PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Aqcoe3G198200.1.p
Organism
Aquilegia coerulea
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: 1038aa    MW: 115987 Da    PI: 6.4545
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Aqcoe3G198200.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1170.91.9e-53111262116
               CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenp 92 
                        ++e ++rwlk+ e++ iL+++e+++lt+ ++++p+sgsl+L+n++++r+frkDG++w+kkk+g+tvrE he+LKvg+ve+l+cyYah+e+n+
  Aqcoe3G198200.1.p  11 VQEaQNRWLKPAEVLFILQHHENFQLTEVAPQKPPSGSLFLFNKRVTRFFRKDGHNWRKKKEGRTVREGHERLKVGNVEALNCYYAHGEQNS 102
                        66779*************************************************************************************** PP

               CG-1  93 tfqrrcywlLeeelekivlvhyle 116
                        +fqrr++w+L++++e+ivlvhy+e
  Aqcoe3G198200.1.p 103 NFQRRSFWMLDRAYEHIVLVHYRE 126
                        **********************98 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143776.267133IPR005559CG-1 DNA-binding domain
SMARTSM010763.3E-6910128IPR005559CG-1 DNA-binding domain
PfamPF038593.2E-4713126IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.103.9E-7452539IPR013783Immunoglobulin-like fold
PfamPF018334.2E-8455537IPR002909IPT domain
SuperFamilySSF812969.94E-18455538IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.201.4E-14647742IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.194648740IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484034.66E-15651742IPR020683Ankyrin repeat-containing domain
CDDcd002044.05E-9668740No hitNo description
PfamPF127966.0E-7668741IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.728681713IPR002110Ankyrin repeat
SMARTSM002483.5E-4681710IPR002110Ankyrin repeat
SuperFamilySSF525401.62E-8829906IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000150.065853875IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.821854881IPR000048IQ motif, EF-hand binding site
PfamPF006120.015856874IPR000048IQ motif, EF-hand binding site
SMARTSM000155.7E-4876898IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.121877901IPR000048IQ motif, EF-hand binding site
PfamPF006122.2E-4879898IPR000048IQ 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: 1038 aa     Download sequence    Send to blast
MNSRFDMNDL VQEAQNRWLK PAEVLFILQH HENFQLTEVA PQKPPSGSLF LFNKRVTRFF  60
RKDGHNWRKK KEGRTVREGH ERLKVGNVEA LNCYYAHGEQ NSNFQRRSFW MLDRAYEHIV  120
LVHYREITEG RNSAGLLHIS PDSSTFSTSF HTAENQGSIS VFSEPYQSSS FSPEFSSELL  180
IRSNGGNHMG EIGMAPEPSS AGNINQALGR FEQQLSMSSI KLPGTSPYSV GNERATISEV  240
QDFSERSNQN DLVPRQYKSD YREGHRCSGE SAGFSTESNS CMHLHNPGGH KSGFNKDPTW  300
DALLGQCSGS CHIAPKDEVF STLEQMEKQQ SFSENGNISA TLAEGQEIWT SQFLNPARPT  360
NNAVYKNNCH PTVPNDYQPQ LSEARQFLLS SDDILSPTTT SLLQDVEYSK VSAHPSGTTT  420
REAVSDCYFD DMNQLEVLFG ADSRLTLAQK QRFQIQEISP DWGYATEDTK VVIVGSFLCD  480
PLECTWSCMF GEVEVPMQII QNGVLCCQAP PHVPGKVTLC ITASNRESCS EIREFEYRSN  540
LSICTNCSFV QKDAIKDTEE VLLLVRFVQM LLRNAAVPKE KTVVDTLGIS KVDEDPWEQL  600
IDALLVGKES HLSTKDWLLQ ELLKDKLQHW LSSKYKEGDP SGCSLSKKEQ GIIHLVAGLD  660
FKWALNPILT CGINVNYRDI NGRTALHWAA RFGREKMVAA LIAAGASAGA VTDPTSQDPV  720
GKTPGSIAAA SGHKGLAGYL SEVALTSHLS SLKLEESDTS NGSPAEELER TVEGISKESI  780
TSTDDQLSLK DSLAAVRKST QAASRIQSFF RILSFKRRQQ REAAAACCHE YGITPDELAA  840
ASKLALSRFH DHMLDKAALS IQKKYRGWKG RQEFLALRQK IVMIQAHVRG YQVRKRYKVI  900
LWAVCILDKV VLRWCRKRVG LRRFQPDSAS VDEIEYEDIL KAFRKLKVDK SVDEALSQVL  960
SMVESPDARQ QYRRILRSYS RAKVADLFGN GSGVPSTSQA SDENVESLMD GLSEFDANNI  1020
EYLMDEGNLM DGLCQFP*
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator that 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 together with CAMTA2 and CAMTA3 in the positive regulation of a general stress response (PubMed:25039701). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:25039701, ECO:0000305|PubMed:11925432}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, salt, wounding, ethylene, methyl jasmonate, abscisic acid, H(2)O(2) and salicylic acid (PubMed:12218065). Induced by cold stress (PubMed:28351986). {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:28351986}.
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_010249049.10.0PREDICTED: calmodulin-binding transcription activator 4-like isoform X1
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A2G5CR640.0A0A2G5CR64_AQUCA; Uncharacterized protein
STRINGAquca_040_00102.10.0(Aquilegia coerulea)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.10.0Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains
Publications ? help Back to Top
  1. Benn G, et al.
    A key general stress response motif is regulated non-uniformly by CAMTA transcription factors.
    Plant J., 2014. 80(1): p. 82-92
    [PMID:25039701]
  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]