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 Aqcoe2G277000.2.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; stem eudicotyledons; Ranunculales; Ranunculaceae; Thalictroideae; Aquilegia
Family CAMTA
Protein Properties Length: 871aa    MW: 98497.6 Da    PI: 6.6474
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Aqcoe2G277000.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1131.72.6e-412110434117
               CG-1  34 pksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywlLeeelekivlvhylev 117
                         + g ++L++rkk+r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+np f rrcywlL++++e++vlvhy+e+
  Aqcoe2G277000.2.p  21 LEGGLIVLFDRKKLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDNPGFVRRCYWLLDKTYEHVVLVHYRET 104
                        567999****************************************************************************97 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM010764.2E-421105IPR005559CG-1 DNA-binding domain
PROSITE profilePS5143758.5881110IPR005559CG-1 DNA-binding domain
PfamPF038594.9E-3423103IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.101.4E-6320412IPR013783Immunoglobulin-like fold
SuperFamilySSF812962.76E-15325411IPR014756Immunoglobulin E-set
CDDcd002041.33E-15493618No hitNo description
PfamPF127962.7E-7506587IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.87E-17508625IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.201.4E-17516623IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029718.324517622IPR020683Ankyrin repeat-containing domain
SMARTSM002481.9E-5559588IPR002110Ankyrin repeat
PROSITE profilePS5008812.075559591IPR002110Ankyrin repeat
SMARTSM002481000598628IPR002110Ankyrin repeat
SMARTSM00015230669693IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.76707733IPR000048IQ motif, EF-hand binding site
SMARTSM0001570722744IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.577723752IPR000048IQ motif, EF-hand binding site
SMARTSM000150.074745767IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.444746770IPR000048IQ motif, EF-hand binding site
PfamPF006120.011747767IPR000048IQ motif, EF-hand binding site
SMARTSM000152.7826848IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.773827856IPR000048IQ motif, EF-hand binding site
PfamPF006120.13828848IPR000048IQ 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: 871 aa     Download sequence    Send to blast
MDNNSASVRV AGAEIHGFHT LEGGLIVLFD RKKLRNFRKD GHNWKKKKDG KTVKEAHEHL  60
KVGNEERIHV YYAHGEDNPG FVRRCYWLLD KTYEHVVLVH YRETSELQDS PVTPPNSSSA  120
SSYSDSSSRL VSEETDSGAD RAYYMDPETP FGGESTDRGE RMIVQNHEVR LHEINTLEWE  180
DLLVSNDPNN FNITSQDDIS FLQQQNHSEM YDSHNNSLQP IAESGSLGVG LPEDGHLLNK  240
GTNSGVQNQE FDMVTEHHDD SAHVVQDGFG TQDSFGRWMN GIVTDSPGSL NNLPVGSTIS  300
SGHESNTSTV LDPYQFLTQQ QIFSITDISP AWSFTAEETK VIVVGYFHPA HSHFAETNLF  360
CVFGDVCVPA EMIQVGVIRC RALPHNPGIV NFYLSFDGHT PISQVMTFEY RASILENGLS  420
PHEDNKWEEF QVQIRLSRLL FSTTNSLNML LSNISPNDLK EAKKFATATS SVDKDWAYLM  480
KSIGKNEISF PQAKNNLFEI ILKNKLQEWL LCRVVEGCQI TMRDRQGQGV LHLCAILGYT  540
WAVRPYSHSG LSLDFRDASG WTALHWAAFY GREKMVAILL SAGANPSLVS DPTSEFPGGC  600
NAADLASKNG YEGLAAYLAE KGLTEHFRLM SVCGNISGSL QSNSTDLVNP GNLSEEQLCQ  660
KDTLTAYRTA AEAASRIQSA FRENSFKLRK KAVEIATPET EARDIIAAMK IQHAFRNYDT  720
RKKIAAAGRI QYRFRTWKIR KDFLNMRRQA IKIQAAFRAL QVRKHYHKIL WSVGVLEKGI  780
LRWRQKRKGF RGLQVESTEV VDGEQKKESD VEDDFFRISR KQAEDRIERS VVRVQALFRS  840
FRAQQEYRRM KMAYDQVKLE ELLDTEVGFD *
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
13047RKKLRNFRKDGHNWKKKK
23146KKLRNFRKDGHNWKKK
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
PlantRegMap-Retrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_010259340.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2G5EZD70.0A0A2G5EZD7_AQUCA; Uncharacterized protein
STRINGAquca_003_00568.10.0(Aquilegia coerulea)
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]