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.0060s0114.2.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: 925aa    MW: 104771 Da    PI: 6.6787
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0060s0114.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1157.92.1e-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+
  Kalax.0060s0114.2.p  28 EaKSRWLRPNEIHAILCNHVYFPIHVKPVNLPKSGEIHLFDRKKLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNA 117
                          559*************************************************************************************** PP

                 CG-1  93 tfqrrcywlLeeelekivlvhylev 117
                          tf rrcywlL++++e+ivlvhy+e+
  Kalax.0060s0114.2.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 profilePS5143773.41722148IPR005559CG-1 DNA-binding domain
SMARTSM010763.0E-7025143IPR005559CG-1 DNA-binding domain
PfamPF038591.7E-4428141IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.105.2E-6371460IPR013783Immunoglobulin-like fold
CDDcd006031.70E-4373460No hitNo description
PfamPF018333.6E-7373459IPR002909IPT domain
SuperFamilySSF812964.9E-15373460IPR014756Immunoglobulin E-set
CDDcd002041.46E-17532668No hitNo description
SuperFamilySSF484032.02E-17553669IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.202.3E-17555670IPR020683Ankyrin repeat-containing domain
PfamPF127963.8E-8559638IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.441576668IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.728609641IPR002110Ankyrin repeat
SMARTSM002483.5E-6609638IPR002110Ankyrin repeat
SuperFamilySSF525403.98E-7742823IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001538772794IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071773802IPR000048IQ motif, EF-hand binding site
PfamPF006120.06775793IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0017795817IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908796820IPR000048IQ motif, EF-hand binding site
PfamPF006123.6E-4799817IPR000048IQ motif, EF-hand binding site
SMARTSM000157877899IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.37879907IPR000048IQ motif, EF-hand binding site
PfamPF006120.084880899IPR000048IQ 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: 925 aa     Download sequence    Send to blast
MEPVLLDGFQ IHGFRTMNEL DLKSIFEEAK SRWLRPNEIH AILCNHVYFP IHVKPVNLPK  60
SGEIHLFDRK KLRNFRKDGH NWKKKNDGKT VKEAHEHLKV GNEERIHVYY AHGQDNATFV  120
RRCYWLLDKS MEHIVLVHYR ETCELLDSST APVNSNSSSG LTELHVPFLT YEETESGSQQ  180
SNTSNQLEYI ESIENVTAVT LERRLREINT LDWDELLVDT DPSVPIAYEE GKSGGFQQQN  240
PVMINVSKDD GSALLMNLPT ELSSGWHSAC PETRSDSING DILDGSYNHA VHSQLMMEAA  300
PNNSGTLFGG QSFSITQGGG GQDQDRRWMN SSLTVESPGS VNDSIHESSI SSAQNSMVPT  360
IMDQPQSADQ IFTITDISPE WAFSCEKTKI LLTGYFHQGF GNLLNSNLYC VCGSSCVPVE  420
IVQTGVMRCI LPPHSPGQFD LYLSTERLKP VSQLKTFEYR SSLQADQNIP SDNLSDWDEF  480
RNKMRLVRLL FSSSKTLNIL SAKVSEHTVN EAKKFSEKTS HTASSWALLK QSVDENKISL  540
HQAEEILFEQ AIRNRLQDWL LERIIEEQSP SDYDEKGLGV LHLCAILNYT WAVYLYSKSG  600
LSLDFRDKYG WTALHWAAYY GREDIVGALL SAGARPNLVT DPTPLIPGGC TASDLAAQKG  660
HNGLAAYLGE EALVDHFNDM ALAGNASGSI EFQRTCSVKR ETVYDEASCL KDTLAAYRTA  720
ADAAARINAA FREQSLKLRT EAVQGSNPED EARTIISAMR IQHAFRSFES RKKMAAALRI  780
QYGFRTWKTR RDFLNMRQQA IKIQAVFRGF QVRRHYRKII WSVGVLEKAV LRWRFKRRGF  840
RGLQVAPVQE ITSVAQEQEN DVEEDFFVLG RKQAEDRVES AVIKVQAMFR SKQAQQEYRR  900
MKWAHNQAKI EYEGFFNHNA KMES*
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]