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 WALNUT_00003750-RA
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fagales; Juglandaceae; Juglans
Family CAMTA
Protein Properties Length: 953aa    MW: 107990 Da    PI: 8.0802
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
WALNUT_00003750-RAgenomeJHUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1166.35e-52701844118
                CG-1   4 ekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptf 94 
                          + rwl+++ei+aiL n++ +++ +++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+++nptf
  WALNUT_00003750-RA  70 ARIRWLRPNEIHAILCNYKYFSINAKPLNLPPSGTILLFDRKVLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGQDNPTF 160
                         489**************************************************************************************** PP

                CG-1  95 qrrcywlLeeelekivlvhylevk 118
                          rrcywlL+++le+ivlvhy+e++
  WALNUT_00003750-RA 161 VRRCYWLLDKSLEHIVLVHYRETQ 184
                         *********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.14963189IPR005559CG-1 DNA-binding domain
SMARTSM010762.2E-7566184IPR005559CG-1 DNA-binding domain
PfamPF038591.3E-4669182IPR005559CG-1 DNA-binding domain
SuperFamilySSF812968.82E-8414492IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.203.3E-15588703IPR020683Ankyrin repeat-containing domain
CDDcd002042.86E-14590700No hitNo description
PfamPF127962.0E-7590670IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.71E-15591702IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.663608673IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.354641673IPR002110Ankyrin repeat
SMARTSM002482.4E-6641670IPR002110Ankyrin repeat
PROSITE profilePS500966.998789815IPR000048IQ motif, EF-hand binding site
SMARTSM0001514804826IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.236805834IPR000048IQ motif, EF-hand binding site
SMARTSM000158.3E-4827849IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.164828852IPR000048IQ motif, EF-hand binding site
PfamPF006122.3E-4829849IPR000048IQ motif, EF-hand binding site
SMARTSM0001511907929IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.023909937IPR000048IQ 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: 953 aa     Download sequence    Send to blast
MNATNLVFAD SSNFLWFKVR RRRLRSEKNH CRGRFWFVRG FMMDGKLVGA EIHGFHTLHD  60
LDVQNTIEEA RIRWLRPNEI HAILCNYKYF SINAKPLNLP PSGTILLFDR KVLRNFRKDG  120
HNWKKKKDGK TVKEAHEHLK VGNEERIHVY YAHGQDNPTF VRRCYWLLDK SLEHIVLVHY  180
RETQELQGSP ATPVNSNSSG VSEPSAPWLS SEEHETESIG PGDNLTVQNH ELTIHEINTL  240
EWDELLLTND SNISTAPTGD KFSSFDQSNQ IAVNGSLHDV SRPFTIALAQ DINLAGAKFS  300
AEVSSFSNLT ELVARNDNIH LSLRDNIHIQ TLESQVNTNG DSITMGSTNS SDILVHDGLQ  360
GQDSFGRWMN HILADSPGSS ENTVLESSIS PGHESFVSSV MDHQKSSAPE QIFTITDISP  420
AWAFSTERTK ECQHLWKSSL FCVCGDACVP AEAVQGGVYR CLVLPHSPGL VNLFMSFDGH  480
KPISQVLNFE YRTSLLSDPV VSSEENYKWE EFQVQLRLAS LLFSTSKSLN IMSNKVSPKS  540
LKEAKKFANK SSIILNGWAD FSKSIEDNKP LFPQAKDGLF ELTLKNKVRE WLLERVVEGS  600
KTKEYDAQGQ GVIHLCAILE YTWAVYLFAC SGLSLDFRDK CGWTALHWAA YHGREKMVAA  660
LLSAGAKPNL VTDPTPGNPG GCTSADLASS KGYDGLAAYL SEKALVEQFN EMSIAGNASG  720
SLDTSSTDNL NTENLSEDQL YLKDTLAAYQ TTAEAAARIQ AAFRERSLKR RTQEIQFSIS  780
EAEAHSIVAA MKIQHAFRKY ESRKRIAAAA RIQHRFRTWK IRKEFLNLRR QAIKIQAVFR  840
GYQMRKQYHK ILWSVGVLEK AVLRWRLKRK GFRGLNVDPI EADPSLKQEG DAEEDFYRTS  900
RKQAEDRVER SVIRVQSMFR SKKAQEEYRR MKMSHNQARL EYEGLLHPDI YMT
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
11724KVRRRRLR
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}.
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_018825661.10.0PREDICTED: calmodulin-binding transcription activator 6 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2I4F1Z20.0A0A2I4F1Z2_JUGRE; calmodulin-binding transcription activator 6 isoform X2
STRINGXP_008223308.10.0(Prunus mume)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF42883459
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]