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 Eucgr.H04783.1.p
Common NameEUGRSUZ_H04783, LOC104415786
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus
Family CAMTA
Protein Properties Length: 1048aa    MW: 117034 Da    PI: 5.4111
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Eucgr.H04783.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1179.15.5e-56201362118
              CG-1   2 lkekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptf 94 
                       l+ ++rwl++ ei++iL+n++k++++ e+++ p+sgsl+L++rk++ryfrkDG++w+kk+dgktv+E+he+LK g+++vl+cyYah+e+n++f
  Eucgr.H04783.1.p  20 LDAQHRWLRPAEICEILQNYKKFQIAPEPANMPPSGSLFLFDRKVLRYFRKDGHNWRKKRDGKTVKEAHERLKAGSIDVLHCYYAHGEHNENF 112
                       6779***************************************************************************************** PP

              CG-1  95 qrrcywlLeeelekivlvhylevk 118
                       qrr+yw+Leeel++ivlvhylevk
  Eucgr.H04783.1.p 113 QRRTYWMLEEELSHIVLVHYLEVK 136
                       *********************985 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143780.45515141IPR005559CG-1 DNA-binding domain
SMARTSM010761.7E-7718136IPR005559CG-1 DNA-binding domain
PfamPF038593.3E-4922135IPR005559CG-1 DNA-binding domain
PfamPF018332.2E-4464544IPR002909IPT domain
SuperFamilySSF812968.92E-16464550IPR014756Immunoglobulin E-set
Gene3DG3DSA:2.60.40.106.3E-4464539IPR013783Immunoglobulin-like fold
CDDcd002041.23E-13640755No hitNo description
Gene3DG3DSA:1.25.40.203.4E-17641758IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029717.873644757IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484039.17E-17644757IPR020683Ankyrin repeat-containing domain
PfamPF127968.2E-8668759IPR020683Ankyrin repeat-containing domain
PROSITE profilePS500889.671696728IPR002110Ankyrin repeat
SMARTSM002480.011696725IPR002110Ankyrin repeat
SMARTSM00248190735764IPR002110Ankyrin repeat
SuperFamilySSF525401.78E-7866921IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000150.13870892IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.48871900IPR000048IQ motif, EF-hand binding site
PfamPF006120.0042872891IPR000048IQ motif, EF-hand binding site
SMARTSM000150.36893915IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.956894918IPR000048IQ motif, EF-hand binding site
PfamPF006120.0011896913IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0009409Biological Processresponse to cold
GO:0010150Biological Processleaf senescence
GO:0042742Biological Processdefense response to bacterium
GO:0050832Biological Processdefense response to fungus
GO:0005634Cellular Componentnucleus
GO:0003677Molecular FunctionDNA binding
GO:0005516Molecular Functioncalmodulin binding
Sequence ? help Back to Top
Protein Sequence    Length: 1048 aa     Download sequence    Send to blast
MADARRYVLG NPLDIQQILL DAQHRWLRPA EICEILQNYK KFQIAPEPAN MPPSGSLFLF  60
DRKVLRYFRK DGHNWRKKRD GKTVKEAHER LKAGSIDVLH CYYAHGEHNE NFQRRTYWML  120
EEELSHIVLV HYLEVKGNRM NIHRIKDTEE TISLSHETEV NHETNSSLSS ISHQNNYQVP  180
SQTTDSSSPQ ASEYEDAESA YSNQANSGNH SIVDFQEAGM QNIDTGHSDP YYPASDSTDD  240
YQQNLSLKPG MDFLSLSRAD ITRECNVAGL ALEPQKNLDF SSWEPLLESC TSGGQSTLIQ  300
VLGSSAQPVT PDIMPKHAHD TVEQLFTDGI STKQEIGIQS QDQEELQVHL TNKIAESVST  360
ENGHHSNSFL DGNVALEVKA GCPSMGKQPF ANILAEEGLK KMDSFNRWMS KQLGDVNALL  420
GQSSTGAYWS AIVNDDGIDS SDSQEHDNNF MLTPSLSQEQ LFSIIDFSPS WTYADLEIKV  480
LITGRFLRSQ QDAELCKWSC MFGEVEVPAE VMADGVLRCH APVHKAGRVP FYVTCSNRVA  540
CSELREFEFR VNNSQDVISA DTKDGSINET LYMRFTKLLC SNTPRLSNSN IGENSQLRSK  600
ICSLLKDDDD AHWDHVMEST SDEFSTEGVR EQFFQKLLKE KLCEWLIEKA AEGGKGASVL  660
DEDGQGVLHF ASALGYDWAL QPTIIAGVSV NFRDANGWTA LHWAASFGRE RTVASLISLG  720
AAPGALTDPT PKYTTGRTPA DLASANGHKG IAGYLAESAL SAHLSLLNLD TAGGDASHGS  780
GGKAVQTISE RSPTPIREGD LPSGVSLKDS LAAVCNATQA AARIHQVFRV QSFQRKQLRE  840
FGDDNHGISD EHALTLVASK VYKPGQVDEP LHAAAVRIQN KFRGWKGRKE FLITRQRIVK  900
IQAHFRGHQV RKNRKNILWS VGIVEKVILR WRRKGSGLRG FKREELTDTS SMQDASSDED  960
EYDFLKEGRK QTEERLEKAL ARVKSMVQYP EARDQYRRLL NVVSEIQEAQ VEYEMTPDHN  1020
GEATDFDGDL TDLEQLLDDD TYMHLGP*
