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 Kaladp0018s0264.1.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: 946aa    MW: 106941 Da    PI: 6.4064
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kaladp0018s0264.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11581.9e-49501644117
                 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+
  Kaladp0018s0264.1.p  50 EaKSRWLRPNEIHAILFNHMYFPIHVKPVNLPKSGEIHLFDRKKLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNA 139
                          559*************************************************************************************** PP

                 CG-1  93 tfqrrcywlLeeelekivlvhylev 117
                          tf rrcywlL++++e+ivlvhy+e+
  Kaladp0018s0264.1.p 140 TFVRRCYWLLDKSMEHIVLVHYRET 164
                          **********************986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143772.25744170IPR005559CG-1 DNA-binding domain
SMARTSM010761.2E-7047165IPR005559CG-1 DNA-binding domain
PfamPF038592.2E-4450163IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.105.4E-6392481IPR013783Immunoglobulin-like fold
SuperFamilySSF812965.07E-15394481IPR014756Immunoglobulin E-set
PfamPF018333.7E-7394480IPR002909IPT domain
CDDcd006031.75E-4394481No hitNo description
CDDcd002041.43E-17553689No hitNo description
PfamPF127963.3E-8572659IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.71E-17574690IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.6E-17588691IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.52597689IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.728630662IPR002110Ankyrin repeat
SMARTSM002483.5E-6630659IPR002110Ankyrin repeat
SuperFamilySSF525402.92E-7752844IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.504778804IPR000048IQ motif, EF-hand binding site
SMARTSM0001538793815IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071794823IPR000048IQ motif, EF-hand binding site
PfamPF006120.065796814IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0017816838IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908817841IPR000048IQ motif, EF-hand binding site
PfamPF006123.7E-4820838IPR000048IQ motif, EF-hand binding site
SMARTSM000157898920IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.517900928IPR000048IQ motif, EF-hand binding site
PfamPF006120.086901920IPR000048IQ 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: 946 aa     Download sequence    Send to blast
MCAFGVDQLF DFVGSEEIGG LVMESVLLDG FQIHGFRTMN ELDLKSIFEE AKSRWLRPNE  60
IHAILFNHMY FPIHVKPVNL PKSGEIHLFD RKKLRNFRKD GHNWKKKNDG KTVKEAHEHL  120
KVGNEERIHV YYAHGQDNAT FVRRCYWLLD KSMEHIVLVH YRETCELLDP SAAPVNSNSS  180
SGLTELHVPF LTYEETESGS QQSNTSNQLE YIESIENVTA VTLERRLREI NTLDWDELLV  240
DTDPSVPIAY EEGKSGGVQQ QNPVMINVSK DDGSALLMNL PTELSSGWHS ACPETRSDSI  300
NGDILDGSYN HAVHSQLMME AAPNNSGTLF GGQSFSITQG GGQDQDRRWM NSSLTVESPG  360
SVNDSIHESS ISSAQNSMVP TIMDQPQSAD QIFTITDISP EWAFSCEKTK ILLTGYFHQG  420
FGNLLNSNLY CVCGSSCVPV EIVQTGVMRC ILPPHSPGQF DLYLSTERLK PVSQLKTFEY  480
RSSLQADQNI PSDNLSEWDE FRNKMRLVRL LFSSSKTLNI LSAKVSEHTV NEAKKFSEKT  540
SHTASSWALL KQSVDENKIS LHQAEEILFE QAIRNRLQDW LLERIIEEQS PSDYDEQGLG  600
VLHLCAILNY TWAVYLYSKS GLSLDFRDKY GWTALHWAAY YGREDIVGAL LSAGARPNLV  660
TDPTPLIPGG CTASDLAAQK GHNGLAAYLG EEALVDHFND MALAGNASGS IEFQRTCSVK  720
RETVYDEASC LKDTLAAYRT AADAAARINA AFREQSLKLR TEAVQGSNPE DEARTIISAM  780
KIQHAFRSFE SRKKMAAALR IQYGFRTWKT RRDFLNMRQQ AIKIQAVFRG FQVRRHYRKI  840
IWSVGVLEKA VLRWRFKRRG FRGLQVAPVQ EITSVAQEQE NDVEEDFFVL GRKQAEDRVE  900
SAVIKVQAMF RSKQAQQEYR RMKLAHNQAK IEYEGFFNHN AKMES*
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
191106KKLRNFRKDGHNWKKK
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]