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.0060s0114.3.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: 913aa    MW: 103320 Da    PI: 6.6538
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0060s0114.3.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1157.92e-49161304117
                 CG-1   4 e.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenp 92 
                          e k+rwl+++ei+aiL n+  + ++ ++ + pksg++ L++rkk+r+frkDG++wkkk dgktv+E+he+LKvg+ e +++yYah+++n+
  Kalax.0060s0114.3.p  16 EaKSRWLRPNEIHAILCNHVYFPIHVKPVNLPKSGEIHLFDRKKLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNA 105
                          559*************************************************************************************** PP

                 CG-1  93 tfqrrcywlLeeelekivlvhylev 117
                          tf rrcywlL++++e+ivlvhy+e+
  Kalax.0060s0114.3.p 106 TFVRRCYWLLDKSMEHIVLVHYRET 130
                          **********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143773.41710136IPR005559CG-1 DNA-binding domain
SMARTSM010763.0E-7013131IPR005559CG-1 DNA-binding domain
PfamPF038591.6E-4416129IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.105.1E-6359448IPR013783Immunoglobulin-like fold
CDDcd006031.68E-4361448No hitNo description
SuperFamilySSF812964.9E-15361448IPR014756Immunoglobulin E-set
PfamPF018333.6E-7361447IPR002909IPT domain
CDDcd002041.43E-17520656No hitNo description
SuperFamilySSF484032.02E-17541657IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.202.5E-17546658IPR020683Ankyrin repeat-containing domain
PfamPF127963.8E-8547626IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.441564656IPR020683Ankyrin repeat-containing domain
SMARTSM002483.5E-6597626IPR002110Ankyrin repeat
PROSITE profilePS5008811.728597629IPR002110Ankyrin repeat
SuperFamilySSF525404.25E-7736811IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001538760782IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071761790IPR000048IQ motif, EF-hand binding site
PfamPF006120.059763781IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0017783805IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908784808IPR000048IQ motif, EF-hand binding site
PfamPF006123.5E-4787805IPR000048IQ motif, EF-hand binding site
SMARTSM000157865887IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.37867895IPR000048IQ motif, EF-hand binding site
PfamPF006120.083868887IPR000048IQ 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: 913 aa     Download sequence    Send to blast
MLCDCAELDL KSIFEEAKSR WLRPNEIHAI LCNHVYFPIH VKPVNLPKSG EIHLFDRKKL  60
RNFRKDGHNW KKKNDGKTVK EAHEHLKVGN EERIHVYYAH GQDNATFVRR CYWLLDKSME  120
HIVLVHYRET CELLDSSTAP VNSNSSSGLT ELHVPFLTYE ETESGSQQSN TSNQLEYIES  180
IENVTAVTLE RRLREINTLD WDELLVDTDP SVPIAYEEGK SGGFQQQNPV MINVSKDDGS  240
ALLMNLPTEL SSGWHSACPE TRSDSINGDI LDGSYNHAVH SQLMMEAAPN NSGTLFGGQS  300
FSITQGGGGQ DQDRRWMNSS LTVESPGSVN DSIHESSISS AQNSMVPTIM DQPQSADQIF  360
TITDISPEWA FSCEKTKILL TGYFHQGFGN LLNSNLYCVC GSSCVPVEIV QTGVMRCILP  420
PHSPGQFDLY LSTERLKPVS QLKTFEYRSS LQADQNIPSD NLSDWDEFRN KMRLVRLLFS  480
SSKTLNILSA KVSEHTVNEA KKFSEKTSHT ASSWALLKQS VDENKISLHQ AEEILFEQAI  540
RNRLQDWLLE RIIEEQSPSD YDEKGLGVLH LCAILNYTWA VYLYSKSGLS LDFRDKYGWT  600
ALHWAAYYGR EDIVGALLSA GARPNLVTDP TPLIPGGCTA SDLAAQKGHN GLAAYLGEEA  660
LVDHFNDMAL AGNASGSIEF QRTCSVKRET VYDEASCLKD TLAAYRTAAD AAARINAAFR  720
EQSLKLRTEA VQGSNPEDEA RTIISAMRIQ HAFRSFESRK KMAAALRIQY GFRTWKTRRD  780
FLNMRQQAIK IQAVFRGFQV RRHYRKIIWS VGVLEKAVLR WRFKRRGFRG LQVAPVQEIT  840
SVAQEQENDV EEDFFVLGRK QAEDRVESAV IKVQAMFRSK QAQQEYRRMK WAHNQAKIEY  900
EGFFNHNAKM ES*
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
15772KKLRNFRKDGHNWKKK
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_002272118.20.0PREDICTED: calmodulin-binding transcription activator 6 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A1R3GK400.0A0A1R3GK40_9ROSI; IQ motif, EF-hand binding site
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]