PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Thecc1EG001108t2
Common NameTCM_001108
Organism
Theobroma cacao
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma
Family CAMTA
Protein Properties Length: 956aa    MW: 108076 Da    PI: 6.1891
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Thecc1EG001108t2genomeCGDView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11795.8e-56201362118
              CG-1   2 lkekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptf 94 
                       ++ ++rwl++ ei++iL++++k++++ e+++ p+sgsl+L++rk++ryfrkDG++w+kkkdgktv+E+he+LK g+++vl+cyYah+e+n++f
  Thecc1EG001108t2  20 MEAQHRWLRPAEICEILKDYKKFHIAPEPAHMPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHERLKAGSIDVLHCYYAHGEDNENF 112
                       5569***************************************************************************************** PP

              CG-1  95 qrrcywlLeeelekivlvhylevk 118
                       qrr+yw+Lee+l++ivlvhy+evk
  Thecc1EG001108t2 113 QRRSYWMLEEDLSHIVLVHYREVK 136
                       *********************986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143782.21515141IPR005559CG-1 DNA-binding domain
SMARTSM010766.9E-7718136IPR005559CG-1 DNA-binding domain
PfamPF038596.9E-4921134IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.103.8E-6503590IPR013783Immunoglobulin-like fold
SuperFamilySSF812961.01E-18504590IPR014756Immunoglobulin E-set
PfamPF018335.0E-7504589IPR002909IPT domain
PROSITE profilePS5029718.112685806IPR020683Ankyrin repeat-containing domain
CDDcd002042.21E-13685794No hitNo description
SuperFamilySSF484037.31E-17686796IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.6E-17691800IPR020683Ankyrin repeat-containing domain
PfamPF127965.2E-7707799IPR020683Ankyrin repeat-containing domain
SMARTSM002480.0046735764IPR002110Ankyrin repeat
PROSITE profilePS500889.912735767IPR002110Ankyrin repeat
SMARTSM00248490774803IPR002110Ankyrin repeat
PROSITE profilePS500968.956911939IPR000048IQ 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: 956 aa     Download sequence    Send to blast
MAETRRYGLS NQLDIEQILM EAQHRWLRPA EICEILKDYK KFHIAPEPAH MPPSGSLFLF  60
DRKVLRYFRK DGHNWRKKKD GKTVKEAHER LKAGSIDVLH CYYAHGEDNE NFQRRSYWML  120
EEDLSHIVLV HYREVKGNRT NFNRIKETEE AIPYSQDTEG ILPNSEMESS VSSSFHPNNG  180
QIPSKTTDTT SLNSVQASEY EDAESDYNHQ ASSQFNSFLE LQQPVVGRVD SGFSDPYVPL  240
SHSNDYHGKP SGTGFQLTQP DKSREYNDAG LTYEPQKNLD FTSWEDVLEN CTPGVESAQH  300
QPPFSSTQRD TMGQLFNNSF LTKQEFDNQA PVQEEWQASE GDSSHLSKWP LNQKLHPDLR  360
YDLTFRFHEQ EVNHHVHPDK QHDNSMQNNE QIEPSNGKHG YALKPDPESH LTLEGKSINS  420
SAMRQHLFDG SLVEEGLKKL DSFNRWMSKE LGDVDESHMQ SSSGAYWDAV EGQNGVDVST  480
IPSQGQLDTF LLGPSLSQDQ LFSIIDFSPN WAYVGSEIKV LITGRFLKSR DEAENCKWSC  540
MFGEVEVPAE VIADGVLRCH TPIHKAGRVP FYVTCSNRLA CSEVREFEYR VNHMETMDYP  600
RSNTNEILDM RFGRLLCLGP RSPYSITYNV ADVSQLSDEI NSLLKEDIKE WDQMLMHNSA  660
EEISPEKMKE QLLQKLLKEK LRVWLLQKVA EGGKGPNILD DGGQGVIHFA AALGYDWALE  720
PTIVAGVSVN FRDVNGWTAL HWAASYGRER TVASLISLGA APGALTDPTP KYPLGRTPAD  780
LASTNGHKGI SGYLAESDLS FHLRSLNLDN QGNNDTVDSR ADAIQKILER STAPLGCGDA  840
SDGPSLKDSL AAVRNATQAA ARIHQVFRVQ SFQKRQLKEY GDGKFGMSNE RALSLIAVKS  900
NKPGQHDEHV QAAAIRIQNK FRGWKGRKEF LIIRQRIRSC TIRFSAVQKQ FWMKT*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2cxk_A5e-13504590989calmodulin binding transcription activator 1
2cxk_B5e-13504590989calmodulin binding transcription activator 1
2cxk_C5e-13504590989calmodulin binding transcription activator 1
2cxk_D5e-13504590989calmodulin binding transcription activator 1
2cxk_E5e-13504590989calmodulin 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_007047945.20.0PREDICTED: calmodulin-binding transcription activator 3
SwissprotQ8GSA70.0CMTA3_ARATH; Calmodulin-binding transcription activator 3
TrEMBLA0A061DQ830.0A0A061DQ83_THECC; Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains, putative isoform 2
STRINGEOX921020.0(Theobroma cacao)
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. Motamayor JC, et al.
    The genome sequence of the most widely cultivated cacao type and its use to identify candidate genes regulating pod color.
    Genome Biol., 2013. 14(6): p. r53
    [PMID:23731509]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]