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 KZV41121.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae; Loxocarpinae; Dorcoceras
Family C3H
Protein Properties Length: 690aa    MW: 77303.8 Da    PI: 6.8961
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
KZV41121.1genomeCNUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH18.44e-0695119526
                 --SGGGGTS...--TTTTT-SS-SS CS
     zf-CCCH   5 lCrffartG...tCkyGdrCkFaHg 26 
                 lC+  a++G    C+y +rC+F+H+
  KZV41121.1  95 LCPEVAKSGkvsSCRYNERCRFSHD 119
                 799*********************7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5010310.88795121IPR000571Zinc finger, CCCH-type
PROSITE profilePS501037.563134159IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.20.20.702.6E-74334578IPR013785Aldolase-type TIM barrel
CDDcd028011.48E-94338572No hitNo description
SuperFamilySSF513952.56E-64338651No hitNo description
PfamPF012071.7E-54341608IPR001269tRNA-dihydrouridine synthase
PROSITE patternPS011360422440IPR018517tRNA-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: 690 aa     Download sequence    Send to blast
MEAGANSLNN VVSNPPETVS VRSTEELMAK SIAPVKREFL CPPSVKTSDS NNVNDSDVKK  60
ADVNYETSTP ILKEKKSKRQ LKRERREEKK SALHLCPEVA KSGKVSSCRY NERCRFSHDL  120
EAFKVQKPDD LEGSCPFLVN EGPCPYGLAC RFAGTHRDND ACVGNGTINS HKKDNETNIL  180
DKDFQKLLWK NKVKFPKADA SLKLLGLLGN GKGKKMVDGE NVDENFANGT EKIDENGCCK  240
VPAVLVNEVD SFLAVFEEDE KHETDLDDEL RLSKKTKFMV DETCSVQHNN GQIQQKEEVD  300
KSSGHNEQQT IVEHIIGDTD KSLKLHPHEK KLIDFSQRLY LAPLTTVGNL PYRRVCKALG  360
ADITCGEMAM CTNLLQGQAS EWALLRRHSS EDFFGVQICG AYPDTVAKTV ELIEKHCTVD  420
FIDINMGCPI DIVVNKGAGS ALLTKPMRMK SVVQASSRAV DTPVTIKVRT GYFEGKNRID  480
SLIHDIGNCG ASAITIHGRT RQQRYSKLAD WQYIYQCARA TPPGLQVLGN GDVFSYLDWN  540
IHHTDCPELS SCMIGRGALI KPWIFTEIKE QRNWDISSAE RLDILKDYVR FGLEHWGSDS  600
KGVETTRHFL LEWLSYTCRY VPVGLLDVIP QKINWRPPSY FGRDDLETLM ASDSAADWIR  660
ISEMLLGKVP TGFTFAPKHK SNAYDKAENG
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ei9_A1e-2833856930257tRNA-dihydrouridine synthase B
6ei9_B1e-2833856930257tRNA-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}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapKZV41121.1
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_011088544.10.0tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like isoform X2
SwissprotQ9T0J60.0DUS3L_ARATH; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
TrEMBLA0A2Z7C5C40.0A0A2Z7C5C4_9LAMI; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
STRINGMigut.B00123.1.p0.0(Erythranthe guttata)
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]