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 Migut.G00093.2.p
Common NameMIMGU_mgv1a001025mg
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Phrymaceae; Erythranthe
Family CAMTA
Protein Properties Length: 932aa    MW: 105483 Da    PI: 7.4302
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Migut.G00093.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1166.93.3e-52301472118
              CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenpt 93 
                       l+e k+rwl+++ei+a+L n+++++++ ++k+ pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+ pt
  Migut.G00093.2.p  30 LEEaKSRWLRPNEIHAVLCNHKHFTVHVKPKNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDSPT 122
                       55669**************************************************************************************** PP

              CG-1  94 fqrrcywlLeeelekivlvhylevk 118
                       f rrcywlL+++le+ivlvhy+e++
  Migut.G00093.2.p 123 FVRRCYWLLDKSLEHIVLVHYRETQ 147
                       **********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.97126152IPR005559CG-1 DNA-binding domain
SMARTSM010762.0E-7529147IPR005559CG-1 DNA-binding domain
PfamPF038594.2E-4632145IPR005559CG-1 DNA-binding domain
SuperFamilySSF812969.8E-10382467IPR014756Immunoglobulin E-set
SuperFamilySSF484031.32E-17550679IPR020683Ankyrin repeat-containing domain
CDDcd002043.49E-16562677No hitNo description
Gene3DG3DSA:1.25.40.201.4E-17562680IPR020683Ankyrin repeat-containing domain
PfamPF127963.3E-7564647IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.494573650IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.968618650IPR002110Ankyrin repeat
SMARTSM002481.8E-6618647IPR002110Ankyrin repeat
SuperFamilySSF525405.31E-7746832IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001523781803IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071782811IPR000048IQ motif, EF-hand binding site
SMARTSM000151.9E-4804826IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.798805829IPR000048IQ motif, EF-hand binding site
PfamPF006121.4E-4806826IPR000048IQ motif, EF-hand binding site
SMARTSM0001513885907IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.297887915IPR000048IQ 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: 932 aa     Download sequence    Send to blast
MEINTVPGRL VGSEIHGFRT MEDLEVGAML EEAKSRWLRP NEIHAVLCNH KHFTVHVKPK  60
NLPKSGTIVL FDRKMLRNFR KDGHNWKKKK DGKTVKEAHE HLKVGNEERI HVYYAHGEDS  120
PTFVRRCYWL LDKSLEHIVL VHYRETQELQ GSPATPVNSN SSPAVSDPSA SWPLSEESDS  180
AGHQVNYGSS MSPLERNDSM TIKNHQQTLH EINTLEWDEL VVPDDLDKLN SPEEVQFAGF  240
ELANQYQTSN NRTNDDAVST SKVTPQSSGN SFYEQVGKSN SMNHKNSNNL SYQTVGHEMN  300
VHSETMISGL GTLSGASSIY NLAKDGLQAQ DSFGRWATYD IDNSLESLVD QELESSVLNG  360
HQSFSYQKID NHQPSPPGQI FNITDISPAS ALSTEETKIL VIGFFSEGQL PRTDSKLYLA  420
CGDSIFPLEI VQGGVFRCLI PPQTPGSVNL YMTFDGHKPI SQVLTFEVRA PVQPNRMVSF  480
ENKTDWKEFQ LQLRLAHLLF SSAKGLSIYN TKISQTALKE AKAFAQKTSH ISNGWVFLSK  540
MIEERQMSFP QAKDQLFELT LHNRLLEWLL EKVAAGSKIS ERDEQGQGVI HLCAILGYTW  600
AVYPFSWSGL SLDYRDKHGW TALHWAAYYG REKMVATLLS AGAKPNLVTD PTSQNPGGCN  660
AADLASTNGY DGLAAYLAEK ALVEQFKEMT VAGNVSGSLQ TSSNEPINPE NFTEEELYLK  720
DTLIAYRTAA DAAARINAAF REHSFKIRKQ AVESSNPEIE ARNIVAAMKI QHAFRKYETH  780
KKLAAAARIQ YRFRTWKIRK DFLNMRRQAI KIQAHFRGFQ VRRHYRQIVW SVGVLEKAVL  840
RWRLKRKGFR GLQVQPETAV VDPNQDGEVV EEAFFRASRK QAEDRVERSV VRVQAMFRSK  900
QAQEEYRRMK LEHSKAKLEY DELLHPDDEM G*
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}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapMigut.G00093.2.p
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
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_012827760.10.0PREDICTED: calmodulin-binding transcription activator 5-like isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A022RYH30.0A0A022RYH3_ERYGU; Uncharacterized protein
STRINGMigut.G00093.1.p0.0(Erythranthe guttata)
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]