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.0401s0003.1.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: 918aa    MW: 102057 Da    PI: 6.2023
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0401s0003.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1149.21e-46131283117
                 CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseen 91 
                          +e + rwlk+ e++ i++n e  +l+++++++p+sg+++Lyn++++r+fr DG++w+kk+dg+tv E+he+LKv++ve+l+cyYa++een
  Kalax.0401s0003.1.p  13 REaEVRWLKPAEVYYIIQNCEDRHLQSKSAKKPPSGTFFLYNKRVLRNFRGDGHNWRKKRDGRTVGEAHERLKVDNVEALNCYYARGEEN 102
                          55589*****************999***************************************************************** PP

                 CG-1  92 ptfqrrcywlLeeelekivlvhylev 117
                          ++f+rr++w+L  e+++ivlv+yl+v
  Kalax.0401s0003.1.p 103 SSFRRRSFWMLSGERSHIVLVQYLDV 128
                          ***********************997 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143762.9488134IPR005559CG-1 DNA-binding domain
SMARTSM010761.8E-5211129IPR005559CG-1 DNA-binding domain
PfamPF038596.6E-4115128IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.108.0E-12366454IPR013783Immunoglobulin-like fold
PfamPF018331.4E-8368451IPR002909IPT domain
CDDcd001027.96E-5368452No hitNo description
SuperFamilySSF812961.54E-18368452IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.201.7E-15567662IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.318568660IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.87E-16572662IPR020683Ankyrin repeat-containing domain
CDDcd002043.94E-15573660No hitNo description
PfamPF127967.9E-8588661IPR020683Ankyrin repeat-containing domain
SMARTSM002480.0014601636IPR002110Ankyrin repeat
PROSITE profilePS500889.938601633IPR002110Ankyrin repeat
SMARTSM002482700640669IPR002110Ankyrin repeat
SuperFamilySSF525401.17E-7718823IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001511718740IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.529719748IPR000048IQ motif, EF-hand binding site
SMARTSM000150.12774796IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.608775804IPR000048IQ motif, EF-hand binding site
PfamPF006120.007777795IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0014797819IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.974799824IPR000048IQ motif, EF-hand binding site
PfamPF006127.3E-5800819IPR000048IQ 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: 918 aa     Download sequence    Send to blast
MQSAEFDINE LVREAEVRWL KPAEVYYIIQ NCEDRHLQSK SAKKPPSGTF FLYNKRVLRN  60
FRGDGHNWRK KRDGRTVGEA HERLKVDNVE ALNCYYARGE ENSSFRRRSF WMLSGERSHI  120
VLVQYLDVAN QSPGSVSQPS FLLSPPSSLS PGISSATNQE FVSVSGGYDS NINLPSPVSA  180
EIGFEVGISN NMVEVNQASG HLEKQLSLNY ENLNGINSLS SQEGMLNSSN FEGYGMEIAN  240
QVWLDSLLDG SDYAACDGGY AGLQNGFNSL LHEAGDSGMG RQQTSGRDED CVSWTDVANF  300
GEDEQISLEL HEMFPLNTDR FEGPPFSSFT SSQQRNLGYQ GKYFETDQTL IQPQANSNLF  360
IDQNQKFTIR DVSPEWGYSF ETTKVIIVGS FLCHPSEHVW TCMFGGIEVP IEIIQEGVIL  420
CEAPPNPSGK VTLCVTSGNR ETCSEVREFE YRNKTGICAQ CSASKKETTM SSEELLLLVR  480
LAQMLICDYS LGQRGGDSKE LGNGLSEKRN SDEDSWSLIL ESLLVGSGTF AGTIYWLLEE  540
FLKEKLVRWI SSKTQEPTGE STCLLSRKEQ GIIHMIAGLG YEWALAPILS SGVGINFRDI  600
NGWTALHWAA RFGREKMVAC LIASGALAGA LTDPNVQDPT GKTAASIAAI NGHKGLAGYL  660
SEVALTSHLS SLKLQESELS KELAVSEAEH TVNCIAEANM NTTEDQLSLN DTLTAVRNAA  720
SAAARIQAAF RAHSFRKRQQ EKAFKTISID DYGISSDVQV LSAVSKLAFR NTRDHNSAAL  780
SIQKKYRGYK GRKEFLDFRQ KVVKIQAHVR GHQTRKNYKV CWAAGILEKI ILRWLRKGVG  840
LRGFKPELET IDEIDEEDFA KVFRKKNVEA ALEEAVARVL SMVASPEARQ QYRRMLERYR  900
QAKAHLGNAA NERLQHL*
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator that 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 together with CAMTA2 and CAMTA3 in the positive regulation of a general stress response (PubMed:25039701). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:25039701, ECO:0000305|PubMed:11925432}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, salt, wounding, ethylene, methyl jasmonate, abscisic acid, H(2)O(2) and salicylic acid (PubMed:12218065). Induced by cold stress (PubMed:28351986). {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:28351986}.
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_022725126.10.0calmodulin-binding transcription activator 4-like isoform X3
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLD7TB030.0D7TB03_VITVI; Uncharacterized protein
STRINGVIT_01s0010g03850.t010.0(Vitis vinifera)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.10.0Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains
Publications ? help Back to Top
  1. Benn G, et al.
    A key general stress response motif is regulated non-uniformly by CAMTA transcription factors.
    Plant J., 2014. 80(1): p. 82-92
    [PMID:25039701]
  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]