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 Niben101Scf00380g00001.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; Nicotiana
Family CAMTA
Protein Properties Length: 757aa    MW: 86341.7 Da    PI: 9.2499
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Niben101Scf00380g00001.1genomeBTI-
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1165.58.7e-52301463118
                      CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYa 86 
                               +e k rwl+++ei+aiL n++ +++  ++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYa
  Niben101Scf00380g00001.1  30 EEaKMRWLRPNEIHAILCNYKYFNIFVKPVNLPTSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYA 114
                               45599******************************************************************************** PP

                      CG-1  87 hseenptfqrrcywlLeeelekivlvhylevk 118
                               h+e++ptf rrcywlL+++le+ivlvhy+e++
  Niben101Scf00380g00001.1 115 HGEDHPTFVRRCYWLLDKSLEHIVLVHYRETQ 146
                               *****************************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.01425151IPR005559CG-1 DNA-binding domain
SMARTSM010761.8E-7528146IPR005559CG-1 DNA-binding domain
PfamPF038594.1E-4631144IPR005559CG-1 DNA-binding domain
SuperFamilySSF484034.82E-16397512IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.203.8E-15397511IPR020683Ankyrin repeat-containing domain
PfamPF127968.0E-7398477IPR020683Ankyrin repeat-containing domain
CDDcd002043.43E-12413507No hitNo description
PROSITE profilePS5029714.796415480IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.728448480IPR002110Ankyrin repeat
SMARTSM002483.7E-6448477IPR002110Ankyrin repeat
SuperFamilySSF525401.33E-6560661IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.181595621IPR000048IQ motif, EF-hand binding site
SMARTSM0001516610632IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.327611640IPR000048IQ motif, EF-hand binding site
PfamPF006120.17613631IPR000048IQ motif, EF-hand binding site
SMARTSM000156.6E-4633655IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.468634658IPR000048IQ motif, EF-hand binding site
PfamPF006121.1E-4635655IPR000048IQ motif, EF-hand binding site
SMARTSM0001515712734IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.462714742IPR000048IQ 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: 757 aa     Download sequence    Send to blast
MESSRAGQLS GSDIHGFHTL QDLDIPSIME EAKMRWLRPN EIHAILCNYK YFNIFVKPVN  60
LPTSGTIVLF DRKMLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGNEERIH VYYAHGEDHP  120
TFVRRCYWLL DKSLEHIVLV HYRETQEAQG SPATSVAKGS PATPVTSNSS SDPSDPSGWV  180
LSEECNSVDE RTYGSSQHAH LEPNRDVTAK NHEQRLLEIN TLDWDELLAP DNPNKLIATQ  240
EAGGRASVGQ QNQFEVNGYS LNSGVYRCVI SPQPPGLVSL YLSFDGNTPI SQVMTYEFRA  300
PSARKWTAPL EEQSSWDEFR VQMRLAHLLF STSKSLSIFS SRVHQDSLKE AKRFVRKCSH  360
ITDNWAYLIK SIEDRKLPVP HAKDCLFELS LQTKFHEWLL ERVIGGCKAS EWDEQGQGVI  420
HLCAILGYTW AVYPFSWSGL SLDYRDKYGW TALHWAAHYG REKMVATLLS AGAKPNLVTD  480
PTSENPGGST VADLASKNGF EGLGAYLAEK ALVAHFKDMS LAGNVSGSLQ TTTEHINPGN  540
FTEEELYLRD TLAAYRTAAD AAARIQAAFR EHSFKVQTKA VESSNPEMEA RNIVAAMKIQ  600
HAFRNYESRK KLAAAARIQY RFRSWKMRKD FLNMRRHAIT IQAVFRGFQV RKQYRKIVWS  660
VGVLEKAVLR WRLKRKGFRG LQVQSSQAVD IKPDGDVEED FFRASRKQAE ERVERSVVRV  720
QAMFRSKRAQ EEYRRMKLEH DSATLEYERA SLLNPDI
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}.
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_009788810.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A1U7XQQ20.0A0A1U7XQQ2_NICSY; calmodulin-binding transcription activator 5 isoform X2
STRINGXP_009788809.10.0(Nicotiana sylvestris)
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]