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.1G122800.2.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: 871aa    MW: 97907.7 Da    PI: 6.9774
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Prupe.1G122800.2.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.1G122800.2.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
PROSITE profilePS5143761.1211105IPR005559CG-1 DNA-binding domain
SMARTSM010767.4E-461100IPR005559CG-1 DNA-binding domain
PfamPF038599.7E-361798IPR005559CG-1 DNA-binding domain
SuperFamilySSF812961.26E-13322409IPR014756Immunoglobulin E-set
CDDcd002045.21E-14482616No hitNo description
Gene3DG3DSA:1.25.40.207.7E-17506619IPR020683Ankyrin repeat-containing domain
PfamPF127964.9E-7507586IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484034.51E-17519619IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.777524628IPR020683Ankyrin repeat-containing domain
SMARTSM002489.2E-6557586IPR002110Ankyrin repeat
PROSITE profilePS5008811.621557589IPR002110Ankyrin repeat
SMARTSM002481500596626IPR002110Ankyrin repeat
PROSITE profilePS500967.73705731IPR000048IQ motif, EF-hand binding site
SMARTSM0001526720742IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.053721750IPR000048IQ motif, EF-hand binding site
SMARTSM000150.022743765IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.164744768IPR000048IQ motif, EF-hand binding site
PfamPF006127.7E-4745765IPR000048IQ motif, EF-hand binding site
SMARTSM0001546823845IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.199824853IPR000048IQ 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: 871 aa     Download sequence    Send to blast
MEKQLGGSEI HGFHTMQGGT IVLFDRKMLR NFRKDGHNWK KKKDGKTVKE AHEHLKVGNE  60
ERIHVYYAHG EDSPTFVRRC YWLLDKSLEH IVLVHYRETQ EGSPVTPVNS NNSSSVSDPS  120
APWLLSEELD SGANTTFCAG ENELSEPGDG LTVKNHEKRL HDINTLEWEE LLITNDSKGD  180
IVSCYDQQNQ VVGNGFISGG ASVISAEMSA FGNLTNPTLR SDDVQFNLPD SPYVPTVEYD  240
VNSNVQIRDS IAKTTCDSLD VLVNDGLHSQ DSFGRWINQV MADPPGSVED PALESSSIAA  300
QNSFASPSAD HLQSSIPHQI FNITDLSPAW AFSNEKTKIL ITGFFHQEYL HLAKSDLLCI  360
CGDVCLRAEI VQAGVYRCFV PPHLPRVVNL FMSIDGHKPI SLVLNFEYRA PVLSDPIISS  420
EENNWEEFQA QMRLAYLLFS SSKSLNIVSN KVSLNALKEA KKFSHRTSHI SNSWACLMKA  480
VEDKKSPLPL AKDGLFELIL KNRLKDWLLE KVVDSSTTKE YDAYGQGVIH LCAILEYTWA  540
VRLFSWSGLS LDFRDRRGWT ALHWAAYCGR EKMVAVLLSA GAKPNLVTDP SSENPGGYTA  600
ADLAAMKGYD GLAAYLSEKA LVEQFKDMSI AGNASGSLQT SSNYGGNSEN LSEDEIHLKD  660
TLAAYRTAAD AAARIQAAFR ENSLKLKAKA VQYSTPEAEA RGIIAALKIQ HAFRNYDTRK  720
KIKAAARIQY RFRTWKMRQE FLSLRRQAIK IQAAFRGFQV RRQYRKVLWS VGVLEKAVLR  780
WRLKRRGLRG LNVAPVEVDV DQKQESDTEE DFYRASRKQA EERIERSVVR VQAMFRSKKA  840
QEEYSRMKLT HIEAKLEFEE LLDPDSNMDS *
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.1G122800.2.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_020409880.10.0calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A251QZA20.0A0A251QZA2_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]