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 Dca49164.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus
Family CAMTA
Protein Properties Length: 869aa    MW: 98734.8 Da    PI: 8.6355
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Dca49164.1genomeDCAView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1149.86.8e-47301373109
        CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcyw 100
                 +e k+rwl+++ei+aiL n++ +++  ++ + pk g++iL++rkk+r+frkDG++w+kkkdgktv+E+he+LKvg+ e +++yYah+e+nptf rrcyw
  Dca49164.1  30 NEaKSRWLRPNEIHAILSNYTYFTINVKPVNLPKGGKIILFDRKKIRNFRKDGHNWRKKKDGKTVKEAHEHLKVGTEERIHVYYAHGEDNPTFVRRCYW 128
                 5559*********************************************************************************************** PP

        CG-1 101 lLeeeleki 109
                 lL++  ++ 
  Dca49164.1 129 LLDKYVSRA 137
                 ***986665 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143764.87225155IPR005559CG-1 DNA-binding domain
SMARTSM010762.9E-6028160IPR005559CG-1 DNA-binding domain
PfamPF038591.8E-3931133IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.64E-10322408IPR014756Immunoglobulin E-set
CDDcd002049.58E-16505615No hitNo description
Gene3DG3DSA:1.25.40.208.4E-17505618IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484036.68E-17506619IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.486514615IPR020683Ankyrin repeat-containing domain
PfamPF127962.0E-6546619IPR020683Ankyrin repeat-containing domain
SMARTSM002484.2E-5556585IPR002110Ankyrin repeat
PROSITE profilePS5008811.514556588IPR002110Ankyrin repeat
SMARTSM002483200595626IPR002110Ankyrin repeat
SuperFamilySSF525403.19E-7662768IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001518717739IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.126718747IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0012740762IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.688741765IPR000048IQ motif, EF-hand binding site
PfamPF006122.7E-4742762IPR000048IQ motif, EF-hand binding site
SMARTSM000157.8821843IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.572823851IPR000048IQ 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: 869 aa     Download sequence    Send to blast
MENYSSGRLL ASDVHGFHTM EDLDIPTIMN EAKSRWLRPN EIHAILSNYT YFTINVKPVN  60
LPKGGKIILF DRKKIRNFRK DGHNWRKKKD GKTVKEAHEH LKVGTEERIH VYYAHGEDNP  120
TFVRRCYWLL DKYVSRAYCA CALPRYSRGS GDSVNVTNYQ MRLHEINTLD WDELLASNDP  180
IESLLTTKDS APTAQQYQQN AAYNLENNGN GIIINQSQAT ILAPRNDRDP VEGSNFAGIS  240
PLNDRLLSSV DNLIAQNGDP LQKGGLQSQD SFGRWISDII VDSPVSADDP SFESSGVSGH  300
GTFMSSAAVN HEGSVPLQIF CITDISQSWA SSVEDTKILV VGYFHQEYQH VAKSNIFCVC  360
GDICVSAEVV QVGVFRCLVP PQSPGLTNLY LSIDCCTPIS QVLTFEFRSP VYNNVTVKED  420
KAQWDMFRIQ TRLSHLLFST SKSLDILSSK VSPNALKEGK KFALKYSNIA DSWSYFNRLM  480
EDGRISFERA KDSLFELAMK SRLKEWLLER VIDGSKVAER DARGQGVLHL CAILDYTWAV  540
YPYSSCGMSL DFRDKFGWTA LHWAAYYGRE RMVAALLSAG AKANLVSDPT SENPGGCTPA  600
DLAYNQGYEG VAAYLSEKAL IQQFDDMKTA GNVSGFLGTP SEIKPSNISE DELYLKETLT  660
AYRTAADAAA RIQVAFRERS LKQRAKDVEG NNSEAEARYI VSALRIQHAY RNYESRKKMA  720
AAAHIQHRFR AWKLRREFLN MRRQAIKIQA VFRGFQVRKQ YRKICWSVGV LEKAILRWRL  780
KRKGLRGLEV QIKEPPIEDR SPESDNEEDF YRASRKQAEV RVEKAVVRVQ AMFRSRQAQQ  840
EYRRMKLAHA QAQQEFEETT IPYAYMDHI
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
17188RKKIRNFRKDGHNWRKKK
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
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_021730252.10.0calmodulin-binding transcription activator 5-like isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A0K9QKS60.0A0A0K9QKS6_SPIOL; Uncharacterized protein
STRINGXP_010671665.10.0(Beta vulgaris)
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]