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 SapurV1A.3302s0010.1.p
Organism
Salix purpurea
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; Salix
Family RAV
Protein Properties Length: 364aa    MW: 40899.9 Da    PI: 9.2299
Description RAV family protein
Gene Model
Gene Model ID Type Source Coding Sequence
SapurV1A.3302s0010.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP244.15.2e-1469117155
                     AP2   1 sgykGVrwdkkrgrWvAeIrdpsengkrkrfslgkfgtaeeAakaaiaarkkleg 55 
                             s+ykGV   + +grW A+I++      ++r++lg+f  ++eAa+a++ a+++++g
  SapurV1A.3302s0010.1.p  69 SKYKGVVPQP-NGRWGAQIYEK-----HQRVWLGTFNEENEAARAYDIAAQRFRG 117
                             89****9888.8*********3.....5*************************98 PP
2B3104.46e-33202303196
                             EEEE-..-HHHHTT-EE--HHH.HTT......---..--SEEEEEETTS-EEEEEE..EEETTEEEE-TTHHHHHHHHT--TT-EEE CS
                      B3   1 ffkvltpsdvlksgrlvlpkkfaeeh......ggkkeesktltledesgrsWevkliyrkksgryvltkGWkeFvkangLkegDfvv 81 
                             f+k+ tpsdv+k++rlv+pk++ae+h      ++++++++ l led sg++W+++++y+++s++yvltkGW++Fvk+++Lk+gD+v 
  SapurV1A.3302s0010.1.p 202 FEKAVTPSDVGKLNRLVIPKQHAEKHfplqstSNNSTKGVLLNLEDVSGKVWRFRYSYWNSSQSYVLTKGWSRFVKEKNLKAGDTVC 288
                             89*****************************9888899************************************************* PP

                             EEE-SSSEE..EEEE CS
                      B3  82 Fkldgrsefelvvkv 96 
                             F+++   +++l++ +
  SapurV1A.3302s0010.1.p 289 FQRSTGPDKQLYIDW 303
                             **8766777777766 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF541711.24E-1669125IPR016177DNA-binding domain
CDDcd000181.20E-2569127No hitNo description
PfamPF008476.2E-969117IPR001471AP2/ERF domain
PROSITE profilePS5103220.0270125IPR001471AP2/ERF domain
SMARTSM003804.0E-2870131IPR001471AP2/ERF domain
Gene3DG3DSA:3.30.730.106.4E-2070126IPR001471AP2/ERF domain
Gene3DG3DSA:2.40.330.102.4E-41197309IPR015300DNA-binding pseudobarrel domain
CDDcd100174.69E-30201292No hitNo description
SuperFamilySSF1019362.35E-31201301IPR015300DNA-binding pseudobarrel domain
PfamPF023628.7E-30202303IPR003340B3 DNA binding domain
PROSITE profilePS5086314.508202307IPR003340B3 DNA binding domain
SMARTSM010191.4E-26202307IPR003340B3 DNA binding domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0003677Molecular FunctionDNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 364 aa     Download sequence    Send to blast
MDGSCIDEST ISITDNAISI TPACLSPFPP PATTTKSPSE SLCRVGSGNS VILDLESGVE  60
AESRKLPSSK YKGVVPQPNG RWGAQIYEKH QRVWLGTFNE ENEAARAYDI AAQRFRGRDS  120
VTNFKQVDET EDDEIEAAFL NAHSKAEIVD MLRKHTYSDE LEQSKRNHKS NKGANGKQYN  180
NYGDNSYDHG CVRVLRAREQ LFEKAVTPSD VGKLNRLVIP KQHAEKHFPL QSTSNNSTKG  240
VLLNLEDVSG KVWRFRYSYW NSSQSYVLTK GWSRFVKEKN LKAGDTVCFQ RSTGPDKQLY  300
IDWKPRGASS LVQPVQMVRL FGVNIFNVPG MENGCNGKRS MRDLELLSID HQYSKKQRIV  360
RAL*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1wid_A4e-5919931111122DNA-binding protein RAV1
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtTranscriptional repressor of flowering time on long day plants. Acts directly on FT expression by binding 5'-CAACA-3' and 5'-CACCTG-3 sequences. Functionally redundant with TEM2. {ECO:0000269|PubMed:18718758}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapSapurV1A.3302s0010.1.p
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Expressed with a circadian rhythm showing a peak at dawn. {ECO:0000269|PubMed:18718758}.
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_011021709.10.0PREDICTED: AP2/ERF and B3 domain-containing transcription repressor TEM1-like
SwissprotQ9C6M51e-150RAVL1_ARATH; AP2/ERF and B3 domain-containing transcription repressor TEM1
TrEMBLB9HWL70.0B9HWL7_POPTR; Uncharacterized protein
STRINGPOPTR_0010s13930.10.0(Populus trichocarpa)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF29203274
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G25560.11e-152RAV family protein
Publications ? help Back to Top
  1. Ding Y, et al.
    Four distinct types of dehydration stress memory genes in Arabidopsis thaliana.
    BMC Plant Biol., 2013. 13: p. 229
    [PMID:24377444]
  2. Choi D, et al.
    iNID: an analytical framework for identifying network models for interplays among developmental signaling in Arabidopsis.
    Mol Plant, 2014. 7(5): p. 792-813
    [PMID:24380880]
  3. Sgamma T,Jackson A,Muleo R,Thomas B,Massiah A
    TEMPRANILLO is a regulator of juvenility in plants.
    Sci Rep, 2014. 4: p. 3704
    [PMID:24424565]
  4. Matías-Hernández L,Aguilar-Jaramillo AE,Marín-González E,Suárez-López P,Pelaz S
    RAV genes: regulation of floral induction and beyond.
    Ann. Bot., 2014. 114(7): p. 1459-70
    [PMID:24812253]
  5. Marín-González E, et al.
    SHORT VEGETATIVE PHASE Up-Regulates TEMPRANILLO2 Floral Repressor at Low Ambient Temperatures.
    Plant Physiol., 2015. 169(2): p. 1214-24
    [PMID:26243615]
  6. Matías-Hernández L, et al.
    TEMPRANILLO Reveals the Mesophyll as Crucial for Epidermal Trichome Formation.
    Plant Physiol., 2016. 170(3): p. 1624-39
    [PMID:26802039]