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 Sphfalx0100s0013.2.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Bryophyta; Sphagnophytina; Sphagnopsida; Sphagnales; Sphagnaceae; Sphagnum
Family C3H
Protein Properties Length: 896aa    MW: 99152.7 Da    PI: 6.841
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Sphfalx0100s0013.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH22.52e-07237261526
                           --SGGGGTS...--TTTTT-SS-SS CS
               zf-CCCH   5 lCrffartG...tCkyGdrCkFaHg 26 
                           lC   a+tG    C++G +C+F+H+
  Sphfalx0100s0013.2.p 237 LCGSVAKTGdvnACRFGTSCHFNHD 261
                           9***********************7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS501039.056232263IPR000571Zinc finger, CCCH-type
PfamPF006421.2E-4236261IPR000571Zinc finger, CCCH-type
PROSITE profilePS501036.23276301IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.20.20.701.9E-77538781IPR013785Aldolase-type TIM barrel
SuperFamilySSF513951.33E-66542856No hitNo description
CDDcd028019.62E-98542778No hitNo description
PfamPF012074.9E-56545813IPR001269tRNA-dihydrouridine synthase
PROSITE patternPS011360626644IPR018517tRNA-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: 896 aa     Download sequence    Send to blast
MMVDIAKKTL VRTLLTFSLT SLKLSSPIVG RNSSLRDGER CRPPDCCRDL ISNPEFNRGI  60
AWEKNRQSVE HDDDLQRLGF ALGAECPPSW PCHAACDLRS LSQSLRVAIS FAAMETEHVE  120
GKSAGNGILA SGTQTMSDSA KPALESNDAY PSVEELIAKA RAPVKREYLR QSGTRVLANT  180
VVMTEETMAK LREEEGDDAE MMPSGNSIPK TSVEKKSKRQ QRRDRKEARS NKSVENLCGS  240
VAKTGDVNAC RFGTSCHFNH DLAAYLAQKP PDIPGQCPFL GGDIRCPYGY ACRYVGTHPK  300
TSSADLEGQL SKAETRDKNG PLSSIQELNN LNKGFQKLLW KNAVTFPKAD AQLGALGLLG  360
KAKKIVMKIS ANGSEKDTKQ SAPMDPAPQM SLVESLGNEI KEAIKPVSPT DLVLNNLDVE  420
LLATPVEKIS VYTQTGSLEI SLPDEVSKIS KELEPTRTGG LAGMPSSAFT SLDTEFPPQK  480
RIRTETETTE FGDDGHEIFG FRENGDEERT NREIEDDKDW KSMANEVTLP LREKKLIDFR  540
GKLYLAPLTT VGNLPFRRVC KKLGADITCG EMAMCTNLLQ GQASEWALLR RHAEEDMFGV  600
QICGAHPDTV ARAAELIERE CQVDFIDLNL GCPIDLVVNK GAGSSLLTKP ARLEQIVRAT  660
AAAIDTPLTL KVRMGYFEGR NCAHSLIPRM ARWGASAVTV HGRTRQQRYS KAADWDYVQQ  720
CVREVPDDLQ LVGNGDIFSY TEYGKHIQAC GSKLATCMIA RGALVKPWIF TEIKEQRHWD  780
ITAEERLNIL RDYVAFGLKH WGSDTKGVET TRHFLLEWLS YAHRYIPVGL LEVIPQQLNW  840
RPPNYFGRND LETLMASDSA ADWVRLTELV LGPPPSNFTF SPKHKSNAYD KAENG*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ei9_A6e-2953977527258tRNA-dihydrouridine synthase B
6ei9_B6e-2953977527258tRNA-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_024374675.10.0tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
SwissprotQ9T0J60.0DUS3L_ARATH; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
TrEMBLA0A2K1KNF40.0A0A2K1KNF4_PHYPA; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
STRINGPP1S219_23V6.10.0(Physcomitrella patens)
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]