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 NNU_009076-RA
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; stem eudicotyledons; Proteales; Nelumbonaceae; Nelumbo
Family CAMTA
Protein Properties Length: 929aa    MW: 105300 Da    PI: 7.5812
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
NNU_009076-RAgenomeCASView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1165.31e-51291452117
           CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqr 96 
                    ++e ++rwl+++ei+aiL n++ +++  ++ + p+sg++iL++rk++r+frkDG++wkkkkdgktv+E+he+LKvg  e +++yYah+e+np+f r
  NNU_009076-RA  29 MEEaRTRWLRPNEIHAILCNHTYFTVNVKPINLPQSGTIILFDRKVLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGDEERIHVYYAHGEDNPNFVR 124
                    45669******************************************************************************************* PP

           CG-1  97 rcywlLeeelekivlvhylev 117
                    rcywlL++++e+ivlvhy+e+
  NNU_009076-RA 125 RCYWLLDKKQEHIVLVHYRET 145
                    ******************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143776.63725151IPR005559CG-1 DNA-binding domain
SMARTSM010765.1E-7528146IPR005559CG-1 DNA-binding domain
PfamPF038592.4E-4531144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812964.9E-13378464IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.201.1E-16560675IPR020683Ankyrin repeat-containing domain
CDDcd002041.28E-15562672No hitNo description
PfamPF127962.7E-6562642IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484039.79E-16567675IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.626568675IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.701613645IPR002110Ankyrin repeat
SMARTSM002486.0E-6613642IPR002110Ankyrin repeat
SMARTSM002483500652681IPR002110Ankyrin repeat
SMARTSM0001558757779IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.272761787IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.108777806IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0014799821IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.823800824IPR000048IQ motif, EF-hand binding site
PfamPF006123.6E-4801821IPR000048IQ motif, EF-hand binding site
SMARTSM0001513882904IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.334884912IPR000048IQ 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: 929 aa     Download sequence    Send to blast
MERSVPGRLA GSEIHGFRTM EDLDVPSMME EARTRWLRPN EIHAILCNHT YFTVNVKPIN  60
LPQSGTIILF DRKVLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGDEERIH VYYAHGEDNP  120
NFVRRCYWLL DKKQEHIVLV HYRETLEAQG SPVTPVNSNS SPENSGPFAS RVLSEENDSG  180
ANHGFYAGSG SPLVSESAEL DDHFSVLHEI NTLEWEDLLG AQDASNPSPP KRGEVAHLEQ  240
QNLYELRGSL HSQGSFLPTN SLPTTLSSFR HPTEQMAKSA SIDIRPPNSG YVQTAGVISN  300
NQWKDFEKTD ESLNASFGNS LLTQDSFGRW MNCIISDSPG SIDNVQLQSS ISTTHETTLS  360
EITDHHHHTS TQGQVFSITD VSPSWAFSTE ETKVIMVGFF HAEYSHIAES NLLCVIGDVC  420
VPVEMIQVGV FRCMASPNNT GFVDLYLSLD GRTPISQVLT FEYRSPLIDN QGASQEDKCK  480
WKEFQIQLRL ARLLFSTNNS LSILSSKVLP NALKEAKKFA LMTSAIEKDW AYLIKSIGNS  540
GIPFLQAKDI LFELTLKNKL QEWLLERVAE GSKTTIRDTR GQGVIHLCAI LGYTWAVYPY  600
SRSGLSLDFR DAYGWTALHW AAFYGREKMV AVLLSAGAKP NLVTDPTPEF PGGRTAADLA  660
SKNGYEGLSA YLAEKALIFQ FYEMKISGNA SGSLGTNTTT YTSPEALNED ELCLKDTLAA  720
YRTAADAAAH IQAAFRQHSL KLKEKAVQLA NPEMEARNII AAMKIQHAFR NYETRKKMTA  780
AARIQYRFRT WKIRKDFLNM RRQAIKIQAV FRGYQVRRQY RKILWSVGVL EKVILRWRLK  840
RKGFRGLSVE LEPTQEMPVD QNQESDVEDD FFRVSRKQAE ERVERSVVRV QAMFRSKQAQ  900
QEYRRMKLAY DQAALEYEDL LDPEVRNQK
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_010259339.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A1U8A3G40.0A0A1U8A3G4_NELNU; calmodulin-binding transcription activator 5 isoform X1
STRINGXP_010259339.10.0(Nelumbo nucifera)
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]