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 PK07194.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Cannabaceae; Cannabis
Family C3H
Protein Properties Length: 695aa    MW: 77052.4 Da    PI: 6.233
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
PK07194.1genomeCCBRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH222.9e-07103127526
                --SGGGGTS...--TTTTT-SS-SS CS
    zf-CCCH   5 lCrffartG...tCkyGdrCkFaHg 26 
                +C+  a+tG    C+y d+C+F+H+
  PK07194.1 103 ICPEVAKTGdpsSCPYSDKCRFSHD 127
                7***********************7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:4.10.1000.101.8E-496129IPR000571Zinc finger, CCCH-type
PROSITE profilePS5010311.63898129IPR000571Zinc finger, CCCH-type
SMARTSM003560.007499128IPR000571Zinc finger, CCCH-type
PfamPF006425.5E-5103127IPR000571Zinc finger, CCCH-type
SMARTSM0035628139166IPR000571Zinc finger, CCCH-type
PROSITE profilePS501037.301142167IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.20.20.701.6E-68339582IPR013785Aldolase-type TIM barrel
SuperFamilySSF513951.03E-59343656No hitNo description
CDDcd028011.23E-83343578No hitNo description
PfamPF012077.0E-47346592IPR001269tRNA-dihydrouridine synthase
PROSITE patternPS011360427445IPR018517tRNA-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: 695 aa     Download sequence    Send to blast
MDESPADVQL VHEPKDSATP VVEASNGQPE YRTPEELVAK AIAPVKREFL RPPPVRPVSN  60
SNEDGAASES KEKPAQPSVG KEKKSKRQAK RDRLQQQKST SNICPEVAKT GDPSSCPYSD  120
KCRFSHDVEA FKDQKLEDLE GECPFVTAEE PCPYGLACRF LSTHPEGVSG MKSTRRNSSE  180
VNGLRKDVQR LLWKNKMKFP KADAKVKALG LMGPANSKAK ISENKDGDDV ITANNCDAAN  240
GNGSNALVDA TEIEKSAVLE ENKDVEDPSE SNESRPLKKP KCVDAEDCCD KVEGGGVSGT  300
ENVVCESSKQ PEADSAAEIL TPETDGSLKV HPREKKIIDF RDKLYLAPLT TVGNLPFRRV  360
CKVLGADVTC GEMAMCTNLL QGQASEWALL RRHVSEDLFG VQICGAFADT VSRAVELIEQ  420
ECSLDFIDIN MGCPIDLVCN KGAGSALLMK PMRMKGIIEA ASGTMEKPLT VKVRTAYFEG  480
KNRIDSLIAD MGNWGASAVT IHGRSRQQRY SKLADWEYVY QCANKAPDTL HVLGNGDIFS  540
YLDWNKRKVD CPKLSTCMIA RGALVKPWLF TEIKEQRHWD ISSGERLDIL KKFVRFGLEH  600
WGSDTKGVET TRRFLLEWLS YTCRYVPVGL LEVIPQRLNW RQPSYFGRND LETLMASDSA  660
ADWIRISEML LGKVPEDFTF APKHKSNAYD RAENG
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6ei9_A8e-2534058727266tRNA-dihydrouridine synthase B
6ei9_B8e-2534058727266tRNA-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_010095677.10.0tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
SwissprotQ9T0J60.0DUS3L_ARATH; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
TrEMBLA0A2P5FQ790.0A0A2P5FQ79_TREOI; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
STRINGXP_010095677.10.0(Morus notabilis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF108891212
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]