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 MDP0000255768
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Malus
Family WRKY
Protein Properties Length: 951aa    MW: 105300 Da    PI: 8.5941
Description WRKY family protein
Gene Model
Gene Model ID Type Source Coding Sequence
MDP0000255768genomeGDRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1WRKY99.71.8e-31114170258
                    --SS-EEEEEEE--TT-SS-EEEEEE-STT---EEEEEE-SSSTTEEEEEEES--SS CS
           WRKY   2 dDgynWrKYGqKevkgsefprsYYrCtsagCpvkkkversaedpkvveitYegeHnh 58 
                    dDgy+WrKYGqK++k+s++prsYYrCt ++C++kk+vers+e+p++++itYeg H h
  MDP0000255768 114 DDGYKWRKYGQKSIKNSPNPRSYYRCTNPRCSAKKQVERSSEEPDTLIITYEGLHLH 170
                    8******************************************************99 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5081126.9108173IPR003657WRKY domain
Gene3DG3DSA:2.20.25.808.9E-29111170IPR003657WRKY domain
SuperFamilySSF1182907.98E-26111170IPR003657WRKY domain
SMARTSM007741.6E-35113172IPR003657WRKY domain
PfamPF031066.5E-25114170IPR003657WRKY domain
PfamPF064806.6E-7440567IPR011546Peptidase M41, FtsH extracellular
TIGRFAMsTIGR012413.8E-143582948IPR005936Peptidase, FtsH
Gene3DG3DSA:3.40.50.3005.6E-46637811IPR027417P-loop containing nucleoside triphosphate hydrolase
SuperFamilySSF525402.27E-55638876IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM003825.2E-9674805IPR003593AAA+ ATPase domain
CDDcd000091.30E-17675747No hitNo description
PfamPF000042.4E-27679785IPR003959ATPase, AAA-type, core
Gene3DG3DSA:1.10.8.606.0E-24812879No hitNo description
PfamPF014343.1E-27865949IPR000642Peptidase M41
SuperFamilySSF1409907.85E-17886949No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0006508Biological Processproteolysis
GO:0016021Cellular Componentintegral component of membrane
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0004222Molecular Functionmetalloendopeptidase activity
GO:0005524Molecular FunctionATP binding
GO:0008270Molecular Functionzinc ion binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 951 aa     Download sequence    Send to blast
MEEAMXATWS DGSEEELVRE LLDNESPFFV LPEESVQSRT TSAFGKEAIN GFIPNVYSGP  60
TIQDIETALS VTTGTVQPQE LSNARLSLLE RGLSKVEHKY ILKIKSCGNG IMADDGYKWR  120
KYGQKSIKNS PNPRSYYRCT NPRCSAKKQV ERSSEEPDTL IITYEGLHLH FAYPFFDFNN  180
QAQXSSPSMK KPKKKTSVPQ AEDHDREAQE SLRSVTPDPV RDLPPGPFPG RHQGXVEEER  240
SSQGLLQDMV PFMIRNPKPS SWYNLSGSRS RMLFSPTLST PAQRELHQGI AALSLPPSQL  300
PAEAPATGEP KKEEKNVISG SYNWRNTLRH DSFPPSSTPL GNACVDGCVG ILRGYIAYNG  360
AGKQFLSKAY MSNLKSVLGI PRIRRLFSSQ GPGKKTLRKL LSEKQEGNSE RGXTEIXVQR  420
WSGEYSGTVF EAXSRFIAPL MFIGFIVTSL FLNPHQTKEV ITXLRETSLF GSLSRRIKIT  480
FIFQEFKNKL LEPGLVNHVE VANKSVAKVY MRSSACEKVH SDDSVRDTVN GSPSEGNVTQ  540
FKYYFNIGSV QSFEEKLEEA QEALGIDRHD FVPVIYVSQV MWSKELLRYG PTMLLLGALW  600
FMSRKMPSVG GPGGKSGRGI FNIGKAQVTK LDKNAKNKVL FKDVAGCDEA KQEIMEFVHF  660
LKHPKKYEEL GAKIPKGALL VGHPGTGKTL LAKATADESG VPFLSISGSD FMEMFVGVGT  720
SRVQSLFQEA RQCAPSIIFI DEIDAIGWAR GHGGFSGGHG ERESTLNQLL VELDGFGTTA  780
GVVGLAGTLL RPGQFDCQIT IDKPDIKGRN QIFQIYLSKL KLDLEPSFYS ERLAALTPGF  840
AGTDIANICN EAALIAARNE SPKITMKHFE AAIDRVIGGL EKKNKVISKL ERWTVAYHES  900
GHAVAGWFLE HAEPLLKVTI VRHGAAALGF AQYVPNENLL MTKEQLFDMN A
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6nyy_A1e-1356039483355AFG3-like protein 2
6nyy_B1e-1356039483355AFG3-like protein 2
6nyy_C1e-1356039483355AFG3-like protein 2
6nyy_D1e-1356039483355AFG3-like protein 2
6nyy_E1e-1356039483355AFG3-like protein 2
6nyy_F1e-1356039483355AFG3-like protein 2
Search in ModeBase
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Mdo.103110.0bud| leaf| stem
Functional Description ? help Back to Top
Source Description
UniProtProbable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V of the mitochondrial oxidative phosphorylation system. {ECO:0000269|Ref.9}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By high light. {ECO:0000269|PubMed:15266057}.
