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 Niben101Scf10919g01035.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; Nicotiana
Family C3H
Protein Properties Length: 705aa    MW: 78286.4 Da    PI: 6.1064
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Niben101Scf10919g01035.1genomeBTI-
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH21.54e-07115139526
                               --SGGGGTS...--TTTTT-SS-SS CS
                   zf-CCCH   5 lCrffartG...tCkyGdrCkFaHg 26 
                               +C+  a+tG    C+y d+C+F+H+
  Niben101Scf10919g01035.1 115 ICPEVAKTGivsACPYSDKCRFSHD 139
                               5999********************7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5010310.728115141IPR000571Zinc finger, CCCH-type
PfamPF006421.2E-4115139IPR000571Zinc finger, CCCH-type
PROSITE profilePS501038.305154179IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.20.20.704.2E-73349592IPR013785Aldolase-type TIM barrel
CDDcd028013.11E-91353585No hitNo description
SuperFamilySSF513951.77E-63353666No hitNo description
PfamPF012072.0E-52356623IPR001269tRNA-dihydrouridine synthase
PROSITE patternPS011360437455IPR018517tRNA-dihydrouridine synthase, conserved site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0008033Biological ProcesstRNA processing
GO:0055114Biological Processoxidation-reduction process
GO:0017150Molecular FunctiontRNA dihydrouridine synthase activity
GO:0046872Molecular Functionmetal ion binding
GO:0050660Molecular Functionflavin adenine dinucleotide binding
Sequence ? help Back to Top
Protein Sequence    Length: 705 aa     Download sequence    Send to blast
MENETLTDSS PAATTTEHPE APVQQTSSNT DDGGVSQPFR TPEELVAKAI APVKREYLRP  60
PPSRPSNNND SNNSTVGVEN DDAAEAKSAP ILKEKKSKRQ IKRERRQEQK SPLHICPEVA  120
KTGIVSACPY SDKCRFSHDL EAFKAEKPAD IEGSCPFLVY EGPCPYGLAC RFAGTHEDDV  180
STQTEKISRK SSELNFFNKD TQKLLWKNKM KFPKAEATLK LLGLKGHPKD KILVDKEENG  240
EVVPKEPATD TKTDSNEAAS DCSNKVEITP SISPEDVVEN NLADDIRPLK KAKSSIDEIC  300
SSQASNGSSV QGEVLDSNCD VNKSDPTADM VTDSDKSLKL HPREKKLIDF RDKLYLAPLT  360
TVGNLPFRRV CKVLGADVTS GEMAMCTNLL QGQASEWALL RRHSSENLFG VQICGAYPDT  420
VTKTVELIEQ ECSVDFIDIN MGCPIDIVVN KGAGSALLTK PTRMKSVVEA ASATVDIPVT  480
IKVRTAYFEG KNRIDSLIAD IGNWGATAVT IHGRSRQQRY SKLADWDYIY QCVQRAPKSL  540
QVLGNGDVFS YLDWNKHKTD SPELSTCMIA RGALIKPWIF TEIKEQKHWD ITSGERLDIL  600
KDYARFGLEH WGSDSKGVET TRHFLLEWLS YTCRYVPVGL LEIIPQRINW RPPSYYGRDD  660
LETLMASDSA ADWIRISEML LGKVPAGFSF APKHKSNAYD RAENG
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ei9_A2e-2835059727266tRNA-dihydrouridine synthase B
6ei9_B2e-2835059727266tRNA-dihydrouridine synthase B
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtCatalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_009768328.10.0PREDICTED: tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
SwissprotQ9T0J60.0DUS3L_ARATH; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
TrEMBLA0A1U7VPK10.0A0A1U7VPK1_NICSY; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
STRINGXP_009768328.10.0(Nicotiana sylvestris)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA80391923
Publications ? help Back to Top
  1. Szponarski W,Sommerer N,Boyer JC,Rossignol M,Gibrat R
    Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography.
    Proteomics, 2004. 4(2): p. 397-406
    [PMID:14760709]