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 Cagra.0053s0009.2.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella
Family CAMTA
Protein Properties Length: 920aa    MW: 104340 Da    PI: 7.6107
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Cagra.0053s0009.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1162.57.7e-51301463118
                 CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseen 91 
                          +e  +rwl+++ei+a+L n++ +++  ++ + pksg+++L++rk++r+frkDG++wkkkkdgkt++E+he+LKvg+ e +++yYah+++n
  Cagra.0053s0009.2.p  30 DEaYTRWLRPNEIHALLCNHKFFTINVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHVYYAHGNDN 119
                          45589************************************************************************************* PP

                 CG-1  92 ptfqrrcywlLeeelekivlvhylevk 118
                          ptf rrcywlL++++e+ivlvhy+e++
  Cagra.0053s0009.2.p 120 PTFVRRCYWLLDKSQEHIVLVHYRETH 146
                          ************************985 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143776.40525151IPR005559CG-1 DNA-binding domain
SMARTSM010767.1E-7328146IPR005559CG-1 DNA-binding domain
PfamPF038595.3E-4532144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812964.2E-13370456IPR014756Immunoglobulin E-set
CDDcd002041.46E-13556666No hitNo description
Gene3DG3DSA:1.25.40.201.5E-15557669IPR020683Ankyrin repeat-containing domain
PfamPF127969.6E-7557636IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484032.02E-15565676IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.292574669IPR020683Ankyrin repeat-containing domain
SMARTSM002482.7E-6607636IPR002110Ankyrin repeat
PROSITE profilePS5008811.808607639IPR002110Ankyrin repeat
PROSITE profilePS500966.595756782IPR000048IQ motif, EF-hand binding site
SMARTSM00015260771793IPR000048IQ motif, EF-hand binding site
SMARTSM000152.5E-4794816IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.237795819IPR000048IQ motif, EF-hand binding site
PfamPF006123.2E-4797816IPR000048IQ motif, EF-hand binding site
SMARTSM000156.8870892IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.37871900IPR000048IQ motif, EF-hand binding site
PfamPF006120.22872892IPR000048IQ 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: 920 aa     Download sequence    Send to blast
MAGVDSGKLI GSEIHGFHTL QDLDIQTMLD EAYTRWLRPN EIHALLCNHK FFTINVKPVN  60
LPKSGTIVLF DRKMLRNFRK DGHNWKKKKD GKTIKEAHEH LKVGNEERIH VYYAHGNDNP  120
TFVRRCYWLL DKSQEHIVLV HYRETHEAQA APATPGNSYS SSISDHLSPK LVAEDINSVV  180
RNTCNTVRSN SLGARNHEIR LHEINTLDWD ELLVPADISN QSHPTEEDML YFTEQLETAP  240
RGSAKQGNHL AGYNGSVDIP SFPGLEDPVY QNNNSCGAGE FSSQHVHCGV ESILQRRNSN  300
ATVADQPGDA LLNNGYGSQD SFGRWVNNFI SDSPGSVDDP SLEAVYTPGQ ESSTTAVSHS  360
HSNAPEQVFN ITDVSPAWAY STEKTKILVT GFFHDSFQHF GRSNLFCICG ELRVPAEFLQ  420
LGVYRCFLPP QSPGVVNLYL SVDGNKPVSQ LFSFEHRSVP VIEKAIPQDD QLHKWEEFEF  480
QVRLAHLLFT SSNKISVLTS KISPDNLLEA KKLASRTSHL LNSWAYLMKS IQANEVPFDQ  540
ARDHLFELTL KNRLKEWLLE KVIENRNTKE YDSKGLGVIH LCAVLGYTWS ILLFSWANIS  600
LDFRDKHGWT ALHWAAYYGR EKMVAALLSA GARPNLVTDP TKEFLGGCTP ADLAQQKGYD  660
GLAAFLAEKC LVAQFKDMQV AGNISGNLET IKAEQSSNPG NANEEEQSLK DTLAAYRTAA  720
EAAARIQGAF REHELKVRSS AVRFASKEEE AKNIIAAMKI QHAFRNFETR RKIAAAARIQ  780
YRFQTWKMRR EFLNMRNKAI RIQAAFRGYQ VRRQYQKITW SVGVLEKAIL RWRLKRKGFR  840
GLQVSQPEKK EGDEEVEDFY KTSQKQAEDR LERSVVKVQA MFRSKKAQQD YRRMKLAHEE  900
AQLEYDGMQE LDQMAMEES*
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
PlantRegMapCagra.0053s0009.2.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 -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAY1282950.0AY128295.1 Arabidopsis thaliana AT4g16150/dl4115w mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_023635492.10.0calmodulin-binding transcription activator 5 isoform X3
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLR0GWD20.0R0GWD2_9BRAS; Uncharacterized protein
STRINGCagra.0053s0009.1.p0.0(Capsella grandiflora)
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]