PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Lsa013364
Organism
Lactuca sativa
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: 864aa    MW: 98814.9 Da    PI: 6.8618
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
gnl|UG|Lsa#S58671851PU_unrefUnigeneView CDS
gnl|UG|Lsa#S58694113PU_unrefUnigeneView CDS
PUT-187a-Lactuca_sativa-37039PU_refplantGDBView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1152.97e-48311463118
       CG-1   3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywlL 102
                + k+rwl+++ei+a+L n+++++++ ++ + pksg+++L++rk++r+fr+DG++wkkkkdgktv+E+he+LK+g+ e +++yYah+e+++t+ rrcy lL
  Lsa013364  31 EAKTRWLRPNEIHAMLCNHKHFNIHVKPVNLPKSGTIVLFDRKMLRNFRRDGHNWKKKKDGKTVKEAHEHLKIGNDERIHVYYAHGEDQSTLVRRCYCLL 130
                3499************************************************************************************************ PP

       CG-1 103 eeelekivlvhylevk 118
                +++le+ivlvhy++++
  Lsa013364 131 DKKLEHIVLVHYRDTQ 146
                *************986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143771.87125151IPR005559CG-1 DNA-binding domain
SMARTSM010761.8E-6628146IPR005559CG-1 DNA-binding domain
PfamPF038593.0E-4431144IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.104.5E-5301397IPR013783Immunoglobulin-like fold
SuperFamilySSF812961.15E-15307394IPR014756Immunoglobulin E-set
PfamPF018333.4E-5308393IPR002909IPT domain
SuperFamilySSF484039.17E-16489606IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.201.7E-15491606IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.486499606IPR020683Ankyrin repeat-containing domain
CDDcd002041.77E-12502603No hitNo description
PROSITE profilePS5008811.648544576IPR002110Ankyrin repeat
SMARTSM002483.9E-4544573IPR002110Ankyrin repeat
PfamPF000231.5E-6545575IPR002110Ankyrin repeat
SMARTSM002481200583612IPR002110Ankyrin repeat
SuperFamilySSF525403.45E-6688762IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.797696722IPR000048IQ motif, EF-hand binding site
SMARTSM0001516711733IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.602712741IPR000048IQ motif, EF-hand binding site
SMARTSM000157.5E-4734756IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.109735759IPR000048IQ motif, EF-hand binding site
PfamPF006129.1E-5736756IPR000048IQ motif, EF-hand binding site
SMARTSM0001514816838IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.425818846IPR000048IQ 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: 864 aa     Download sequence    Send to blast
MEPAVPSQLV GSEIHGFKTM QDLDIPPWFE EAKTRWLRPN EIHAMLCNHK HFNIHVKPVN  60
LPKSGTIVLF DRKMLRNFRR DGHNWKKKKD GKTVKEAHEH LKIGNDERIH VYYAHGEDQS  120
TLVRRCYCLL DKKLEHIVLV HYRDTQELQS SPTIESNASS DAPASWTLSE EHDGVDQVYN  180
VEPNETIINH KMTLHELNTL EWDDLVVPND SDNLITHEGG NIPYFDQDDQ YGLNGIVNTM  240
DPGFINSSND ILDSLEKDGL KNQDSFGRWM NYNMTDTDSP LVIDEPIGKE TVRNPSSQSQ  300
SLEQIFNITE VSPSWASSKE ETKVLVVGVF HEEHLHLSNS NLFCVCGDVC VPIETVQPGV  360
FRCFMPPHTP GVVNLFITPD GQTPISQLIP FEYRAPPTQQ NITISSQEKP EWEDFQVKMR  420
LAHLLFSTSR SLNILSSHVP PKVIKEAKIF AHKTRSIVKS WDLLVDSIVG KKIAFSQAKN  480
SLFELILQNR LLEWLLERLL EGSKIPERDD EGQGVIHLCA VLDYTWAIFP YSWSGLSIDF  540
RDKRGWTALH WAAHYGKQRT VASLLSAGAN PNLVTDPTSE NPGGCTPADL ASKNGYEGLA  600
AFLAEKALLA HFEAMTLAGN VSGSLQSTIP KDDDYTAADE PVTEEEQYLK ETLAAYRRAA  660
DAAARIQAAF REQSFKLRSK AVEFANTEDE ARCIIAAMRI QHAYRKHETR KQMAAAVRIQ  720
HRFRTWKIRK DFLNKRRQAI KIQAFFRGFQ VRKQYKKIVW SVGVLEKAIL RWRLKRKGFR  780
GLKVASNNDD VDNNENEENI VEENFYNASR KQAEERVERS IIRVQAMFRS KRAQEEYRKM  840
KQALSQASLE YDELLNPATI NMER
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_023765664.10.0calmodulin-binding transcription activator 6-like
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2J6L9M50.0A0A2J6L9M5_LACSA; Uncharacterized protein
STRINGVIT_05s0077g01240.t010.0(Vitis vinifera)
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]