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 SMil_00013498-RA_Salv
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salvia
Family CAMTA
Protein Properties Length: 948aa    MW: 107297 Da    PI: 7.1819
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
SMil_00013498-RA_SalvgenomeNDCTCMView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1165.21.1e-51621783118
                   CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahse 89 
                            +e ++rwl+++ei+aiL n++ + ++ ++ + pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e
  SMil_00013498-RA_Salv  62 EEaTSRWLRPNEIHAILSNHKYFPVHVKPMNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGE 149
                            45489*********************************************************************************** PP

                   CG-1  90 enptfqrrcywlLeeelekivlvhylevk 118
                            +n+tf rrcywlL+++le+ivlvhy+e++
  SMil_00013498-RA_Salv 150 DNSTFVRRCYWLLDKSLEHIVLVHYRETQ 178
                            **************************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.22657183IPR005559CG-1 DNA-binding domain
SMARTSM010769.1E-7460178IPR005559CG-1 DNA-binding domain
PfamPF038594.7E-4663176IPR005559CG-1 DNA-binding domain
SuperFamilySSF812964.06E-10400487IPR014756Immunoglobulin E-set
PfamPF127962.4E-8585665IPR020683Ankyrin repeat-containing domain
CDDcd002048.25E-18585695No hitNo description
SuperFamilySSF484031.71E-19589700IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029717.502591707IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.203.9E-19592698IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.007636668IPR002110Ankyrin repeat
SMARTSM002483.3E-5636665IPR002110Ankyrin repeat
SMARTSM002482200675705IPR002110Ankyrin repeat
SuperFamilySSF525406.11E-6749850IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.144784810IPR000048IQ motif, EF-hand binding site
SMARTSM0001525799821IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.998800826IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0069822844IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.542823847IPR000048IQ motif, EF-hand binding site
PfamPF006120.0047824844IPR000048IQ motif, EF-hand binding site
SMARTSM000154.6902924IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.95904932IPR000048IQ 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: 948 aa     Download sequence    Send to blast
LLILDSSVNL NHPIIWEFYN FWGRQVICQL QMEGNSVPSR LVGLEIHGFR TMEDLDFQNI  60
LEEATSRWLR PNEIHAILSN HKYFPVHVKP MNLPKSGTIV LFDRKMLRNF RKDGHNWKKK  120
KDGKTVKEAH EHLKVGNEER IHVYYAHGED NSTFVRRCYW LLDKSLEHIV LVHYRETQEN  180
SPATPVKSPF PTWTLPEGSE SAIDSMYYDG SMPVLERNDS VVIKTHEQRL HEINTLDWDE  240
LLVPIDPNKH NSPQEGKTAG FELPNQYHTN NYKISNDAQS TNKVSPESSD NSFSGQAAYS  300
VNYNIPNNSS YQTVGLETTF SSDTRTSGLV TLGGAGNGMH SVGADGSQSQ DSFGTTHVVA  360
GSPDSVDNQS LESSLLNSHQ SFSYNMKDNH HHPPLGQIFN VTDISPAWAL STEETKILVV  420
GFFSDGHQHY ADSKLYLACG DSVIPVEVVQ AGVFRCLISS QAPGLVNLFM TFDGHNPVSQ  480
VLTFEFRAPI QHNGLVSTEN TDNWEEFQLQ MRLARLLFSS SKDLSVYTAK PSQSALKEAK  540
VFAKKTSVIS LGWGYLCKMI EEAKMSFPQA KDRLFELTLE NRLQEWLLEK VATGCKITER  600
DEQGQGVIHL CAVLGYTWAV RLFSQSSLSL DYRDKCGWTA LHWAAYYGRE KMVATLLSVG  660
AKPNLVTDPT SQNPGGCTAA DLASLSGHEG LAAFLAEKAL VAQFKDMTLA GNVSGSLQTT  720
TNDMVDTGSF TEEEVYLKDT LAAYRTAADA AARIQAAFRE HALKVQTQAV EASSPETEAR  780
NIVAAMRIQH AFRNYETRKK IAAAARIQYR FRTWKIRKDF LNMRRQAIRI QANFRGFQVR  840
RQYRKICWSV GVLEKAILRW RLKRKGFRGL QVQPDETLPD QNQESDAEED FFKASRKQAE  900
ERVERSVVKV QAMFRSRRAQ EEYRRMKVEC SRATLEYEEL LHPDTQMG
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_011100790.10.0calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A4D9BHR30.0A0A4D9BHR3_SALSN; Uncharacterized protein
STRINGMigut.G00093.1.p0.0(Erythranthe guttata)
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]