycine max)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF145333101
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G49950.32e-97telomere repeat binding factor 1
Publications ? help Back to Top
  1. Alexandrov NN, et al.
    Features of Arabidopsis genes and genome discovered using full-length cDNAs.
    Plant Mol. Biol., 2006. 60(1): p. 69-85
    [PMID:16463100]
  2. Schrumpfová PP, et al.
    Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase.
    Plant J., 2014. 77(5): p. 770-81
    [PMID:24397874]
  3. Qi X, et al.
    Identification of a novel salt tolerance gene in wild soybean by whole-genome sequencing.
    Nat Commun, 2014. 5: p. 4340
    [PMID:25004933]
  4. Liang SC, et al.
    Kicking against the PRCs - A Domesticated Transposase Antagonises Silencing Mediated by Polycomb Group Proteins and Is an Accessory Component of Polycomb Repressive Complex 2.
    PLoS Genet., 2015. 11(12): p. e1005660
    [PMID:26642436]
  5. Fulcher N,Riha K
    Using Centromere Mediated Genome Elimination to Elucidate the Functional Redundancy of Candidate Telomere Binding Proteins in Arabidopsis thaliana.
    Front Genet, 2015. 6: p. 349
    [PMID:26779251]
  6. Kotliński M, et al.
    Phylogeny-Based Systematization of Arabidopsis Proteins with Histone H1 Globular Domain.
    Plant Physiol., 2017. 174(1): p. 27-34
    [PMID:28298478]