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.1LG94
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: 908aa    MW: 103371 Da    PI: 7.1324
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Aradu.1LG94genomeNCGR_PGCView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1157.82.2e-49321493118
         CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpk.sgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrc 98 
                  +e ++rwl+++ei+aiL n + +++  ++ + p+ sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+++np f rrc
  Aradu.1LG94  32 EEaRTRWLRPNEIHAILCNSKYFTINVKPVNLPTcSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGQDNPGFVRRC 129
                  4559***********************9999997579************************************************************* PP

         CG-1  99 ywlLeeelekivlvhylevk 118
                  ywlL+++le+ivlvhy+e++
  Aradu.1LG94 130 YWLLDKSLEHIVLVHYRETQ 149
                  *****************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143770.74927154IPR005559CG-1 DNA-binding domain
SMARTSM010761.6E-7330149IPR005559CG-1 DNA-binding domain
PfamPF038591.0E-4333147IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.103.6E-5336450IPR013783Immunoglobulin-like fold
SuperFamilySSF812964.55E-16362448IPR014756Immunoglobulin E-set
PfamPF018334.3E-4363447IPR002909IPT domain
CDDcd002041.12E-14552656No hitNo description
PfamPF127962.3E-7552626IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484032.33E-18552659IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.207.1E-17555659IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.857564656IPR020683Ankyrin repeat-containing domain
SMARTSM002481.4E-5597626IPR002110Ankyrin repeat
PROSITE profilePS5008811.461597629IPR002110Ankyrin repeat
SMARTSM002482400636667IPR002110Ankyrin repeat
SuperFamilySSF525402.3E-6709811IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.943745771IPR000048IQ motif, EF-hand binding site
SMARTSM0001522760782IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.199761790IPR000048IQ motif, EF-hand binding site
PfamPF006120.25763781IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0022783805IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.407784808IPR000048IQ motif, EF-hand binding site
PfamPF006120.0059788805IPR000048IQ motif, EF-hand binding site
SMARTSM0001513859881IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.114861889IPR000048IQ 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: 908 aa     Download sequence    Send to blast
MMMANNFAGR LVGSEIHGFH TLQDLDLGNI MEEARTRWLR PNEIHAILCN SKYFTINVKP  60
VNLPTCSGTI VLFDRKMLRN FRKDGHNWKK KKDGKTVKEA HEHLKVGNEE RIHVYYAHGQ  120
DNPGFVRRCY WLLDKSLEHI VLVHYRETQE LQASPAAPIN SHSSSGSDPN APWILSEEID  180
SGIKTTNAGE INNNITVKNH EQRLHEINTL EWDDLVVAND PNTSTINGGG KVPHFDQQNQ  240
SNLSNVANNL SAEIPSFDNL TQPIAGSHTF PENLNLQTDN QMNPNEQINH NVLVNGVSLD  300
TLGNGGLQSQ DSFGMWVNHM LSDSPCSVDE SAVESSVSSI HESYSSLVGD DKQTSLPEQV  360
FNLTDVSPAW VPSTEKSKIL VTGFFHKDAD LSKSNLLCVC GDVSVPVECV QVGVYRCWVP  420
PHSPGFVNLY LSFDGHKPIS QVVNFEYRTP ILHDPVAFME NNDNWDKFQF EMRLSYLLFT  480
KKNSLDVFSC TVSPKRLKEA RNFAIRTSFI SNSWQYLMKS TQYNRIPYSQ AKEDLFGISL  540
RSRLKEWILE RIILGCKTTE YDAQGQSVIH LCAILDYTWA VSLFSWSGLS LDFRDKLGWT  600
ALHWAAYYGR EKMVATLLSA GAKPNLVTDP TPQNPGGQTA ADLAYMNGYD GLAAYLSEKA  660
LVRQFNDMSL AGNISGQLET NTTDPEDPEN LSEDQLYLKD TLAAYRTAAQ AAARIQAAFR  720
EHSLKLQTET IELLTPEAEA RKIVAAMKIQ HAFRNFESRK MMKAAARIQY TYRTWKIRRE  780
FLNMRHQAIK IQAAFRCFQL RKHYRKILWS VGVVEKALLR WRLKRKGLRG LHVNNADQKE  840
EGDGEEEFFR IGRKQAEERV ERSVVRVQAM FRSKKAQQDY RRMKLALNQA NLDREYEEFL  900
GTEDNMEI
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}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapAradu.1LG94
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
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_016197987.10.0calmodulin-binding transcription activator 5 isoform X4
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A445EM740.0A0A445EM74_ARAHY; Uncharacterized protein
STRINGGLYMA07G37090.20.0(Glycine max)
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]