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 Kalax.0391s0012.1.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Saxifragales; Crassulaceae; Kalanchoe
Family CAMTA
Protein Properties Length: 919aa    MW: 103827 Da    PI: 6.94
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0391s0012.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11599.5e-50261432118
                 CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahsee 90 
                          l+e k+rwl+++ei+a+L n++ +++++++ + pksg+++Ly+rk++r+fr+DG++wkkk dgkt++E+he+LKvg+ e +++yYah+++
  Kalax.0391s0012.1.p  26 LEEaKSRWLRPNEIHALLCNYKYFNIHAKPLNLPKSGTVVLYDRKMLRNFRRDGHNWKKKNDGKTIKEAHEHLKVGNEERIHVYYAHGHD 115
                          55669************************************************************************************* PP

                 CG-1  91 nptfqrrcywlLeeelekivlvhylevk 118
                          n tf rrcywlL+++le+ivlvhy+e++
  Kalax.0391s0012.1.p 116 NLTFVRRCYWLLDKSLEHIVLVHYRETQ 143
                          *************************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143772.92422148IPR005559CG-1 DNA-binding domain
SMARTSM010763.0E-6925143IPR005559CG-1 DNA-binding domain
PfamPF038594.9E-4428141IPR005559CG-1 DNA-binding domain
SuperFamilySSF812962.29E-14369456IPR014756Immunoglobulin E-set
SuperFamilySSF484035.91E-16550672IPR020683Ankyrin repeat-containing domain
CDDcd002042.03E-14554664No hitNo description
Gene3DG3DSA:1.25.40.201.2E-15559669IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.52563676IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.06605637IPR002110Ankyrin repeat
SMARTSM002484.2E-5605634IPR002110Ankyrin repeat
PfamPF000231.1E-4605636IPR002110Ankyrin repeat
SMARTSM00248370644675IPR002110Ankyrin repeat
SuperFamilySSF525402.31E-6766840IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001550768790IPR000048IQ motif, EF-hand binding site
SMARTSM000155.3E-4791813IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.676792816IPR000048IQ motif, EF-hand binding site
PfamPF006128.1E-5794813IPR000048IQ motif, EF-hand binding site
SMARTSM000156.7871893IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525402.31E-6871899IPR027417P-loop containing nucleoside triphosphate hydrolase
PfamPF006120.12873893IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.895873901IPR000048IQ 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: 919 aa     Download sequence    Send to blast
MDAVLLAGSE IHGFHTMADL DVANMLEEAK SRWLRPNEIH ALLCNYKYFN IHAKPLNLPK  60
SGTVVLYDRK MLRNFRRDGH NWKKKNDGKT IKEAHEHLKV GNEERIHVYY AHGHDNLTFV  120
RRCYWLLDKS LEHIVLVHYR ETQELQGAPD TPVNSNSSSG NSDISVHQLL SDGTDSGHVE  180
SHYTGQNLYS ELGEIITEHI HEKTLHEINT LEWDELLVTN DPANIIAPKE GTHTSSHSIT  240
SDDNQEGFLL LNNISSEINP YLGYGSHNPG RGGANVKVLD EASFLSISGQ LNTHLSGKNY  300
VPVNSSSLIP KESLQNQDSF GRWMNDIIVD SPRSDENSML EQSLCPSHAP SGSFALRQSQ  360
SSFPDQIFTI TDISPGWAFS TENTKILLTG FFHKEYAHLA ISDITCVCGD ASVSVEVLQV  420
GVFRCFISPH KPGFVNIYLS LDGSKPISQV LTFEYRSSLS PTTLVSSEDT NKWMELRMKT  480
RLTHLLYLKS KSLDILSSKL SQNSVKEAKK FALKTSHIAN RWAYLIESLE DQKMSFHEAQ  540
DDLLELSLRN RLREWLLESI IQGSKIAYLD DEGLGVIHMC AILEYTWAVY LYSKSGLSLD  600
FRDKHGWTAL HWAAFYGREK MTAALLSAGA KPNLVTDPTP EHPGGCTAAD LASKQGYEGV  660
AAYLAEKGLV EHFNDMSIAG NVSGSLQTYT PDPTEISTLN EEEQYLKESL AAYRTAADAA  720
ARIQTAMREH ALKVKAKAVE VATPEAEARA IVAAMKIQHA FRNFETRKKI VAAGRIQQRF  780
RTWKIRKDFL QKRHKAIKIQ AVFRGYQVRR QYRKILWSVG VLEKAILRWR LKRKGFRGLQ  840
LDPDEALTKD GQEPNGEEDF FEAGRKQAEE RVERSVIKVQ AMFRSKQAQQ EYQRMKLAHT  900
QAKLEYEEFV EPEMDTDS*
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}.
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
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_028075463.10.0calmodulin-binding transcription activator 5-like isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLD7SY490.0D7SY49_VITVI; Uncharacterized protein
STRINGVIT_05s0077g01240.t010.0(Vitis vinifera)
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]