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 SapurV1A.0050s0650.3.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; Salix
Family CAMTA
Protein Properties Length: 899aa    MW: 101308 Da    PI: 7.2774
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
SapurV1A.0050s0650.3.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11642.5e-5131183118
                    CG-1   3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahse 89 
                             ++++rwl+++ei+a+L n++ +++  ++   p+sg+++L++rk++r+frkDG+swkkkkdgktv+E+he+LKvg+ve +++yYah++
  SapurV1A.0050s0650.3.p   3 ESRTRWLRPNEIHAMLCNYKYFTINVKPVYLPESGTIVLFDRKMLRNFRKDGHSWKKKKDGKTVKEAHEHLKVGNVERIHVYYAHGQ 89 
                             559************************************************************************************ PP

                    CG-1  90 enptfqrrcywlLeeelekivlvhylevk 118
                             +n+tf rrcywlL+++le+ivlvhy+e++
  SapurV1A.0050s0650.3.p  90 DNQTFVRRCYWLLDKSLEHIVLVHYRETQ 118
                             **************************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM010761.6E-721118IPR005559CG-1 DNA-binding domain
PROSITE profilePS5143774.4521123IPR005559CG-1 DNA-binding domain
PfamPF038598.9E-454116IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.105.9E-4345438IPR013783Immunoglobulin-like fold
PfamPF018332.4E-5349435IPR002909IPT domain
SuperFamilySSF812964.62E-13350436IPR014756Immunoglobulin E-set
SuperFamilySSF484032.8E-16539647IPR020683Ankyrin repeat-containing domain
CDDcd002045.31E-15540644No hitNo description
Gene3DG3DSA:1.25.40.205.7E-15543647IPR020683Ankyrin repeat-containing domain
PfamPF127962.7E-6552614IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.902552617IPR020683Ankyrin repeat-containing domain
SMARTSM002481.1E-5585614IPR002110Ankyrin repeat
PROSITE profilePS5008811.354585617IPR002110Ankyrin repeat
PROSITE profilePS500966.54733759IPR000048IQ motif, EF-hand binding site
SMARTSM0001551748770IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.998749778IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0027771793IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.608772796IPR000048IQ motif, EF-hand binding site
PfamPF006123.3E-4775792IPR000048IQ motif, EF-hand binding site
SMARTSM0001563851873IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.309853881IPR000048IQ 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: 899 aa     Download sequence    Send to blast
MEESRTRWLR PNEIHAMLCN YKYFTINVKP VYLPESGTIV LFDRKMLRNF RKDGHSWKKK  60
KDGKTVKEAH EHLKVGNVER IHVYYAHGQD NQTFVRRCYW LLDKSLEHIV LVHYRETQEL  120
QGSPATPVNS HSSSVSDQSA SRILSEEFDS GAARAYDFSE KDLRSSDNST VRSHAMRLHE  180
LNTLEWDELV TNDPGNSILP GGDKIPCFDQ HNHIAVNGSV NDGSTPSGYH LSAEISTLGI  240
LTESIVRSGN TQLNSPDSVY SQLTCAQVNT DAQRKGSIVL GTSDSLNNLV NDGLRSQDSF  300
GRWMSSILDH SPCSVDDAVL ESSISSGHDS FAPPGIDHHQ SSVQEQTFII TDFSPAWAFS  360
NETTKILVTG YFHEQYLNLA KSNLFCICGD AFVRAEIVQV GVYSCMLPSH SPGLVNFCLS  420
LDGLEPTSQI LNFEYRAPSV HDPVVSSEDK SKWEEFHLQM RLAYLLFSTS KTLDVLSNKL  480
SPTNLKEAKN FTRKTSNVSN SWAYLIKAIE DGEISVAQAK DGFFELSLKN TLKEWLSERI  540
LEGCKTTGYD AQGLGVIHLC AIIGYTWAVY LFSWSGLSLD FRDKHGWTAL HWAAYYGREK  600
MVAALLSAGA MPNLVTDPTK ENPGGCTAAD LASARGYDGL AAYLSEKALV AQFESMIIAG  660
NITGSLQTTA TDTVNSENLS EEELYLKDTL AAYRTAADAA ARIQVAFREH SLKVRTKAVQ  720
LSSPEDEARN IIAAMKIQHA FRNHDSKKKM AAAARIQHRF RTWKIRRDFL NMRHHAIKIQ  780
AVFRGFQVRR QFIKIIWSVG VLEKAVLRWR LKRRGFRGLR VEPVEAVVDQ THESDTEEDF  840
YKLSQKQAEE RVERSVIRVQ AMFRSKKAQE EYWRMKLTHK QAKVEYEGLL DSDMNVDR*
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
PlantRegMapSapurV1A.0050s0650.3.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_011009959.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X1
RefseqXP_011009967.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLB9HWX40.0B9HWX4_POPTR; Uncharacterized protein
STRINGPOPTR_0010s15160.10.0(Populus trichocarpa)
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]