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 Lsa004841
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae; Lactucinae; Lactuca
Family CAMTA
Protein Properties Length: 863aa    MW: 98491.6 Da    PI: 6.8443
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
gnl|UG|Lsa#S58695854PU_refUnigeneView CDS
PUT-187a-Lactuca_sativa-33710PU_unrefplantGDBView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1162.57.8e-51281452118
       CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcyw 100
                ++e k+rwl+++ei+a+L n+++++++ ++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+ +tf rrcyw
  Lsa004841  28 MEEaKTRWLRPNEIHAVLYNHKHFSISVKPVNLPSSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNNERIHVYYAHGEDRSTFVRRCYW 127
                55669*********************************************************************************************** PP

       CG-1 101 lLeeelekivlvhylevk 118
                lL+++le+ivlvhy++++
  Lsa004841 128 LLDKNLEHIVLVHYRDTQ 145
                ***************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143773.71724150IPR005559CG-1 DNA-binding domain
SMARTSM010762.2E-7427145IPR005559CG-1 DNA-binding domain
PfamPF038599.3E-4630143IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.55E-12307393IPR014756Immunoglobulin E-set
CDDcd002044.91E-14490605No hitNo description
Gene3DG3DSA:1.25.40.205.3E-15493608IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.35E-15494608IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.194504608IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.434546578IPR002110Ankyrin repeat
SMARTSM002482.8E-4546575IPR002110Ankyrin repeat
PfamPF136372.6E-6548605No hitNo description
SMARTSM00248480585614IPR002110Ankyrin repeat
SuperFamilySSF525403.45E-8619766IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001527715737IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.474716742IPR000048IQ motif, EF-hand binding site
PfamPF006120.046718736IPR000048IQ motif, EF-hand binding site
SMARTSM000150.46738760IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.017739763IPR000048IQ motif, EF-hand binding site
PfamPF006120.0065740759IPR000048IQ motif, EF-hand binding site
SMARTSM000158.7816838IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.334818846IPR000048IQ 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: 863 aa     Download sequence    Send to blast
MEPAVSGLVG SEIHGFKTME DLDVPNMMEE AKTRWLRPNE IHAVLYNHKH FSISVKPVNL  60
PSSGTIVLFD RKMLRNFRKD GHNWKKKKDG KTVKEAHEHL KVGNNERIHV YYAHGEDRST  120
FVRRCYWLLD KNLEHIVLVH YRDTQELQGS PGLTVDSNSS SDPPTSSNLS EEIDGVDQVY  180
FTEPNETAIN HEMRIHEINT LEWDELVIPT SDKLSGSEGG NVAQFDQTNQ YISNGSFDNV  240
SRQNAQIANL GIDVLNTMHK DGLPTQESFG RWMNYIITDS PGSIDDPLQH PFTPFNGDNN  300
STDKIFNITD VSPSWALTNE ETKILVVGDF NKKYIHLMNS NIFCVCGDAF VQLEFVQSGV  360
FRCMIPPQNP GIVNLFLSSD CHNPISQVME FEFRPPPPPP ATNLPTPVNE KPDWQELEIN  420
MRLAHLLFST SKSLEILSSK IPQKTLKDAI IFAQKTRHIV NSWDFLVKSI MEKRVPFERA  480
RNSLMELTLQ NRLLEWLLER VLEGGKLPVR DDEGQGVIHL CAILDYNWAI YPYSWSGLSL  540
DFRDKFGWTA LHWAAHHGRQ RMVASLLSVG ANPNLVTDPT SENPSGCTPA DLASKNGYEG  600
LAAYLAEKAL VAHFEAMTLA GNVSGSLQST FPTNEPVVPD TSSILVSEEE QYLKDTLAAY  660
RTAADAAARI QAAFREQSFK LKTKEVEVSN PEDEARCIIA AMRIQHAFRN HESKKQMAAA  720
VRIQYRFRTW KIRKDFLNKR RQAIRIQAIF RGHQVRRQYT KIVWSVGVLE KAILRWRLKR  780
KGFRGLQVDA DKDEKQENVD GEEGFFHASR KQAEERVERS VVRVQAMFRS KLAQEEYRKM  840
KLQHIQASIE YNESFDPPTD MEK
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_023732295.10.0calmodulin-binding transcription activator 6-like
RefseqXP_023732296.10.0calmodulin-binding transcription activator 6-like
RefseqXP_023732297.10.0calmodulin-binding transcription activator 6-like
RefseqXP_023732298.10.0calmodulin-binding transcription activator 6-like
RefseqXP_023732299.10.0calmodulin-binding transcription activator 6-like
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2J6KIY40.0A0A2J6KIY4_LACSA; Uncharacterized protein
STRINGXP_009609050.10.0(Nicotiana tomentosiformis)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT3G16940.10.0calmodulin 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]