PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Kaladp0018s0264.4.p
Organism
Kalanchoe laxiflora
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: 912aa    MW: 103244 Da    PI: 6.5981
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kaladp0018s0264.4.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11581.8e-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+
  Kaladp0018s0264.4.p  16 EaKSRWLRPNEIHAILFNHMYFPIHVKPVNLPKSGEIHLFDRKKLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNA 105
                          559*************************************************************************************** PP

                 CG-1  93 tfqrrcywlLeeelekivlvhylev 117
                          tf rrcywlL++++e+ivlvhy+e+
  Kaladp0018s0264.4.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 profilePS5143772.25710136IPR005559CG-1 DNA-binding domain
SMARTSM010761.2E-7013131IPR005559CG-1 DNA-binding domain
PfamPF038592.0E-4416129IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.105.1E-6358447IPR013783Immunoglobulin-like fold
SuperFamilySSF812964.9E-15360447IPR014756Immunoglobulin E-set
CDDcd006031.68E-4360447No hitNo description
PfamPF018333.5E-7360446IPR002909IPT domain
CDDcd002041.35E-17519655No hitNo description
PfamPF127963.2E-8538625IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.55E-17540656IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.203.5E-17554658IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.52563655IPR020683Ankyrin repeat-containing domain
SMARTSM002483.5E-6596625IPR002110Ankyrin repeat
PROSITE profilePS5008811.728596628IPR002110Ankyrin repeat
SuperFamilySSF525402.58E-7718810IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.504744770IPR000048IQ motif, EF-hand binding site
SMARTSM0001538759781IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071760789IPR000048IQ motif, EF-hand binding site
PfamPF006120.062762780IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0017782804IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908783807IPR000048IQ motif, EF-hand binding site
PfamPF006123.5E-4786804IPR000048IQ motif, EF-hand binding site
SMARTSM000157864886IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.517866894IPR000048IQ motif, EF-hand binding site
PfamPF006120.083867886IPR000048IQ 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: 912 aa     Download sequence    Send to blast
MLCDYAELDL KSIFEEAKSR WLRPNEIHAI LFNHMYFPIH VKPVNLPKSG EIHLFDRKKL  60
RNFRKDGHNW KKKNDGKTVK EAHEHLKVGN EERIHVYYAH GQDNATFVRR CYWLLDKSME  120
HIVLVHYRET CELLDPSAAP VNSNSSSGLT ELHVPFLTYE ETESGSQQSN TSNQLEYIES  180
IENVTAVTLE RRLREINTLD WDELLVDTDP SVPIAYEEGK SGGVQQQNPV MINVSKDDGS  240
ALLMNLPTEL SSGWHSACPE TRSDSINGDI LDGSYNHAVH SQLMMEAAPN NSGTLFGGQS  300
FSITQGGGQD QDRRWMNSSL TVESPGSVND SIHESSISSA QNSMVPTIMD QPQSADQIFT  360
ITDISPEWAF SCEKTKILLT GYFHQGFGNL LNSNLYCVCG SSCVPVEIVQ TGVMRCILPP  420
HSPGQFDLYL STERLKPVSQ LKTFEYRSSL QADQNIPSDN LSEWDEFRNK MRLVRLLFSS  480
SKTLNILSAK VSEHTVNEAK KFSEKTSHTA SSWALLKQSV DENKISLHQA EEILFEQAIR  540
NRLQDWLLER IIEEQSPSDY DEQGLGVLHL CAILNYTWAV YLYSKSGLSL DFRDKYGWTA  600
LHWAAYYGRE DIVGALLSAG ARPNLVTDPT PLIPGGCTAS DLAAQKGHNG LAAYLGEEAL  660
VDHFNDMALA GNASGSIEFQ RTCSVKRETV YDEASCLKDT LAAYRTAADA AARINAAFRE  720
QSLKLRTEAV QGSNPEDEAR TIISAMKIQH AFRSFESRKK MAAALRIQYG FRTWKTRRDF  780
LNMRQQAIKI QAVFRGFQVR RHYRKIIWSV GVLEKAVLRW RFKRRGFRGL QVAPVQEITS  840
VAQEQENDVE EDFFVLGRKQ AEDRVESAVI KVQAMFRSKQ AQQEYRRMKL AHNQAKIEYE  900
GFFNHNAKME S*
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]