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 Ote100012360071
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ocimum
Family CAMTA
Protein Properties Length: 1034aa    MW: 117008 Da    PI: 6.8292
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Ote100012360071genomeOteDB-
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11512.7e-47311673118
                          CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvgg..... 77 
                                   +e ++rwl+++ei+aiL n+++++++ ++ + pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LK +      
  Ote100012360071|100012360071  31 EEaTSRWLRPNEIHAILSNHKHFTVHVKPMNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKENLniigp 111
                                   45489********************************************************************8878999* PP

                          CG-1  78 ...............vevlycyYahseenptfqrrcywlLeeelekivlvhylevk 118
                                                   e +++yYah+e+nptf rrcywlL+++le+ivlvhy+e++
  Ote100012360071|100012360071 112 lvcyciilvvmkvgnEERIHVYYAHGEDNPTFVRRCYWLLDKSLEHIVLVHYRETQ 167
                                   *****************************************************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143774.96426172IPR005559CG-1 DNA-binding domain
SMARTSM010761.4E-6529167IPR005559CG-1 DNA-binding domain
PfamPF038596.5E-2532105IPR005559CG-1 DNA-binding domain
PfamPF038597.3E-15122165IPR005559CG-1 DNA-binding domain
SuperFamilySSF812962.38E-5511573IPR014756Immunoglobulin E-set
CDDcd002042.81E-17666781No hitNo description
Gene3DG3DSA:1.25.40.204.9E-17668785IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.38E-18669784IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.3677793IPR020683Ankyrin repeat-containing domain
PfamPF127965.9E-7695782IPR020683Ankyrin repeat-containing domain
SMARTSM002481.2E-4722751IPR002110Ankyrin repeat
PROSITE profilePS5008811.194722754IPR002110Ankyrin repeat
SMARTSM002481900761790IPR002110Ankyrin repeat
SuperFamilySSF525409.03E-6831936IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.163870896IPR000048IQ motif, EF-hand binding site
SMARTSM0001516885907IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.98889915IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0012908930IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.725909933IPR000048IQ motif, EF-hand binding site
PfamPF006120.0011910930IPR000048IQ motif, EF-hand binding site
SMARTSM000158.69881010IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.9869901018IPR000048IQ 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: 1034 aa     Download sequence    Send to blast
MEGNSVPSLL VGPEIHGFRT MEDLDFQNIL EEATSRWLRP NEIHAILSNH KHFTVHVKPM  60
NLPKSGTIVL FDRKMLRNFR KDGHNWKKKK DGKTVKEAHE HLKENLNIIG PLVCYCIILV  120
VMKVGNEERI HVYYAHGEDN PTFVRRCYWL LDKSLEHIVL VHYRETQELQ GSPATPANSN  180
SAISNPSAPR PLHEGSDSAV DPMYYSSSMP VLERNDSMMI KDHAQRLHEI NTLDWDELLV  240
AVDPNKHNSP QEGNTAGFEL PNQYHTNSYN ISCTWAHESP GLFPASSGKL VSSYLPVIGW  300
MSDLFWPVSL GVFGYQCVTC LPTWHEFVPS FQLNDALSSN QVSPESSDIS EQVAWMNSVN  360
FNIPNNLSYQ TVGNETTVSQ ETRISGLVTL SGSGANSLVT DSSQSQDSFG NMTTHMIAES  420
PESVDNHSLE SSLLNGHQSL SYSLVDNHRP SPLGQIFNVT DITPTWALST EETKVLSSVT  480
VFLSIGLSCW YASDNGMLNC FVILVVGFFS DGHQHHADSK LYLACGDSIL PVEVVQRGVF  540
RCLISPQAPG MVNLYMTFDG HKPISQVLTF EFRAPMQPNG SISIENADNW KEFQLQMRLA  600
HLLFPSSKDL NIYSTKSSQT ALKEAKFFAK KTSHFSDGWF YLSKMIEETK MPFPQAKDRL  660
FDLTLQNRLV EWLLEKVATG CKITERDEQG QGVIHLCAIL GYTWAVYPFS WSGLSLDYRD  720
KFGWTALHWA AYYGREKMVA ALLSVGAKAN LVTDPTSQNP GGCTAADLAS INGYEGLAAY  780
LAEKALVQQF EDMTLAGNVS GSLQTTTNES VNIGNFNEDE LYLKDTLAAY RTAADAAARI  840
QAAFREHSLK VQTQVIEASN TEIEARNIVA AMKIQHAFRN YETRKKIVAA ARIQHRFRTW  900
KIRKDFLNMR RQAIKIQAMF RGFQVRRQYR KICWSVGVLE KAILRWRLKR KGFRGLQVEP  960
TETMKDQNQD SDVEEDFFKA SRKQAEERVE RSVVRVQAMF RSRRAQEEYR RMKLECSKAT  1020
LEYEEFLHPD AEMG
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}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_012840434.10.0PREDICTED: calmodulin-binding transcription activator 5-like isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2G9H5Q90.0A0A2G9H5Q9_9LAMI; Uncharacterized protein
STRINGMigut.N00052.1.p0.0(Erythranthe guttata)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA45652232
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]