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 XP_015900007.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rhamnaceae; Paliureae; Ziziphus
Family CAMTA
Protein Properties Length: 892aa    MW: 100619 Da    PI: 7.4266
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_015900007.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1168.97.7e-5331183118
            CG-1   3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrr 97 
                     + ++rwl+++ei+aiL n++++++  ++ + pksg++iL++rk++r+frkDG++wkkkkdgktv+E+he+LKvg  e +++yYah+++nptf rr
  XP_015900007.1   3 EARSRWLRPNEIHAILCNYKRFTINVKPVNLPKSGTIILFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGDEERIHVYYAHGQDNPTFVRR 97 
                     459******************************************************************************************** PP

            CG-1  98 cywlLeeelekivlvhylevk 118
                     cywlL+++le+ivlvhy+e++
  XP_015900007.1  98 CYWLLDKSLEHIVLVHYRETQ 118
                     ******************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143778.5021123IPR005559CG-1 DNA-binding domain
SMARTSM010761.2E-771118IPR005559CG-1 DNA-binding domain
PfamPF038592.1E-463116IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.29E-15343430IPR014756Immunoglobulin E-set
PfamPF018333.9E-4344429IPR002909IPT domain
SuperFamilySSF484033.11E-18529641IPR020683Ankyrin repeat-containing domain
PfamPF127961.4E-8530608IPR020683Ankyrin repeat-containing domain
CDDcd002041.24E-15530638No hitNo description
Gene3DG3DSA:1.25.40.206.8E-18532642IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029717.237537650IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.915579611IPR002110Ankyrin repeat
SMARTSM002484.3E-6579608IPR002110Ankyrin repeat
SuperFamilySSF525405.84E-7690793IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001533723745IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.327727753IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.272743772IPR000048IQ motif, EF-hand binding site
SMARTSM00015270746764IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0011765787IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.768766790IPR000048IQ motif, EF-hand binding site
PfamPF006124.1E-4767787IPR000048IQ motif, EF-hand binding site
SMARTSM0001510845867IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.279847875IPR000048IQ 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: 892 aa     Download sequence    Send to blast
MEEARSRWLR PNEIHAILCN YKRFTINVKP VNLPKSGTII LFDRKMLRNF RKDGHNWKKK  60
KDGKTVKEAH EHLKVGDEER IHVYYAHGQD NPTFVRRCYW LLDKSLEHIV LVHYRETQEG  120
SPVTPVNSNS SSASDPSAPW PLSEELDSGT NHAYYAGENE ILVSSDNLTV RNHEQRLHDI  180
NTLEWDELLA IHDPNNSVAS RDKVSFFNQQ NQVAGNGLLH GGATSLSPEI LSFNILTNPT  240
ATSGDIGYNL PQSAYVPTVG AQLNSNVQRR DSIGAGAGGS LDVLVNDGLH SQDSFGRWIN  300
DFITDSSDSV DGSVLETSIP SAQDSFSSLA MHLQSPVSEQ IFNITDVSPA WAYSNEKTKI  360
LLTGFFREEY QHLSKSDLLC VCGDISVTAE IVQVGVYRCL VSPHSPGLVN LYISLEGFKP  420
ISQVLNFEYR TPALSDQIVS SEERDRWEEF QMQMRLAYLL FSTSKSLEIL TSKASPNALK  480
EAKKYAQKTS HVSNSWAIFI KSIEDSKIPF SQAKDSLFKL ILRNRLKDWL LERVVYGSKI  540
SEFDAQGQGV IHLCAILGYT WAISLFSASG LSLDFRDKHG WTALHWAAYF GREKMVAVLL  600
SAGAKPNLVT DPTSDNPGGR TAADLASLNG YDGLAGYLSE KALVEQFKDM SIAGNVSGTL  660
DTSTNDFVNP ENLCEEELNL KETLAAYRTA ADAAARIQVA FREHSLKIRT QAVENSNPEI  720
EARNIVAAMK IQHAFRNYES RKKMAAAARI QHRFRTWKIR KEFLNLRRQA IKIQAAFRGY  780
QVRRQYRKIL WSVGVLEKAI LRWRLKRRGF RGLQVDPIEA VDDQFQGSDT EEDFYKASKK  840
QAEERVERAV VSVQAMFRSK KAQEEYRRMK MAHNQAMLEY EGFLDPENDL VG
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
Cis-element ? help Back to Top
SourceLink
PlantRegMapXP_015900007.1
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
PlantRegMap-Retrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_015900007.10.0calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2P5F6180.0A0A2P5F618_TREOI; Notch
STRINGXP_009369951.10.0(Pyrus x bretschneideri)
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]