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 Lsa011807
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: 847aa    MW: 94754.2 Da    PI: 5.5889
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
gnl|UG|Lsa#S58696078PU_refUnigeneView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1167.12.8e-52151265116
       CG-1   5 kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywlLee 104
                + rwlk+ e++ iL+nfe+ +lt++++++p+sgsl+L+n++++r+frkDG++w++kkdg+tv E+he+LKvg+ve+l+cyYah+e+np+fqrr+yw+L+ 
  Lsa011807  15 HIRWLKPGEVLFILQNFEEKQLTHAPPEKPPSGSLFLFNKRVLRFFRKDGHNWRRKKDGRTVGEAHERLKVGNVEALNCYYAHGEHNPSFQRRSYWMLDP 114
                78************************************************************************************************** PP

       CG-1 105 elekivlvhyle 116
                 +++ivlvhy++
  Lsa011807 115 LMDHIVLVHYRD 126
                **********97 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143773.9597133IPR005559CG-1 DNA-binding domain
SMARTSM010768.6E-7210128IPR005559CG-1 DNA-binding domain
PfamPF038595.2E-4713126IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.101.1E-8328422IPR013783Immunoglobulin-like fold
SuperFamilySSF812965.47E-16335420IPR014756Immunoglobulin E-set
PfamPF018331.5E-8336420IPR002909IPT domain
CDDcd001023.21E-5336422No hitNo description
SuperFamilySSF484036.84E-14505603IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.201.1E-13506603IPR020683Ankyrin repeat-containing domain
CDDcd002044.75E-12528600No hitNo description
PROSITE profilePS5029714.371528600IPR020683Ankyrin repeat-containing domain
PfamPF127962.0E-7531601IPR020683Ankyrin repeat-containing domain
PROSITE profilePS500889.992541573IPR002110Ankyrin repeat
SMARTSM002480.005541573IPR002110Ankyrin repeat
SMARTSM002483500580609IPR002110Ankyrin repeat
SMARTSM000153.1647669IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.419648677IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525402.1E-7652670IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001517699721IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525402.1E-7700751IPR027417P-loop containing nucleoside triphosphate hydrolase
PfamPF006120.024702720IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.638702729IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0013722744IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.389723747IPR000048IQ motif, EF-hand binding site
PfamPF006121.6E-4725743IPR000048IQ 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: 847 aa     Download sequence    Send to blast
MTSGYNIRDL VGEAHIRWLK PGEVLFILQN FEEKQLTHAP PEKPPSGSLF LFNKRVLRFF  60
RKDGHNWRRK KDGRTVGEAH ERLKVGNVEA LNCYYAHGEH NPSFQRRSYW MLDPLMDHIV  120
LVHYRDITMT GNSGGSISTL STGSSSLIQS PDSYATPLSR SGGGFSQSTS SPSSVEVSSD  180
VVTMSNGTSP LSLIEGTDNF EIDVALRRIE EQLSLGEENL KDLSLYYSEN EISNDSGFSI  240
DDQDYGDVSI TNNQQTLIWD DVIEYGGNPV EEKGANNNPS LPQEIEDFKF PAYTPDRNLS  300
DRYPDFYSTF FDQGQTEMPL ESNLGLSISQ EQKFNIRDIA PESGSASEST KVLIIGKFTC  360
DSDTYKNKWY CMFGETEVPI EIMQEGVLCC YAPPLPPGKV TVCITSGNRE SISETREFEY  420
LEKHRGGKKC WRSSEELLLL VRFVQMLLSE KEGGEEVEES WSQLIEGVLD GSLASYDAID  480
CLLEELLKEK LKQWLSSSSS SCGLLSKREQ GIIHMVSGLG FGWALTPILN SGVGVNFRDI  540
NGWTALHWAA RFGREKMVAE LVASGAFTGA VTDPSHEDPK GKTPASIAAT SGHKGLAGYL  600
SEVSLTTHPS LQTQISHNIQ PQTTSLNPNN ISNEDLSLTD TLAAVRNATQ AAACIQSAFR  660
AHSFRKRQQK ESFQLEEEDE YGILPSHIET LSTFLKNGND YNAALSIQKK YRGWKGRKDF  720
LALRQKVVKI QAHVRGHQVR KNYMVFCWAV GVVEKVVLRW RRKGVGLRGF KQGGDETEDE  780
DIVKAFRKEK VDVSIDEAVS RVLSMVDSQQ ARQQYRRMLL KYRQAKAERE GLESQGGSTS  840
QNDVMNT
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator that 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 together with CAMTA2 and CAMTA3 in the positive regulation of a general stress response (PubMed:25039701). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:25039701, ECO:0000305|PubMed:11925432}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, salt, wounding, ethylene, methyl jasmonate, abscisic acid, H(2)O(2) and salicylic acid (PubMed:12218065). Induced by cold stress (PubMed:28351986). {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:28351986}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_023763404.10.0calmodulin-binding transcription activator 4-like
SwissprotQ9FYG21e-173CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A2J6LEL00.0A0A2J6LEL0_LACSA; Uncharacterized protein
STRINGVIT_01s0010g03850.t010.0(Vitis vinifera)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.11e-149Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains
Publications ? help Back to Top
  1. Benn G, et al.
    A key general stress response motif is regulated non-uniformly by CAMTA transcription factors.
    Plant J., 2014. 80(1): p. 82-92
    [PMID:25039701]
  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]