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 Kaladp0018s0264.3.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: 924aa    MW: 104625 Da    PI: 6.6235
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kaladp0018s0264.3.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11581.9e-49281424117
                 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+
  Kaladp0018s0264.3.p  28 EaKSRWLRPNEIHAILFNHMYFPIHVKPVNLPKSGEIHLFDRKKLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNA 117
                          559*************************************************************************************** PP

                 CG-1  93 tfqrrcywlLeeelekivlvhylev 117
                          tf rrcywlL++++e+ivlvhy+e+
  Kaladp0018s0264.3.p 118 TFVRRCYWLLDKSMEHIVLVHYRET 142
                          **********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143772.25722148IPR005559CG-1 DNA-binding domain
SMARTSM010761.2E-7025143IPR005559CG-1 DNA-binding domain
PfamPF038592.1E-4428141IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.105.2E-6370459IPR013783Immunoglobulin-like fold
SuperFamilySSF812964.9E-15372459IPR014756Immunoglobulin E-set
CDDcd006031.70E-4372459No hitNo description
PfamPF018333.6E-7372458IPR002909IPT domain
CDDcd002041.38E-17531667No hitNo description
PfamPF127963.2E-8550637IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.71E-17552668IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.5E-17566669IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.52575667IPR020683Ankyrin repeat-containing domain
SMARTSM002483.5E-6608637IPR002110Ankyrin repeat
PROSITE profilePS5008811.728608640IPR002110Ankyrin repeat
SuperFamilySSF525402.66E-7730822IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.504756782IPR000048IQ motif, EF-hand binding site
SMARTSM0001538771793IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071772801IPR000048IQ motif, EF-hand binding site
PfamPF006120.063774792IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0017794816IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908795819IPR000048IQ motif, EF-hand binding site
PfamPF006123.6E-4798816IPR000048IQ motif, EF-hand binding site
SMARTSM000157876898IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.517878906IPR000048IQ motif, EF-hand binding site
PfamPF006120.084879898IPR000048IQ 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: 924 aa     Download sequence    Send to blast
MESVLLDGFQ IHGFRTMNEL DLKSIFEEAK SRWLRPNEIH AILFNHMYFP IHVKPVNLPK  60
SGEIHLFDRK KLRNFRKDGH NWKKKNDGKT VKEAHEHLKV GNEERIHVYY AHGQDNATFV  120
RRCYWLLDKS MEHIVLVHYR ETCELLDPSA APVNSNSSSG LTELHVPFLT YEETESGSQQ  180
SNTSNQLEYI ESIENVTAVT LERRLREINT LDWDELLVDT DPSVPIAYEE GKSGGVQQQN  240
PVMINVSKDD GSALLMNLPT ELSSGWHSAC PETRSDSING DILDGSYNHA VHSQLMMEAA  300
PNNSGTLFGG QSFSITQGGG QDQDRRWMNS SLTVESPGSV NDSIHESSIS SAQNSMVPTI  360
MDQPQSADQI FTITDISPEW AFSCEKTKIL LTGYFHQGFG NLLNSNLYCV CGSSCVPVEI  420
VQTGVMRCIL PPHSPGQFDL YLSTERLKPV SQLKTFEYRS SLQADQNIPS DNLSEWDEFR  480
NKMRLVRLLF SSSKTLNILS AKVSEHTVNE AKKFSEKTSH TASSWALLKQ SVDENKISLH  540
QAEEILFEQA IRNRLQDWLL ERIIEEQSPS DYDEQGLGVL HLCAILNYTW AVYLYSKSGL  600
SLDFRDKYGW TALHWAAYYG REDIVGALLS AGARPNLVTD PTPLIPGGCT ASDLAAQKGH  660
NGLAAYLGEE ALVDHFNDMA LAGNASGSIE FQRTCSVKRE TVYDEASCLK DTLAAYRTAA  720
DAAARINAAF REQSLKLRTE AVQGSNPEDE ARTIISAMKI QHAFRSFESR KKMAAALRIQ  780
YGFRTWKTRR DFLNMRQQAI KIQAVFRGFQ VRRHYRKIIW SVGVLEKAVL RWRFKRRGFR  840
GLQVAPVQEI TSVAQEQEND VEEDFFVLGR KQAEDRVESA VIKVQAMFRS KQAQQEYRRM  900
KLAHNQAKIE YEGFFNHNAK MES*
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
16984KKLRNFRKDGHNWKKK
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]