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 Aradu.KT95M
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; Dalbergieae; Arachis
Family CAMTA
Protein Properties Length: 939aa    MW: 107379 Da    PI: 8.411
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Aradu.KT95MgenomeNCGR_PGCView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1161.61.5e-50611763118
         CG-1   3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcyw 100
                  + k+rwl+++ei+aiL n + ++++ ++ ++pksg++iL++rk++r+frkDGy+wkkk dgktv+E+he+LKvg+ e +++yYah+++np + rrcyw
  Aradu.KT95M  61 EAKSRWLRPNEIHAILSNSKYFTIHVKPVNKPKSGRIILFDRKMLRNFRKDGYNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNPGLVRRCYW 158
                  459*********************************************************************************************** PP

         CG-1 101 lLeeelekivlvhylevk 118
                  lL+++le+ivlvhy+e++
  Aradu.KT95M 159 LLDKRLEHIVLVHYRETQ 176
                  ***************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143773.78555181IPR005559CG-1 DNA-binding domain
SMARTSM010764.6E-7259176IPR005559CG-1 DNA-binding domain
PfamPF038595.6E-4561174IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.106.1E-6360474IPR013783Immunoglobulin-like fold
SuperFamilySSF812966.02E-15385472IPR014756Immunoglobulin E-set
PfamPF018333.2E-4385471IPR002909IPT domain
SuperFamilySSF484034.66E-19559683IPR020683Ankyrin repeat-containing domain
PfamPF127968.7E-7568650IPR020683Ankyrin repeat-containing domain
CDDcd002045.02E-15570680No hitNo description
Gene3DG3DSA:1.25.40.205.1E-17570684IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.433576653IPR020683Ankyrin repeat-containing domain
SMARTSM002482.9E-5621650IPR002110Ankyrin repeat
PROSITE profilePS5008810.98621653IPR002110Ankyrin repeat
SMARTSM002482400660691IPR002110Ankyrin repeat
SMARTSM0001533765787IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.961766795IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.559785812IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0038807829IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.054808832IPR000048IQ motif, EF-hand binding site
PfamPF006120.0017812829IPR000048IQ motif, EF-hand binding site
SMARTSM0001511887909IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.187889917IPR000048IQ 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: 939 aa     Download sequence    Send to blast
MFNDDGAATK LNGSTCGFRD TWLPHIASNN GIWFRKYWWL FIPIGVQNLL LYLDVENTME  60
EAKSRWLRPN EIHAILSNSK YFTIHVKPVN KPKSGRIILF DRKMLRNFRK DGYNWKKKND  120
GKTVKEAHEH LKVGNEERIH VYYAHGQDNP GLVRRCYWLL DKRLEHIVLV HYRETQESQV  180
SPVTPVNSHS SSASDQPWLS EELDSGTNTA YASGFNDNLT VESHEMKLHE LNTLEWDDLV  240
LSNDNTSTIV TSGNVQSFNQ QNQSFLKGSS GNVASNLVPE IHSFSKLAQP IVESNSVPYS  300
IPDSVDFQRT SPISLAGVDS SNTLVNPSLQ SQDSFGMWIN NMISDSPPCS VESALESSIS  360
SSVQGQYSSL VAGNQLSSLP EQVFTITDVS PTWASSTEKT KILVTGLFHN DYQHLAKSNL  420
YCVCSDASIP VETVQLGVYR CWVSPHSPGF VNLYLSFDGR KPISQVVNFE YRTPLLHDPT  480
AFMEQKYDWE EFRLQIRLTN LLFDTKKSLD IFSSKVSPKS LKEARKFAFK TSFISKSWQY  540
LMKSTEENTI PFPQAKDDLF QIALKNRLKE WLLERISLGV KTTEHDKQGQ GVIHLCAILG  600
YTWAVSLFSW SGLSLDFRDK FGWTALHWAA YYGREKMVGT LLSFGAKPNL VTDPTPQNPG  660
GCTAADLAYI KGYDGLAAYL SEKSLVEQVN DMNLAGNISG PLETTTVDIG NTENLTEDQL  720
YLKETLASYR TAAEAAARIQ SAFREHSLKL RSMKIESLSP EDQERQIVAA MKIQHAFRNY  780
ETRKTMAAAA RIQYRYRTFK LRREFLHMKR QVIRIQAAFR GFQARKQYRK IIWSVGVLEK  840
VILRWRLKRK GFRGLQVNHD QEMKDETQGS DIEEDFFRTS RKQAEERVER SVVRVQAMFR  900
SKKAQEEYRR MKLAHNQAQL ELEFEELLIC GDDMITEKQ
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
Cis-element ? help Back to Top
SourceLink
PlantRegMapAradu.KT95M
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_015959568.10.0calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A444WPP00.0A0A444WPP0_ARAHY; Uncharacterized protein
STRINGAES650410.0(Medicago truncatula)
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]