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 Peinf101Scf02809g00011.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia; Petunia integrifolia
Family CAMTA
Protein Properties Length: 876aa    MW: 98463.5 Da    PI: 8.539
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Peinf101Scf02809g00011.1genomeSGNView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-195.44.7e-3016114392
                      CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvgg........v 78 
                               +e k rwl+++ei+aiL n + +++  ++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LK +g        v
  Peinf101Scf02809g00011.1  16 EEaKMRWLRPNEIHAILCNSKYFNIFVKPVNLPTSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKTQGspatsvakV 100
                               45599**********************************************************************9777776665 PP

                      CG-1  79 evlycyYahseenp 92 
                                  + +Y++s+++p
  Peinf101Scf02809g00011.1 101 SPATPVYSNSSSDP 114
                               55666666666655 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143744.89911146IPR005559CG-1 DNA-binding domain
SMARTSM010769.0E-3514210IPR005559CG-1 DNA-binding domain
PfamPF038596.6E-251794IPR005559CG-1 DNA-binding domain
SuperFamilySSF812969.8E-11335422IPR014756Immunoglobulin E-set
CDDcd002044.05E-14520630No hitNo description
SuperFamilySSF484039.48E-16520634IPR020683Ankyrin repeat-containing domain
PfamPF127963.0E-6521600IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.203.4E-15521633IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.743538642IPR020683Ankyrin repeat-containing domain
SMARTSM002486.4E-6571600IPR002110Ankyrin repeat
PROSITE profilePS5008811.594571603IPR002110Ankyrin repeat
SuperFamilySSF525401.83E-5712784IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.181718744IPR000048IQ motif, EF-hand binding site
SMARTSM0001518733755IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.089734763IPR000048IQ motif, EF-hand binding site
PfamPF006120.24736754IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0026756778IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.688757781IPR000048IQ motif, EF-hand binding site
PfamPF006126.5E-4758778IPR000048IQ motif, EF-hand binding site
SMARTSM0001513835857IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.517837865IPR000048IQ 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: 876 aa     Download sequence    Send to blast
MFPVACADLD IPSIMEEAKM RWLRPNEIHA ILCNSKYFNI FVKPVNLPTS GTIVLFDRKM  60
LRNFRKDGHN WKKKKDGKTV KEAHEHLKTQ GSPATSVAKV SPATPVYSNS SSDPSDPSSW  120
VLSEECNSVD ERAYGASQHA QLEPNRDVTV KNHEQRLLEI NTLEWDELLA PGDPNKLIAT  180
QEGNVDSGGG RASVGQQNQC EVNGYSLNVS RANIQLASLD GSLSVSRVPI ASLESYVGQV  240
SGSETVNINP SNGMSFRSGD GQMTSNFHNN EPRVLPVGTG DSFDGLNKDG LQTQDSFGRW  300
MNYFISDSPG SADEMMTPES SVTIDQSYVM QQIFNITEIA PAWALSSEET KILVIGHFPG  360
GQSQLARSNL LCVCANVCFP AEFVQPGVYR CIIAPQSPGL VNLFLSFDGN TPISQVMTFE  420
FRAPSARKWT ASPEDQSNWD EFRVQMRLAH LLFSTSKSLS IFSSKVQQDS LRDAKRFVRK  480
CAHITDTWSY LIKSIEDKKL PIPHAKDCLF ELSLQTKFHE WLLERVVEGC KKLERDDQGQ  540
GVIHLCAILG YTWAVYPFSW SGLSLDYRDK GGWTALHWAA YYGREKMVAT LLSAGAKPNL  600
VTDPTSENPG GSTAADLASK NGFEGLGAYL AEKALVEHFK DMTLAGNVSG SLQTTTEPIN  660
PGNFTDEELY LKDTLAAYRN AADAAARIQA AFREHSFKVR TKVVESLNPE MEARNIVAAM  720
KIQHAFRNYE SRKKLAAAAR IQYRFRTWKM RKDFLNMRRQ AIKIQAVFRG FQVRRQYRKI  780
CWSVGVLEKA VLRWRLKRKG FRGLQVQSSP TVDIRPDSDV EEDFFRASRK QAEERVERSV  840
VRVQAMFRSK QAQEEYRRMK LEYNSATLEY ERVSQS
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}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieveRetrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_018628583.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A344X3900.0A0A344X390_NICTO; Calmodulin-binding transcription activator 5
STRINGXP_009609050.10.0(Nicotiana tomentosiformis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA45652232
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]