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_011100790.1
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: 927aa    MW: 104925 Da    PI: 7.2512
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_011100790.1genomeNCBIView 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_011100790.1  30 MEEaKARWLRPNEIHAILCNHKYFTVYVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDNPTFV 124
                     45669****************************************************************************************** PP

            CG-1  96 rrcywlLeeelekivlvhylevk 118
                     rrcywlL+++le+ivlvhy+e++
  XP_011100790.1 125 RRCYWLLDKSLEHIVLVHYRETQ 147
                     ********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.67126152IPR005559CG-1 DNA-binding domain
SMARTSM010763.5E-7729147IPR005559CG-1 DNA-binding domain
PfamPF038597.0E-4632145IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.22E-9380465IPR014756Immunoglobulin E-set
CDDcd002041.30E-13564674No hitNo description
Gene3DG3DSA:1.25.40.205.1E-15565677IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484033.42E-16565677IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.345573647IPR020683Ankyrin repeat-containing domain
SMARTSM002485.1E-6615644IPR002110Ankyrin repeat
PROSITE profilePS5008811.434615647IPR002110Ankyrin repeat
PfamPF000239.2E-5616646IPR002110Ankyrin repeat
SuperFamilySSF525402.92E-6723829IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.163763789IPR000048IQ motif, EF-hand binding site
SMARTSM0001514778800IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.089782808IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0012801823IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.091802826IPR000048IQ motif, EF-hand binding site
PfamPF006120.001803823IPR000048IQ motif, EF-hand binding site
SMARTSM0001535881903IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.114883911IPR000048IQ 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: 927 aa     Download sequence    Send to blast
MENTGVRGRF VGSEIHGFRT LEDLDVGNMM EEAKARWLRP NEIHAILCNH KYFTVYVKPV  60
NLPKSGTIVL FDRKMLRNFR KDGHNWKKKK DGKTVKEAHE HLKVGNEERI HVYYAHGEDN  120
PTFVRRCYWL LDKSLEHIVL VHYRETQEGS PATPVNSNSN SAGSDLSATW PMSEESDSAV  180
DRVYYGSTGS YLECHDSVTV KHHEQRLYEI NTLEWDELLV PDDPHRLITR QQGTTAGFEL  240
QNQYQMNSYR INDDAPSNNK VSPECSTNSF SEPVAGRSSI NYTSPNNMSY QTVEQDTIVN  300
SETMVSGLMP SGGAGSLYNL GKDGLQSQDS FGRWVTHIIA ESPESVDDHT LESSNLAGHQ  360
SSTYPLMDSH DSSPLGPIFT ITDVSPAWAL STEETKILVV GFFNEGQLPY SESKLYLACG  420
DSLLPVDVVQ AGVFRCLIPP QAPKLGNLYI TFDGHKPISQ VLTFEIRAPV QPGTVSFENK  480
TDWEEFQLQM RLAHLLFSSS KGLSIYSTKL SPTALKEAKA FAQKTSHISD GWLHMAKVIE  540
DTKMSFPQAK DKLFELTLQN RLQEWLLEKV VAGCKISERD EQGLGVIHLC SILGYTWAVY  600
PYSWSGLSLD YRDKFGWTAL HWAAYYGREK MVATLLSAGA KPNLVTDPTS QNPGGCSAHD  660
LASKNGYDGL AAYLAEKALV AQFDDMTLAG NVSGSLQTTT NETVNPGNFS EDELYLKDTL  720
AAYRTAADAA ARIQTAFREH SLKIRTKVVE SSNPELEARN IVAAMKIQHA FRNYETRKKI  780
VAAARIQHRF RTWKIRKEFL NMRRQAIKIQ AMFRGFQVRR QYRKIVWSVG VLEKAILRWR  840
LKRKGFRGLQ VQPAETPREP NEESDVEEDF FQASRKQAEE RVEQSVVRVQ AMFRSKQAQE  900
AYRRMKLEHN KAKLEYEGLL HPDLQMG
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_011100790.1
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_011100790.10.0calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A022RYH30.0A0A022RYH3_ERYGU; Uncharacterized protein
STRINGMigut.G00093.1.p0.0(Erythranthe guttata)
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]