PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Dca41227.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus
Family C3H
Protein Properties Length: 697aa    MW: 77517.5 Da    PI: 6.0475
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Dca41227.1genomeDCAView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH185.2e-061241361426
                 --TTTTT-SS-SS CS
     zf-CCCH  14 tCkyGdrCkFaHg 26 
                  C++Gd+C+F+H+
  Dca41227.1 124 SCRFGDKCRFSHD 136
                 8***********7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5010311.882112138IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:4.10.1000.109.0E-4120141IPR000571Zinc finger, CCCH-type
PROSITE profilePS501039.019151176IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.20.20.703.8E-73341585IPR013785Aldolase-type TIM barrel
SuperFamilySSF513959.16E-64345657No hitNo description
CDDcd028011.01E-91345579No hitNo description
PfamPF012074.0E-49348615IPR001269tRNA-dihydrouridine synthase
PROSITE patternPS011360429447IPR018517tRNA-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: 697 aa     Download sequence    Send to blast
MAESIPENSS AQPPPSTVNS VSMDESVTES SIQNSSAQPP STSAMFEKIC KMSAEELVAK  60
AIAPVKKEFL RPPPSSRLTS ENDDGEKKSV VAEKKSKRSL RRERHNERLA GLCSEVAKTE  120
DVNSCRFGDK CRFSHDLEAY RLQKPADLEG ECPFITPTKR CPYGASCRFS GTHKPVDGDT  180
FNDLREDFEV NSLRKDVQKL LWKNKMKFPK SNTALKQLGV TGKGFTKVTD TEENGVDQSV  240
SNGSHCAEDN GCEKDNAGNK QNESSVLEKE SDDGISVNDG GRPLKKAKAA DDEKPCSDDV  300
KNGDAVMRNA SDDEREITTE NILPETDASL KLHPRERKLI DFRGKLYLAP LTTVGNLPFR  360
RVCKGLGADV TCGEMAMCTN LLQGQASEWA LLRRHKSEDL FGVQICGAYP DVVGRAAELI  420
DLECSVDFID INMGCPIDLV VNKGAGSALI TKPLRMKNVI QAACASSEKP ITVKVRTGYI  480
EGRNRIDSMI ADIYDWGASA ITIHGRSRQQ RYSKLADWGY VYDCVRKAPS SFPVLGNGDV  540
FSYQDWNTHL SDCPELSSCM VARGALIKPW LFTEIKEQRN WDISSSERLD ILRDYVRFGL  600
EHWGSDTKGV ETTRHFLLEW MSYMFRYVPV GLLEVVPQKP NWRPPSYFGR NDLETMMASE  660
SAADWIRISE MLLGKVPDGF TFAPKHKSNA YDSAENG
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ei9_A2e-2734257727258tRNA-dihydrouridine synthase B
6ei9_B2e-2734257727258tRNA-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}.
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_021738748.10.0tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
RefseqXP_021738749.10.0tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
RefseqXP_021738750.10.0tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
SwissprotQ9T0J60.0DUS3L_ARATH; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
TrEMBLA0A0K9RD760.0A0A0K9RD76_SPIOL; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
STRINGXP_010665864.10.0(Beta vulgaris)
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]