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 678293760
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Lentibulariaceae; Utricularia
Family CAMTA
Protein Properties Length: 868aa    MW: 98792.9 Da    PI: 8.3769
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
678293760genomeUGSPView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1166.54.5e-52311473118
       CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywl 101
                +e ++rwl+++ei+aiL n++ +++  ++ t pksg+++L++rk++r+frkDGyswkkkkdgkt++E+he+LKvg+ e +++yYah+e+nptf rrcywl
  678293760  31 EEaRTRWLRPNEIHAILCNHKFFTINVKPVTLPKSGTILLFDRKMFRNFRKDGYSWKKKKDGKTIKEAHEHLKVGNEERIHVYYAHGENNPTFVRRCYWL 130
                4559************************************************************************************************ PP

       CG-1 102 Leeelekivlvhylevk 118
                Le++l++ivlvhy+e++
  678293760 131 LEKSLDHIVLVHYRETQ 147
                **************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143778.50226152IPR005559CG-1 DNA-binding domain
SMARTSM010763.8E-7629147IPR005559CG-1 DNA-binding domain
PfamPF038591.7E-4532145IPR005559CG-1 DNA-binding domain
SuperFamilySSF812966.3E-8320407IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.205.2E-16505619IPR020683Ankyrin repeat-containing domain
CDDcd002048.14E-16505615No hitNo description
SuperFamilySSF484031.16E-16506619IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.451514627IPR020683Ankyrin repeat-containing domain
PfamPF127963.1E-6529618IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008810.072556588IPR002110Ankyrin repeat
SMARTSM002481.1E-4556585IPR002110Ankyrin repeat
SMARTSM002483900595626IPR002110Ankyrin repeat
SuperFamilySSF525403.72E-6693770IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.687704730IPR000048IQ motif, EF-hand binding site
SMARTSM0001516719741IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.199720746IPR000048IQ motif, EF-hand binding site
SMARTSM000159.6E-4742764IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.676743767IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0005634Cellular Componentnucleus
GO:0003677Molecular FunctionDNA binding
GO:0005515Molecular Functionprotein binding
Sequence ? help Back to Top
Protein Sequence    Length: 868 aa     Download sequence    Send to blast
MEHNSGLIQL VGSEIHGFRS MADLDVRSIL EEARTRWLRP NEIHAILCNH KFFTINVKPV  60
TLPKSGTILL FDRKMFRNFR KDGYSWKKKK DGKTIKEAHE HLKVGNEERI HVYYAHGENN  120
PTFVRRCYWL LEKSLDHIVL VHYRETQESH GSPATPVNSY TNSGVSDPGS WNFSEEPDSA  180
EVQEHSERMI LEDHEQRLRE INTLEWDELL GTDVPQRLTP PQEGKTAGTE LPNAYQTANQ  240
GICEIAEGFH VKRGSITSGH LPSCRVEGLS TQDSFGRWIS NLIVDSPQSM DDRSPESSNE  300
SFNYPPGQNH DVSVLGQIFK ILDVSPAWAS ANEETKILVV VAVEEGHQLV RGLKLYLACG  360
SCIAPVEVVE AGVYRCILPP QSPGSKNLYL TVDGNKPISQ VLNFEYRGPV LSHAPALLED  420
EVDWAEYHLQ MRLARLLFSS SRAPSTYSNK TSETSLKEAR AFYRSTSSIS EGWLHLSRMI  480
EDARMSFAQA KTKLFELILQ SRLREWLLEK VVSGDKISER DEKGLGVIHL CTILGYAWAV  540
QPFSLSGLSM DYRDKFGWTA LHWAAFYGKE KMVAALLSAG AKPYLVTDPN SENPSGCTAS  600
DLASRNGYNG LAAYLAEKAL LAQLNDMTLA GNASDSVQTT ARSTIYFGNT SEEEMNMKES  660
LTAYRTAAEA ASRIQTAFRV RSLKIRTKQA ELHHPEMEAR NIVAALKIQH AYKNYEARKR  720
IAAAARIQHR FRTWKMRRDF LNMRRQAIRI QAHFRGYQVR KQYRKLVWSV GVLEKAILRW  780
RLKRKGFRGL QVQLDETIKD SYPTSDVEED FFKASRREAE DRVERSVARV QALIHSKEAQ  840
EEYRRVKREH TKATLECQEP QPPDHDII
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator (PubMed:14581622). Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:14581622, ECO:0000269|PubMed:28351986, ECO:0000305|PubMed:11925432}.
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00435DAPTransfer from AT4G16150Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMap678293760
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, wounding, abscisic acid, H(2)O(2) and salicylic acid. {ECO:0000269|PubMed:12218065}.
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_011100788.10.0calmodulin-binding transcription activator 5 isoform X1
RefseqXP_011100789.10.0calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A022RYH30.0A0A022RYH3_ERYGU; Uncharacterized protein
STRINGMigut.G00093.1.p0.0(Erythranthe guttata)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA45652232
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT4G16150.10.0calmodulin binding;transcription regulators
Publications ? help Back to Top
  1. Ye J, et al.
    Arabidopsis formin3 directs the formation of actin cables and polarized growth in pollen tubes.
    Plant Cell, 2009. 21(12): p. 3868-84
    [PMID:20023198]
  2. 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]
  3. Lan Y,Liu X,Fu Y,Huang S
    Arabidopsis class I formins control membrane-originated actin polymerization at pollen tube tips.
    PLoS Genet., 2018. 14(11): p. e1007789
    [PMID:30418966]