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator that binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3'. Binds calmodulin in a calcium-dependent manner in vitro (PubMed:12218065). Regulates transcriptional activity in response to calcium signals (Probable). Involved in freezing tolerance in association with CAMTA1 and CAMTA2 (PubMed:23581962). Required for the cold-induced expression of DREB1B/CBF1, DREB1C/CBF2, ZAT12 and GOLS3 (PubMed:19270186). Involved in response to cold. Contributes together with CAMTA5 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986). Involved together with CAMTA2 and CAMTA4 in the positive regulation of a general stress response (GSR) (PubMed:25039701). Involved in the regulation of GSR amplitude downstream of MEKK1 (PubMed:25157030). Involved in the regulation of a set of genes involved in defense responses against pathogens (PubMed:18298954). Involved in the regulation of both basal resistance and systemic acquired resistance (SAR) (PubMed:21900483). Acts as negative regulator of plant immunity (PubMed:19122675, PubMed:21900483, PubMed:22345509, PubMed:28407487). Binds to the promoter of the defense-related gene EDS1 and represses its expression (PubMed:19122675). Binds to the promoter of the defense-related gene NDR1 and represses its expression (PubMed:22345509). Involved in defense against insects (PubMed:23072934, PubMed:22371088). Required for tolerance to the generalist herbivore Trichoplusia ni, and contributes to the positive regulation of genes associated with glucosinolate metabolism (PubMed:23072934). Required for tolerance to Bradysia impatiens larvae. Mediates herbivore-induced wound response (PubMed:22371088). Required for wound-induced jasmonate accumulation (PubMed:23072934, PubMed:22371088). Involved in the regulation of ethylene-induced senescence by binding to the promoter of the senescence-inducer gene EIN3 and repressing its expression (PubMed:22345509). {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:18298954, ECO:0000269|PubMed:19122675, ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:21900483, ECO:0000269|PubMed:22345509, ECO:0000269|PubMed:22371088, ECO:0000269|PubMed:23072934, ECO:0000269|PubMed:23581962, ECO:0000269|PubMed:25039701, ECO:0000269|PubMed:25157030, ECO:0000269|PubMed:28351986, ECO:0000269|PubMed:28407487, ECO:0000305|PubMed:11925432}.
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00042PBMTransfer from AT2G22300Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMapEucgr.H04783.1.p
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, salt, wounding, ethylene and methyl jasmonate (PubMed:11162426, PubMed:12218065). Induced by infection with the fungal pathogen Golovinomyces cichoracearum (powdery mildew) and the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000 (PubMed:22345509). {ECO:0000269|PubMed:11162426, ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:22345509}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieveRetrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_010025463.10.0PREDICTED: calmodulin-binding transcription activator 3 isoform X1
SwissprotQ8GSA70.0CMTA3_ARATH; Calmodulin-binding transcription activator 3
TrEMBLA0A059B7C00.0A0A059B7C0_EUCGR; Uncharacterized protein
STRINGXP_010025463.10.0(Eucalyptus grandis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM86012535
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G22300.20.0signal responsive 1
Publications ? help Back to Top
  1. Zhang L,Du L,Shen C,Yang Y,Poovaiah BW
    Regulation of plant immunity through ubiquitin-mediated modulation of Ca(2+) -calmodulin-AtSR1/CAMTA3 signaling.
    Plant J., 2014. 78(2): p. 269-81
    [PMID:24528504]
  2. Benn G, et al.
    A key general stress response motif is regulated non-uniformly by CAMTA transcription factors.
    Plant J., 2014. 80(1): p. 82-92
    [PMID:25039701]
  3. Rahman H,Yang J,Xu YP,Munyampundu JP,Cai XZ
    Phylogeny of Plant CAMTAs and Role of AtCAMTAs in Nonhost Resistance to Xanthomonas oryzae pv. oryzae.
    Front Plant Sci, 2016. 7: p. 177
    [PMID:26973658]
  4. Benn G, et al.
    Plastidial metabolite MEcPP induces a transcriptionally centered stress-response hub via the transcription factor CAMTA3.
    Proc. Natl. Acad. Sci. U.S.A., 2016. 113(31): p. 8855-60
    [PMID:27432993]
  5. Kidokoro S, et al.
    Different Cold-Signaling Pathways Function in the Responses to Rapid and Gradual Decreases in Temperature.
    Plant Cell, 2017. 29(4): p. 760-774
    [PMID:28351986]
  6. Lolle S, et al.
    Matching NLR Immune Receptors to Autoimmunity in camta3 Mutants Using Antimorphic NLR Alleles.
    Cell Host Microbe, 2017. 21(4): p. 518-529.e4
    [PMID:28407487]
  7. Kim YS, et al.
    CAMTA-Mediated Regulation of Salicylic Acid Immunity Pathway Genes in Arabidopsis Exposed to Low Temperature and Pathogen Infection.
    Plant Cell, 2017. 29(10): p. 2465-2477
    [PMID:28982964]
  8. Jacob F, et al.
    A dominant-interfering camta3 mutation compromises primary transcriptional outputs mediated by both cell surface and intracellular immune receptors in Arabidopsis thaliana.
    New Phytol., 2018. 217(4): p. 1667-1680
    [PMID:29226970]