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 Prupe.1G122800.3.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Amygdaleae; Prunus
Family CAMTA
Protein Properties Length: 873aa    MW: 98149 Da    PI: 6.9774
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Prupe.1G122800.3.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1135.32.1e-421510033118
                CG-1  33 rpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywlLeeelekivlvhylevk 118
                         + + g+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+ ptf rrcywlL+++le+ivlvhy+e++
  Prupe.1G122800.3.p  15 TMQGGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDSPTFVRRCYWLLDKSLEHIVLVHYRETQ 100
                         5689*******************************************************************************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM010767.4E-461100IPR005559CG-1 DNA-binding domain
PROSITE profilePS5143760.9181105IPR005559CG-1 DNA-binding domain
PfamPF038599.8E-361798IPR005559CG-1 DNA-binding domain
SuperFamilySSF812961.26E-13324411IPR014756Immunoglobulin E-set
CDDcd002045.23E-14484618No hitNo description
Gene3DG3DSA:1.25.40.207.7E-17508621IPR020683Ankyrin repeat-containing domain
PfamPF127965.0E-7509588IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484034.51E-17521621IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.777526630IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.621559591IPR002110Ankyrin repeat
SMARTSM002489.2E-6559588IPR002110Ankyrin repeat
SMARTSM002481500598628IPR002110Ankyrin repeat
PROSITE profilePS500967.73707733IPR000048IQ motif, EF-hand binding site
SMARTSM0001526722744IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.053723752IPR000048IQ motif, EF-hand binding site
SMARTSM000150.022745767IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.164746770IPR000048IQ motif, EF-hand binding site
PfamPF006127.7E-4747767IPR000048IQ motif, EF-hand binding site
SMARTSM0001546825847IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.199826855IPR000048IQ 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: 873 aa     Download sequence    Send to blast
MEKQLGGSEI HGFHTMQGGT IVLFDRKMLR NFRKDGHNWK KKKDGKTVKE AHEHLKVGNE  60
ERIHVYYAHG EDSPTFVRRC YWLLDKSLEH IVLVHYRETQ ELQGSPVTPV NSNNSSSVSD  120
PSAPWLLSEE LDSGANTTFC AGENELSEPG DGLTVKNHEK RLHDINTLEW EELLITNDSK  180
GDIVSCYDQQ NQVVGNGFIS GGASVISAEM SAFGNLTNPT LRSDDVQFNL PDSPYVPTVE  240
YDVNSNVQIR DSIAKTTCDS LDVLVNDGLH SQDSFGRWIN QVMADPPGSV EDPALESSSI  300
AAQNSFASPS ADHLQSSIPH QIFNITDLSP AWAFSNEKTK ILITGFFHQE YLHLAKSDLL  360
CICGDVCLRA EIVQAGVYRC FVPPHLPRVV NLFMSIDGHK PISLVLNFEY RAPVLSDPII  420
SSEENNWEEF QAQMRLAYLL FSSSKSLNIV SNKVSLNALK EAKKFSHRTS HISNSWACLM  480
KAVEDKKSPL PLAKDGLFEL ILKNRLKDWL LEKVVDSSTT KEYDAYGQGV IHLCAILEYT  540
WAVRLFSWSG LSLDFRDRRG WTALHWAAYC GREKMVAVLL SAGAKPNLVT DPSSENPGGY  600
TAADLAAMKG YDGLAAYLSE KALVEQFKDM SIAGNASGSL QTSSNYGGNS ENLSEDEIHL  660
KDTLAAYRTA ADAAARIQAA FRENSLKLKA KAVQYSTPEA EARGIIAALK IQHAFRNYDT  720
RKKIKAAARI QYRFRTWKMR QEFLSLRRQA IKIQAAFRGF QVRRQYRKVL WSVGVLEKAV  780
LRWRLKRRGL RGLNVAPVEV DVDQKQESDT EEDFYRASRK QAEERIERSV VRVQAMFRSK  840
KAQEEYSRMK LTHIEAKLEF EELLDPDSNM DS*
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Expressed in roots, stems, leaves, pollen, top of sepals and siliques. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
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
PlantRegMapPrupe.1G122800.3.p
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_020409879.10.0calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A251QWH20.0A0A251QWH2_PRUPE; Uncharacterized protein
STRINGXP_008223308.10.0(Prunus mume)
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]