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_008369915.20.0ATP-dependent zinc metalloprotease FTSH 10, mitochondrial-like
SwissprotQ8VZI80.0FTSHA_ARATH; ATP-dependent zinc metalloprotease FTSH 10, mitochondrial
TrEMBLA0A498K4800.0A0A498K480_MALDO; Uncharacterized protein
STRINGXP_008369915.10.0(Malus domestica)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF71183449
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G43290.13e-47WRKY DNA-binding protein 49
Publications ? help Back to Top
  1. Sokolenko A, et al.
    The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts.
    Curr. Genet., 2002. 41(5): p. 291-310
    [PMID:12185496]
  2. Sakamoto W,Zaltsman A,Adam Z,Takahashi Y
    Coordinated regulation and complex formation of yellow variegated1 and yellow variegated2, chloroplastic FtsH metalloproteases involved in the repair cycle of photosystem II in Arabidopsis thylakoid membranes.
    Plant Cell, 2003. 15(12): p. 2843-55
    [PMID:14630971]
  3. Lister R, et al.
    A transcriptomic and proteomic characterization of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction.
    Plant Physiol., 2004. 134(2): p. 777-89
    [PMID:14730085]
  4. Yu F,Park S,Rodermel SR
    The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes.
    Plant J., 2004. 37(6): p. 864-76
    [PMID:14996218]
  5. Sinvany-Villalobo G, et al.
    Expression in multigene families. Analysis of chloroplast and mitochondrial proteases.
    Plant Physiol., 2004. 135(3): p. 1336-45
    [PMID:15266057]
  6. Peltier JB,Ytterberg AJ,Sun Q,van Wijk KJ
    New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy.
    J. Biol. Chem., 2004. 279(47): p. 49367-83
    [PMID:15322131]
  7. García-Lorenzo M,Sjödin A,Jansson S,Funk C
    Protease gene families in Populus and Arabidopsis.
    BMC Plant Biol., 2006. 6: p. 30
    [PMID:17181860]
  8. Piechota J,Kolodziejczak M,Juszczak I,Sakamoto W,Janska H
    Identification and characterization of high molecular weight complexes formed by matrix AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana.
    J. Biol. Chem., 2010. 285(17): p. 12512-21
    [PMID:20172857]
  9. Janska H,Piechota J,Kwasniak M
    ATP-dependent proteases in biogenesis and maintenance of plant mitochondria.
    Biochim. Biophys. Acta, 2010 Jun-Jul. 1797(6-7): p. 1071-5
    [PMID:20193658]
  10. Wagner R, et al.
    Fitness analyses of Arabidopsis thaliana mutants depleted of FtsH metalloproteases and characterization of three FtsH6 deletion mutants exposed to high light stress, senescence and chilling.
    New Phytol., 2011. 191(2): p. 449-58
    [PMID:21438879]
  11. Wagner R,Aigner H,Funk C
    FtsH proteases located in the plant chloroplast.
    Physiol Plant, 2012. 145(1): p. 203-14
    [PMID:22121866]
  12. Kolodziejczak M,Skibior-Blaszczyk R,Janska H
    m-AAA Complexes Are Not Crucial for the Survival of Arabidopsis Under Optimal Growth Conditions Despite Their Importance for Mitochondrial Translation.
    Plant Cell Physiol., 2018. 59(5): p. 1006-1016
    [PMID:29462458]