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 Achn048091
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; Ericales; Actinidiaceae; Actinidia
Family CAMTA
Protein Properties Length: 1075aa    MW: 120842 Da    PI: 6.1978
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Achn048091genomeIKGCView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1181.97.1e-57201362118
        CG-1   2 lkekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcyw 100
                 l+ ++rwl++ ei++iL nf+k++++ e++++p+sgsl+L++rk++ryfrkDG++w+kkkdgktv+E+he+LK g+++vl+cyYah+een++fqrr+yw
  Achn048091  20 LEAQHRWLRPAEICEILRNFKKFRIAPEPAHKPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHERLKAGSIDVLHCYYAHGEENENFQRRSYW 118
                 5679*********************************************************************************************** PP

        CG-1 101 lLeeelekivlvhylevk 118
                 lLeee+++ivlvhy+evk
  Achn048091 119 LLEEEHSHIVLVHYREVK 136
                 ***************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143781.215141IPR005559CG-1 DNA-binding domain
SMARTSM010766.2E-7718136IPR005559CG-1 DNA-binding domain
PfamPF038593.0E-4921134IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.104.3E-6486573IPR013783Immunoglobulin-like fold
SuperFamilySSF812961.68E-18487573IPR014756Immunoglobulin E-set
PfamPF018333.7E-6487572IPR002909IPT domain
PROSITE profilePS5029717.767673793IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.1E-18675785IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.87E-17675783IPR020683Ankyrin repeat-containing domain
CDDcd002042.16E-13688781No hitNo description
PfamPF127966.9E-9695784IPR020683Ankyrin repeat-containing domain
SMARTSM002480.018723752IPR002110Ankyrin repeat
SMARTSM00248220761790IPR002110Ankyrin repeat
SuperFamilySSF525403.19E-7894949IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001514898920IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.693900928IPR000048IQ motif, EF-hand binding site
PfamPF006120.036901919IPR000048IQ motif, EF-hand binding site
SMARTSM000150.01921943IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.725922946IPR000048IQ motif, EF-hand binding site
PfamPF006122.8E-4926943IPR000048IQ 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: 1075 aa     Download sequence    Send to blast
MAESRRYGLG TQLDIEQILL EAQHRWLRPA EICEILRNFK KFRIAPEPAH KPPSGSLFLF  60
DRKVLRYFRK DGHNWRKKKD GKTVKEAHER LKAGSIDVLH CYYAHGEENE NFQRRSYWLL  120
EEEHSHIVLV HYREVKGHRA NFNRIKEAEE AILNSQESEE IVSNSDVYSS VSSKFNPHNY  180
QVTSQTTDTS LNSTQASEYE DAESDDYLGK LPGISGMDFG SLSEGEKGKT SVNAALTYPS  240
EKHLDLPSWE DVLENSGTGI QSVPFQPSLS ANRSDIMSFN SGRGNEPRGQ FLIEGFSTKQ  300
EVVSYPHQQD KWQISEDDSL HISKWSMDQK LHKDSSYHLT TGLHGRGHNV DLLYLVGPQH  360
EHPSDQNKHY TQTDFQMHLT YGEGGSAMKS ELDSNLTVEE KAEPSPLKQP LLDGLLKEGL  420
KKLDSFDRWM TKELGDVNES HLQSSSGTYW ETVEAEDGVD DSSIASQAHL GAYMLGPSLS  480
QDQLFSIIDF SPNWAYAGSE IKVLITGKFL NSQQDLEKCK WSCMFGEVEV PAEIIADGVL  540
RCHTPLHNAG RVPFYVTCSN RLACSEVREF EYRVNNFQDA DILDTSYGRT NEILLRMRFG  600
KFLSLESASP PSCVSSPSGE NSHLSSKISL LLKEDSNEWE QMLMLTSEDD FSPEKIKEQL  660
LQKLLKEKLH VWLLQKVAEG GKGPSVLDED GQGVLHFAAA LGYDWAILPT LAAGVSINFR  720
DVNGWTALHW AASCGRERTV GFLISLDAAP GALTDPTPIH PGQTPADLAA SNGHKGIAGY  780
LAESSLSSHL SSLQLKDTKE SGSGETSGMK VVQTVSERTA TPIMDADLAH GLSLKDSLAA  840
VCNATQAAAR IHQVFRVQSF QRKQIKEYGD DKFGMSEERA LALVAVKSKS RLGHREEPVQ  900
AAAIRIQNKF RSWKGRKEFL TIRQQIVKIQ AHVRGHQVRK NYRKIIWSVG IVEKVILRWR  960
RKGSGLRGFK QEAFTQASSK NTSSKEDDYD FLKEGRKQTE ERLEKALARV KSMVQYPEAR  1020
DQYRRLLNVV TEMQETKAVY DKVLNSTEEA SDFDDDLIDL EALLDDDTFM HTVS*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2cxk_A1e-13487573989calmodulin binding transcription activator 1
2cxk_B1e-13487573989calmodulin binding transcription activator 1
2cxk_C1e-13487573989calmodulin binding transcription activator 1
2cxk_D1e-13487573989calmodulin binding transcription activator 1
2cxk_E1e-13487573989calmodulin binding transcription activator 1
Search in ModeBase
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
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_028069892.10.0LOW QUALITY PROTEIN: calmodulin-binding transcription activator 3-like
SwissprotQ8GSA70.0CMTA3_ARATH; Calmodulin-binding transcription activator 3
TrEMBLA0A2R6RJG10.0A0A2R6RJG1_ACTCH; Calmodulin-binding transcription activator 3 like
STRINGVIT_07s0141g00250.t010.0(Vitis vinifera)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA22302146
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]