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 Pp3c4_14410V3.2.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Bryophyta; Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrella
Family C3H
Protein Properties Length: 776aa    MW: 84356.4 Da    PI: 5.5423
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Pp3c4_14410V3.2.pgenomeCOSMOSSView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH22.22.4e-07149173526
                        --SGGGGTS...--TTTTT-SS-SS CS
            zf-CCCH   5 lCrffartG...tCkyGdrCkFaHg 26 
                        +C   a+tG    C++Gd+C+F+H+
  Pp3c4_14410V3.2.p 149 ICGAVAKTGdanACQFGDSCRFNHD 173
                        799999******************7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS501039.807144175IPR000571Zinc finger, CCCH-type
PfamPF006424.9E-5149173IPR000571Zinc finger, CCCH-type
PROSITE profilePS501038.803188213IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.20.20.702.3E-76418661IPR013785Aldolase-type TIM barrel
CDDcd028012.70E-98422658No hitNo description
SuperFamilySSF513956.28E-66422736No hitNo description
PfamPF012076.4E-54425666IPR001269tRNA-dihydrouridine synthase
PROSITE patternPS011360506524IPR018517tRNA-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: 776 aa     Download sequence    Send to blast
MEVGNDLSAG VGKSDVETAS QMADEVLKVA VAAELPSSVT AEEGLGGGST DGADGAQALS  60
KENYPSAEEL IAKSRAPVKR EYVVLNIAPR VMAKSIVITK EAVTNSPEEG TANAVEASKP  120
FTAKASVDKK SRRQRKRERK EAITSAENIC GAVAKTGDAN ACQFGDSCRF NHDLAAFMEQ  180
KPKDLEGLCP LLDVTSSCPY GFACRFSGSH PEVKGTEVAE VLKDGNYDGK NPMSSIRELN  240
SLNKSFQKLL WKNAVTFPKA DAQLQALGLL GKARKLVAKP SVVCKGDEAK PVLVYDDTAA  300
KVKFESSNIV EVSPEEAEII AASETTNGSA GLPGDGEVRT DGPDGPLSSD TSLINKEYPP  360
RKKVRTIVIE AADEALQQAS DNVLEATSGR SNSRVDDDDM KYLNDEVKEP LRDKKLVDFR  420
GKLYLAPLTT VGNLPFRRVC KKLGADITCG EMAMCTNLLQ GQASEWALLR RHEEEDIFGV  480
QICGSYADTV ARAAELIERE CTVDFIDLNV GCPIDVVVNK GGGSSLLTKP QRLQEIVRAA  540
SGSINTPLTV KLRMGFFEGR NCAHSLLPDL GSWGATAVTI HGRTRQQRYS KLADWDYINQ  600
CVTNGPSDVQ LIGNGDVFSY TDYNGHLESS GGKLATCMIA RGALIKPWLF TEIKEQRHWD  660
ITAEERLNIL RDYVKFGLIH WGSDSKGVET TRHFLLEWLS YAHRYIPVGL LDVIPQKLNW  720
RPPNYFGRND LETLMASDSA ADWVRLTEMV LGPPPPGFAF APKHKSNAYD KAENG*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ei9_A1e-2541965527258tRNA-dihydrouridine synthase B
6ei9_B1e-2541965527258tRNA-dihydrouridine synthase B
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1131139RRQRKRERK
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Ppa.40170.0protonema
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]