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_011100788.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Pedaliaceae; Sesamum
Family CAMTA
Protein Properties Length: 929aa    MW: 105167 Da    PI: 7.2512
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_011100788.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1165.96.6e-52301472118
            CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfq 95 
                     ++e k+rwl+++ei+aiL n++ +++  ++ + pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+nptf 
  XP_011100788.1  30 MEEaKARWLRPNEIHAILCNHKYFTVYVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDNPTFV 124
                     45669****************************************************************************************** PP

            CG-1  96 rrcywlLeeelekivlvhylevk 118
                     rrcywlL+++le+ivlvhy+e++
  XP_011100788.1 125 RRCYWLLDKSLEHIVLVHYRETQ 147
                     ********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.33326152IPR005559CG-1 DNA-binding domain
SMARTSM010763.5E-7729147IPR005559CG-1 DNA-binding domain
PfamPF038597.0E-4632145IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.22E-9382467IPR014756Immunoglobulin E-set
CDDcd002041.30E-13566676No hitNo description
SuperFamilySSF484033.42E-16567679IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.205.1E-15567679IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.345575649IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.434617649IPR002110Ankyrin repeat
SMARTSM002485.1E-6617646IPR002110Ankyrin repeat
PfamPF000239.2E-5618648IPR002110Ankyrin repeat
SuperFamilySSF525403.72E-8724831IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.163765791IPR000048IQ motif, EF-hand binding site
SMARTSM0001514780802IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.089784810IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0012803825IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.091804828IPR000048IQ motif, EF-hand binding site
PfamPF006120.001805825IPR000048IQ motif, EF-hand binding site
SMARTSM0001535883905IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.114885913IPR000048IQ 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: 929 aa     Download sequence    Send to blast
MENTGVRGRF VGSEIHGFRT LEDLDVGNMM EEAKARWLRP NEIHAILCNH KYFTVYVKPV  60
NLPKSGTIVL FDRKMLRNFR KDGHNWKKKK DGKTVKEAHE HLKVGNEERI HVYYAHGEDN  120
PTFVRRCYWL LDKSLEHIVL VHYRETQELQ GSPATPVNSN SNSAGSDLSA TWPMSEESDS  180
AVDRVYYGST GSYLECHDSV TVKHHEQRLY EINTLEWDEL LVPDDPHRLI TRQQGTTAGF  240
ELQNQYQMNS YRINDDAPSN NKVSPECSTN SFSEPVAGRS SINYTSPNNM SYQTVEQDTI  300
VNSETMVSGL MPSGGAGSLY NLGKDGLQSQ DSFGRWVTHI IAESPESVDD HTLESSNLAG  360
HQSSTYPLMD SHDSSPLGPI FTITDVSPAW ALSTEETKIL VVGFFNEGQL PYSESKLYLA  420
CGDSLLPVDV VQAGVFRCLI PPQAPKLGNL YITFDGHKPI SQVLTFEIRA PVQPGTVSFE  480
NKTDWEEFQL QMRLAHLLFS SSKGLSIYST KLSPTALKEA KAFAQKTSHI SDGWLHMAKV  540
IEDTKMSFPQ AKDKLFELTL QNRLQEWLLE KVVAGCKISE RDEQGLGVIH LCSILGYTWA  600
VYPYSWSGLS LDYRDKFGWT ALHWAAYYGR EKMVATLLSA GAKPNLVTDP TSQNPGGCSA  660
HDLASKNGYD GLAAYLAEKA LVAQFDDMTL AGNVSGSLQT TTNETVNPGN FSEDELYLKD  720
TLAAYRTAAD AAARIQTAFR EHSLKIRTKV VESSNPELEA RNIVAAMKIQ HAFRNYETRK  780
KIVAAARIQH RFRTWKIRKE FLNMRRQAIK IQAMFRGFQV RRQYRKIVWS VGVLEKAILR  840
WRLKRKGFRG LQVQPAETPR EPNEESDVEE DFFQASRKQA EERVEQSVVR VQAMFRSKQA  900
QEAYRRMKLE HNKAKLEYEG LLHPDLQMG
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_011100788.1
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_011100788.10.0calmodulin-binding transcription activator 5 isoform X1
RefseqXP_011100789.10.0calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A022RYH30.0A0A022RYH3_ERYGU; Uncharacterized protein
STRINGMigut.G00093.1.p0.0(Erythranthe guttata)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA45652232
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]