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 XP_010524575.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Cleomaceae; Tarenaya
Family CAMTA
Protein Properties Length: 923aa    MW: 104090 Da    PI: 6.935
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_010524575.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1163.43.9e-51291462118
            CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfq 95 
                     l+e k rwl+++ei+a+L n++ + +  ++ + pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+nptf 
  XP_010524575.1  29 LEEaKGRWLRPNEIHAVLCNHKYFCINVKPMNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDNPTFV 123
                     455599***************************************************************************************** PP

            CG-1  96 rrcywlLeeelekivlvhylevk 118
                     rrcywlL+++le+ivlvhy+e++
  XP_010524575.1 124 RRCYWLLDKTLEHIVLVHYRETQ 146
                     ********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143779.40225151IPR005559CG-1 DNA-binding domain
SMARTSM010765.1E-7628146IPR005559CG-1 DNA-binding domain
PfamPF038593.2E-4631144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812961.68E-11369453IPR014756Immunoglobulin E-set
CDDcd002044.94E-16554664No hitNo description
Gene3DG3DSA:1.25.40.202.4E-17555667IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484032.95E-18556673IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.486563664IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.301605637IPR002110Ankyrin repeat
SMARTSM002482.0E-5605634IPR002110Ankyrin repeat
PfamPF136371.5E-5607652No hitNo description
SuperFamilySSF525403.19E-7714819IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.181753779IPR000048IQ motif, EF-hand binding site
SMARTSM00015230768790IPR000048IQ motif, EF-hand binding site
SMARTSM000150.002791813IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.871792816IPR000048IQ motif, EF-hand binding site
PfamPF006120.0015794813IPR000048IQ motif, EF-hand binding site
SMARTSM0001511869891IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.334870899IPR000048IQ 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: 923 aa     Download sequence    Send to blast
MDGAGSGRLV GSDIHGFHTL QDLDVPTMLE EAKGRWLRPN EIHAVLCNHK YFCINVKPMN  60
LPKSGTIVLF DRKMLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGNEERIH VYYAHGEDNP  120
TFVRRCYWLL DKTLEHIVLV HYRETQEVQT SPATPGNTSS ISDHSSPTCV AGDIDSGVGN  180
ARYVERNDPI AQNHEIRLHE INTLEWDELL VPNDDNSPPA PTVDDMSYLT QTLQNAANGS  240
AKNGNHLASY NASTDVQSFP CLGEPSYQNN NLCDPGRFSS QQVHCGVDPG LQNRDPSAAV  300
AGESVDALLN NGLQSQESFG RWMNAFISDS PGSVDDPSHE STLSPGQDSL TSPAAYHHQS  360
NMPEQIFSIT DVSPAWAFST EKTKILVTGF FHDGYQHQAR SNLFCICGET CVPAEIIQVG  420
VYRCFLPPQS PAIVNLYLSD DGQKPISQFF SFECRSAAVP EKSITQDNVS SRWEEFEFQV  480
RLAHLLFTSS NKVNILSSEV SAGSIQEAKK FVNKTSHLLN SWAYLVKSVQ GNQLSFEQAK  540
DNLFELTLKN RLKEWLLEKV LEGGKITEYD SKGLGVIHLC AILGYTWSIH LFSWSGLSLN  600
FRDKLGWTAL HWAAYYGREK MVAALLSAGA RPNLVTDPTK KNVDGCTAAD LAQQKGYDGL  660
AAYLSEKCLV AQFKDMKIAG NISGNLETCK AEASNPGTLT EEEQSLKDTL TAYRTAAEAA  720
SRIQVAFREH ALNVRSKAVQ FGSREEEAQS IIAAMKIQHA FRNHDTRKKM AAAVRIQYRF  780
HTWKMRREFL NMRRQVIKIQ AAFRGFQVRR QYRKIVWSVG VLEKAILRWR LKRKGFRGMQ  840
VSAITINEDE GETEEEDFYK TSQRQAEDRL ERSVVRVQAM FRSKKAQQDY RRMKLAHEEA  900
QLEYDGLQEL DDDDDDTSRA MER
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
PlantRegMapXP_010524575.1
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_010524575.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A178UWV10.0A0A178UWV1_ARATH; Uncharacterized protein
STRINGXP_010524574.10.0(Tarenaya hassleriana)
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]