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 PK20811.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Cannabaceae; Cannabis
Family CAMTA
Protein Properties Length: 915aa    MW: 103158 Da    PI: 7.1514
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
PK20811.1genomeCCBRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1163.15e-51291434118
       CG-1   4 ekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywlLe 103
                  +rwl+++ei+a+L n++ ++++ ++ + pk g+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+++ ptf rrcywlL+
  PK20811.1  29 APSRWLRPNEIYAMLSNYKYFTIHVKPMNLPKGGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEEKIHVYYAHGQDSPTFVRRCYWLLN 128
                479************************************************************************************************* PP

       CG-1 104 eelekivlvhylevk 118
                ++le+ivlvhy+e++
  PK20811.1 129 KSLEHIVLVHYRETQ 143
                ************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143774.40422148IPR005559CG-1 DNA-binding domain
SMARTSM010761.2E-6925143IPR005559CG-1 DNA-binding domain
PfamPF038591.5E-4429141IPR005559CG-1 DNA-binding domain
SuperFamilySSF812961.68E-15369456IPR014756Immunoglobulin E-set
PfamPF018331.4E-6370455IPR002909IPT domain
PfamPF127968.7E-8556634IPR020683Ankyrin repeat-containing domain
CDDcd002041.46E-16560664No hitNo description
SuperFamilySSF484032.33E-18563667IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.2E-17563668IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029717.263572676IPR020683Ankyrin repeat-containing domain
SMARTSM002482.3E-6605634IPR002110Ankyrin repeat
PROSITE profilePS5008812.048605637IPR002110Ankyrin repeat
SMARTSM002483700644674IPR002110Ankyrin repeat
SuperFamilySSF525401.83E-9692819IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.053753779IPR000048IQ motif, EF-hand binding site
SMARTSM0001533768790IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.364769798IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0087791813IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.761792816IPR000048IQ motif, EF-hand binding site
PfamPF006120.0023794813IPR000048IQ 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: 915 aa     Download sequence    Send to blast
MEGGQLVDSN IHGFHTLQDL DVPTIMAEAP SRWLRPNEIY AMLSNYKYFT IHVKPMNLPK  60
GGTIVLFDRK MLRNFRKDGH NWKKKKDGKT VKEAHEHLKV GNEEKIHVYY AHGQDSPTFV  120
RRCYWLLNKS LEHIVLVHYR ETQESQGSPI TPLHTPVYSH SSSSPDPHAR ILSDELDSGT  180
KNAHYDAGEE HLESGNTSTD KIYEQSLHDI NTLEWDELLD PNDPINSALG AHTVSCFNQQ  240
NQGVGNGFSS GGAMHSSFDH STNPNAMSGN MPGDLQNSVY VQNMGAQMNS DFQKRDSVGV  300
VTGESDLLAN NGLQSQDSFG RWIDGILIES PGSVIDPLLE TSILPAQDSF VSPATGHNLQ  360
SSVQEHMFNI TDVSPEWAYS NEKTKILVTG FFHEQYQQFA KYNLLCVCGD VCVPAEFIQI  420
GVYRCLVPPH SPGFVNLFLS VDGHKPISQI VNLEYRAPVI SEPVTTLDVK NNWDKFRLQM  480
RLAHLLFSSS KCLNILSSKV SPITLKEAKK FVEKIPNFPK AWDKFINSTG DGKTLFPQAQ  540
DKLFNLILRD RLKDWLVEKV IEGSKPTEFD VHGQSIIHLC AILGYSWAIH LFSMAGLSLD  600
FRDKHGWTAL HWAAYNGNDK MVAVLLTLGA KPNLVTDPTS ANPDGCTAGD LALLMGHEGL  660
AGYLSEKALV EQFKDMTIAG NASGTLDTNA NDTVYPETLS EEQVYLKDTL AAYRNAADAA  720
ARIQVAFREH SLKVRTKAVE GSSPEEEARS IIAAMKIQHA FRNFETRKKI QAAARIQYRF  780
RSWKIRRDFL NLRRQTIKIQ AAFRGFQVRR QYRKILWSVG VLEKLVLRWR LKRKGFRGLQ  840
VPPVEEQGRE SDTEEDFYKA SQKQAGERVG RSMVQVKNMF ASTKAQEEYH RMKVAHNQVK  900
LEYEDLFDPD SDITS
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}.
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00435DAPTransfer from AT4G16150Download
Motif logo
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}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_024019984.10.0calmodulin-binding transcription activator 5
RefseqXP_024019986.10.0calmodulin-binding transcription activator 5
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2P5F6180.0A0A2P5F618_TREOI; Notch
STRINGXP_008223308.10.0(Prunus mume)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF42883459
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]