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.0401s0003.3.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: 901aa    MW: 100327 Da    PI: 6.2301
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0401s0003.3.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.0401s0003.3.p  13 REaEVRWLKPAEVYYIIQNCEDRHLQSKSAKKPPSGTFFLYNKRVLRNFRGDGHNWRKKRDGRTVGEAHERLKVDNVEALNCYYARGEEN 102
                          55589*****************999***************************************************************** PP

                 CG-1  92 ptfqrrcywlLeeelekivlvhylev 117
                          ++f+rr++w+L  e+++ivlv+yl+v
  Kalax.0401s0003.3.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
PfamPF038596.4E-4115128IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.107.8E-12349437IPR013783Immunoglobulin-like fold
CDDcd001027.78E-5351435No hitNo description
SuperFamilySSF812961.54E-18351435IPR014756Immunoglobulin E-set
PfamPF018331.4E-8351434IPR002909IPT domain
Gene3DG3DSA:1.25.40.201.7E-15550645IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.318551643IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.87E-16555645IPR020683Ankyrin repeat-containing domain
CDDcd002043.83E-15556643No hitNo description
PfamPF127967.7E-8571644IPR020683Ankyrin repeat-containing domain
PROSITE profilePS500889.938584616IPR002110Ankyrin repeat
SMARTSM002480.0014584619IPR002110Ankyrin repeat
SMARTSM002482700623652IPR002110Ankyrin repeat
SuperFamilySSF525401.27E-7701806IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001511701723IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.529702731IPR000048IQ motif, EF-hand binding site
SMARTSM000150.12757779IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.608758787IPR000048IQ motif, EF-hand binding site
PfamPF006120.0069760778IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0014780802IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.974782807IPR000048IQ motif, EF-hand binding site
PfamPF006127.2E-5783802IPR000048IQ 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: 901 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 SDYAACDGDS GMGRQQTSGR DEDCVSWTDV ANFGEDEQIS LELHEMFPLN  300
TDRFEGPPFS SFTSSQQRNL GYQGKYFETD QTLIQPQANS NLFIDQNQKF TIRDVSPEWG  360
YSFETTKVII VGSFLCHPSE HVWTCMFGGI EVPIEIIQEG VILCEAPPNP SGKVTLCVTS  420
GNRETCSEVR EFEYRNKTGI CAQCSASKKE TTMSSEELLL LVRLAQMLIC DYSLGQRGGD  480
SKELGNGLSE KRNSDEDSWS LILESLLVGS GTFAGTIYWL LEEFLKEKLV RWISSKTQEP  540
TGESTCLLSR KEQGIIHMIA GLGYEWALAP ILSSGVGINF RDINGWTALH WAARFGREKM  600
VACLIASGAL AGALTDPNVQ DPTGKTAASI AAINGHKGLA GYLSEVALTS HLSSLKLQES  660
ELSKELAVSE AEHTVNCIAE ANMNTTEDQL SLNDTLTAVR NAASAAARIQ AAFRAHSFRK  720
RQQEKAFKTI SIDDYGISSD VQVLSAVSKL AFRNTRDHNS AALSIQKKYR GYKGRKEFLD  780
FRQKVVKIQA HVRGHQTRKN YKVCWAAGIL EKIILRWLRK GVGLRGFKPE LETIDEIDEE  840
DFAKVFRKKN VEAALEEAVA RVLSMVASPE ARQQYRRMLE RYRQAKAHLG NAANERLQHL  900
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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]