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.0391s0012.2.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: 917aa    MW: 103586 Da    PI: 6.94
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0391s0012.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11599.4e-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.0391s0012.2.p  26 LEEaKSRWLRPNEIHALLCNYKYFNIHAKPLNLPKSGTVVLYDRKMLRNFRRDGHNWKKKNDGKTIKEAHEHLKVGNEERIHVYYAHGHD 115
                          55669************************************************************************************* PP

                 CG-1  91 nptfqrrcywlLeeelekivlvhylevk 118
                          n tf rrcywlL+++le+ivlvhy+e++
  Kalax.0391s0012.2.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 profilePS5143773.3422148IPR005559CG-1 DNA-binding domain
SMARTSM010763.0E-6925143IPR005559CG-1 DNA-binding domain
PfamPF038594.9E-4428141IPR005559CG-1 DNA-binding domain
SuperFamilySSF812962.29E-14367454IPR014756Immunoglobulin E-set
SuperFamilySSF484035.91E-16548670IPR020683Ankyrin repeat-containing domain
CDDcd002042.02E-14552662No hitNo description
Gene3DG3DSA:1.25.40.201.2E-15557667IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.52561674IPR020683Ankyrin repeat-containing domain
PfamPF000231.1E-4603634IPR002110Ankyrin repeat
PROSITE profilePS5008811.06603635IPR002110Ankyrin repeat
SMARTSM002484.2E-5603632IPR002110Ankyrin repeat
SMARTSM00248370642673IPR002110Ankyrin repeat
SuperFamilySSF525402.31E-6764838IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001550766788IPR000048IQ motif, EF-hand binding site
SMARTSM000155.3E-4789811IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.676790814IPR000048IQ motif, EF-hand binding site
PfamPF006128.0E-5792811IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525402.31E-6869897IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000156.7869891IPR000048IQ motif, EF-hand binding site
PfamPF006120.12871891IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.895871899IPR000048IQ 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: 917 aa     Download sequence    Send to blast
MDAVLLAGSE IHGFHTMADL DVANMLEEAK SRWLRPNEIH ALLCNYKYFN IHAKPLNLPK  60
SGTVVLYDRK MLRNFRRDGH NWKKKNDGKT IKEAHEHLKV GNEERIHVYY AHGHDNLTFV  120
RRCYWLLDKS LEHIVLVHYR ETQEGAPDTP VNSNSSSGNS DISVHQLLSD GTDSGHVESH  180
YTGQNLYSEL GEIITEHIHE KTLHEINTLE WDELLVTNDP ANIIAPKEGT HTSSHSITSD  240
DNQEGFLLLN NISSEINPYL GYGSHNPGRG GANVKVLDEA SFLSISGQLN THLSGKNYVP  300
VNSSSLIPKE SLQNQDSFGR WMNDIIVDSP RSDENSMLEQ SLCPSHAPSG SFALRQSQSS  360
FPDQIFTITD ISPGWAFSTE NTKILLTGFF HKEYAHLAIS DITCVCGDAS VSVEVLQVGV  420
FRCFISPHKP GFVNIYLSLD GSKPISQVLT FEYRSSLSPT TLVSSEDTNK WMELRMKTRL  480
THLLYLKSKS LDILSSKLSQ NSVKEAKKFA LKTSHIANRW AYLIESLEDQ KMSFHEAQDD  540
LLELSLRNRL REWLLESIIQ GSKIAYLDDE GLGVIHMCAI LEYTWAVYLY SKSGLSLDFR  600
DKHGWTALHW AAFYGREKMT AALLSAGAKP NLVTDPTPEH PGGCTAADLA SKQGYEGVAA  660
YLAEKGLVEH FNDMSIAGNV SGSLQTYTPD PTEISTLNEE EQYLKESLAA YRTAADAAAR  720
IQTAMREHAL KVKAKAVEVA TPEAEARAIV AAMKIQHAFR NFETRKKIVA AGRIQQRFRT  780
WKIRKDFLQK RHKAIKIQAV FRGYQVRRQY RKILWSVGVL EKAILRWRLK RKGFRGLQLD  840
PDEALTKDGQ EPNGEEDFFE AGRKQAEERV ERSVIKVQAM FRSKQAQQEY QRMKLAHTQA  900
KLEYEEFVEP EMDTDS*
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]