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 Thecc1EG021327t1
Common NameTCM_021327
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma
Family CAMTA
Protein Properties Length: 908aa    MW: 102599 Da    PI: 7.0838
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Thecc1EG021327t1genomeCGDView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1164.22.3e-51311463118
              CG-1   3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfq 95 
                       + ++rwl+++ei+aiL n++ + ++ ++ + pksg ++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+++nptf 
  Thecc1EG021327t1  31 EARSRWLRPNEIHAILCNHKYFPIHVKPMNLPKSGIIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGQDNPTFV 123
                       459****************************************************************************************** PP

              CG-1  96 rrcywlLeeelekivlvhylevk 118
                       rrcywlL+++le+ivlvhy+e++
  Thecc1EG021327t1 124 RRCYWLLDKTLEHIVLVHYRETQ 146
                       ********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.23625151IPR005559CG-1 DNA-binding domain
SMARTSM010763.2E-7429146IPR005559CG-1 DNA-binding domain
PfamPF038599.1E-4631144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812961.82E-12363449IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.201.5E-18534660IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484032.95E-19535659IPR020683Ankyrin repeat-containing domain
PfamPF127968.0E-9539627IPR020683Ankyrin repeat-containing domain
CDDcd002046.09E-17553657No hitNo description
PROSITE profilePS5029717.157565669IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008812.155598630IPR002110Ankyrin repeat
SMARTSM002481.7E-6598627IPR002110Ankyrin repeat
SMARTSM002483200637668IPR002110Ankyrin repeat
PROSITE profilePS500966.632746772IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.126762791IPR000048IQ motif, EF-hand binding site
PfamPF006120.1862882IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.51862889IPR000048IQ 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: 908 aa     Download sequence    Send to blast
MDGDRPGRLV GTEIHGFHTL EDLDVQNTME EARSRWLRPN EIHAILCNHK YFPIHVKPMN  60
LPKSGIIVLF DRKMLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGNEERIH VYYAHGQDNP  120
TFVRRCYWLL DKTLEHIVLV HYRETQESQG SPATPVNSNS SSISDQSTPL LVTEEFDSGA  180
GNINYEEPSG LTVRNHEMRL HEINTLEWDD LLVTNDTNDS TLSRRDKDSF FNQGSQIAAN  240
GFSNDDGHTS AYNLSTGISS LGNLTDPVAQ SNNAYINYPE GICNQVSGGQ VNSNVQRKDF  300
RVIGTGDSLD LLVDDGLQSQ DSFGRWINYI ITESPGSVDD PVPESSISSG QEAITSPEQI  360
FSITGVSPAW AYTTEKTKIL VTGVFHQAYQ HLVKSNLFCV CGDVCIPAEL IQVGVYCCSL  420
SEHSPGLVNL YMSLDGHKPI SQVLSFEYRV PVLHDPIPPL EDESRWEEFQ LQMRLAYLLF  480
STSQSLNILS GKVSPNTLKE AKKFALKTTN ISKSWAYLIK SIEENRVSFT QAKDSLLEIA  540
LKSKLKDWLL ERIIEGCKTT EYDAQGQGVL HLCAILGYTW AIYLFSWSGL SLDFRDKHGW  600
TALHWAAYYG REKMVAVLLS AGAKPNLVTD PTAQNPSGRT AADLASLKGY DGLAAYLSEE  660
ALVAQFNDMA VAGNASGSLE TSRTETTNRE NLNEEELYLK ETLAAYRTAA DAAARIHTAF  720
REQSLKMRTK AVQFSNPEDE ARNIVAALKI QHAFRNFETR KKMAAAARIQ YRFRTWKIRK  780
DFLALRRQAA AFRGFQVRRQ YRKIIWSVGV LEKAILRWRL KRKGFRGLQV NTVEPVGEPK  840
QESVTEEDFY RTSRKQAEER VEKAVVCVQS MFRSKKAQQE YRRMKMVHEL AMLEYESLLD  900
PSSDMDA*
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_017974984.10.0PREDICTED: calmodulin-binding transcription activator 5
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A061EWS00.0A0A061EWS0_THECC; Calmodulin binding,transcription regulators, putative isoform 1
STRINGEOY066730.0(Theobroma cacao)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM40212758
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. Motamayor JC, et al.
    The genome sequence of the most widely cultivated cacao type and its use to identify candidate genes regulating pod color.
    Genome Biol., 2013. 14(6): p. r53
    [PMID:23731509]
  3. 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]
  4. 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]