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 Rsa1.0_06190.1_g00003.1
Organism
Raphanus sativus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus
Family MYB
Protein Properties Length: 542aa    MW: 60641.3 Da    PI: 7.5168
Description MYB family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Rsa1.0_06190.1_g00003.1genomeRGDView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding55.99.5e-181461148
                             TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS-HHHHHHHHHHHT CS
          Myb_DNA-binding  1 rgrWTteEdellvdavkqlGggtWktIartmgkgRtlkqcksrwqkyl 48
                             +g+WT+eEd++l+ +++++G g+W++ +++ g++R++k+c++rw +yl
  Rsa1.0_06190.1_g00003.1 14 KGPWTQEEDQKLLAYIEEHGHGSWRSLPEKAGLHRCGKSCRLRWTNYL 61
                             79********************************************97 PP
2Myb_DNA-binding49.97.3e-1667112148
                              TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS-HHHHHHHHHHHT CS
          Myb_DNA-binding   1 rgrWTteEdellvdavkqlGggtWktIartmgkgRtlkqcksrwqkyl 48 
                              rg++  +E++ +++++++lG++ W++Ia +++ +Rt++++k++w+++l
  Rsa1.0_06190.1_g00003.1  67 RGKFNLQEEQTIIQLHALLGNR-WSAIATHLP-KRTDNEIKNYWNTHL 112
                              899*******************.*********.************996 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:1.10.10.606.9E-25563IPR009057Homeodomain-like
PROSITE profilePS5129418.509961IPR017930Myb domain
SuperFamilySSF466895.99E-3011108IPR009057Homeodomain-like
SMARTSM007171.1E-151363IPR001005SANT/Myb domain
PfamPF002493.2E-161461IPR001005SANT/Myb domain
CDDcd001671.35E-111661No hitNo description
PROSITE profilePS5129425.2562116IPR017930Myb domain
Gene3DG3DSA:1.10.10.602.2E-2564117IPR009057Homeodomain-like
SMARTSM007173.9E-1666114IPR001005SANT/Myb domain
PfamPF002495.0E-1567112IPR001005SANT/Myb domain
CDDcd001676.71E-1169112No hitNo description
Gene3DG3DSA:3.40.50.3004.1E-18438527IPR027417P-loop containing nucleoside triphosphate hydrolase
SuperFamilySSF525407.52E-10461525IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS5172021.15463542IPR006703AIG1-type guanine nucleotide-binding (G) domain
PfamPF045485.7E-12466525IPR006703AIG1-type guanine nucleotide-binding (G) domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0000902Biological Processcell morphogenesis
GO:0009651Biological Processresponse to salt stress
GO:0009723Biological Processresponse to ethylene
GO:0009733Biological Processresponse to auxin
GO:0009739Biological Processresponse to gibberellin
GO:0009751Biological Processresponse to salicylic acid
GO:0009753Biological Processresponse to jasmonic acid
GO:0046686Biological Processresponse to cadmium ion
GO:0003677Molecular FunctionDNA binding
GO:0005525Molecular FunctionGTP binding
Sequence ? help Back to Top
Protein Sequence    Length: 542 aa     Download sequence    Send to blast
MGRSPCCDKL GLKKGPWTQE EDQKLLAYIE EHGHGSWRSL PEKAGLHRCG KSCRLRWTNY  60
LRPDIKRGKF NLQEEQTIIQ LHALLGNRWS AIATHLPKRT DNEIKNYWNT HLKKRLVKMG  120
IDPVTHKPKN ETPLSSLGLT KNAAILSHMA QWESARLEAE ARLARESKLL HYQTKPSSHH  180
HHGFTHKTLL TTWTSKTSQD QQQQQLESPT STVSFSEMKE PSAAKTEFVG SSTCLNSIKE  240
PENDWFNSTV HEFETTEMAG GVDEGFMLAG DSLGRSLSDE KHETVKERSG GDCSNYYEED  300
NKNNYLDSIF SFVDPSPPMS EDMEEKKNAD DRIINDNTAS LLPPALPPVL GLGRGAPLLK  360
PTPPRRRVDG NVSQQAEDPP TTTDETSEKL QLIRVKFLRL SHRLGQTPSR NVVVAQFLYR  420
LGLAELSRGS SSSSRVGSTT NRAISMAEQL EAAGGEDQDH PLGFSCTIML LGKSGVGKSA  480
TINSIFDDDH QVKTDAFEMG TKRVQLVEGF VQGIKVRVMD TPGLSPSWFD NYRHSRPLTI  540
ML
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1a5j_A1e-25121165108B-MYB
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtInvolved in the control of epidermal cell morphogenesis in petals. Promotes unidirectional cell expansion once outgrowth has been initiated (PubMed:17376813). Coordinately with WIN1/SHN1, participates in the regulation of cuticle biosynthesis and wax accumulation in reproductive organs and trichomes. Functions in cuticle nanoridge formation in petals and stamens, and in morphogenesis of petal conical cells and trichomes (PubMed:23709630). Functions as a major regulator of cuticle formation in vegetative organs by regulating the cuticle biosynthesis genes CYP86A8/LCR and CER1 (PubMed:24169067). {ECO:0000269|PubMed:17376813, ECO:0000269|PubMed:23709630, ECO:0000269|PubMed:24169067}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapRsa1.0_06190.1_g00003.1
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_018475579.10.0PREDICTED: myb-related protein Hv1-like
SwissprotQ9LXF10.0MYB16_ARATH; Transcription factor MYB16
TrEMBLM4CQ070.0M4CQ07_BRARP; Uncharacterized protein
STRINGBra006296.1-P0.0(Brassica rapa)
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
AT5G15310.11e-159myb domain protein 16
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. Huang BH, et al.
    Positive selection and functional divergence of R2R3-MYB paralogous genes expressed in inflorescence buds of Scutellaria species (Labiatae).
    Int J Mol Sci, 2015. 16(3): p. 5900-21
    [PMID:25782156]
  4. Cui F, et al.
    Dissecting Abscisic Acid Signaling Pathways Involved in Cuticle Formation.
    Mol Plant, 2016. 9(6): p. 926-38
    [PMID:27060495]