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 SapurV1A.0050s0650.2.p
Organism
Salix purpurea
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: 927aa    MW: 104437 Da    PI: 7.072
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
SapurV1A.0050s0650.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1164.51.8e-51301463118
                    CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahs 88 
                             +e ++rwl+++ei+a+L n++ +++  ++   p+sg+++L++rk++r+frkDG+swkkkkdgktv+E+he+LKvg+ve +++yYah+
  SapurV1A.0050s0650.2.p  30 EEsRTRWLRPNEIHAMLCNYKYFTINVKPVYLPESGTIVLFDRKMLRNFRKDGHSWKKKKDGKTVKEAHEHLKVGNVERIHVYYAHG 116
                             4459*********************************************************************************** PP

                    CG-1  89 eenptfqrrcywlLeeelekivlvhylevk 118
                             ++n+tf rrcywlL+++le+ivlvhy+e++
  SapurV1A.0050s0650.2.p 117 QDNQTFVRRCYWLLDKSLEHIVLVHYRETQ 146
                             ***************************986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143774.76125151IPR005559CG-1 DNA-binding domain
SMARTSM010762.1E-7328146IPR005559CG-1 DNA-binding domain
PfamPF038599.3E-4532144IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.106.2E-4373466IPR013783Immunoglobulin-like fold
PfamPF018332.5E-5377463IPR002909IPT domain
SuperFamilySSF812964.76E-13378464IPR014756Immunoglobulin E-set
SuperFamilySSF484032.95E-16567675IPR020683Ankyrin repeat-containing domain
CDDcd002046.52E-15568672No hitNo description
Gene3DG3DSA:1.25.40.206.0E-15571675IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.902580645IPR020683Ankyrin repeat-containing domain
PfamPF127962.9E-6580642IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.354613645IPR002110Ankyrin repeat
SMARTSM002481.1E-5613642IPR002110Ankyrin repeat
PROSITE profilePS500966.54761787IPR000048IQ motif, EF-hand binding site
SMARTSM0001551776798IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.998777806IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0027799821IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.608800824IPR000048IQ motif, EF-hand binding site
PfamPF006123.4E-4803820IPR000048IQ motif, EF-hand binding site
SMARTSM0001563879901IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.309881909IPR000048IQ 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: 927 aa     Download sequence    Send to blast
MESGFSDRLI GSEIHGFHTL RDLDVSNIME ESRTRWLRPN EIHAMLCNYK YFTINVKPVY  60
LPESGTIVLF DRKMLRNFRK DGHSWKKKKD GKTVKEAHEH LKVGNVERIH VYYAHGQDNQ  120
TFVRRCYWLL DKSLEHIVLV HYRETQELQG SPATPVNSHS SSVSDQSASR ILSEEFDSGA  180
ARAYDFSEKD LRSSDNSTVR SHAMRLHELN TLEWDELVTN DPGNSILPGG DKIPCFDQHN  240
HIAVNGSVND GSTPSGYHLS AEISTLGILT ESIVRSGNTQ LNSPDSVYSQ LTCAQVNTDA  300
QRKGSIVLGT SDSLNNLVND GLRSQDSFGR WMSSILDHSP CSVDDAVLES SISSGHDSFA  360
PPGIDHHQSS VQEQTFIITD FSPAWAFSNE TTKILVTGYF HEQYLNLAKS NLFCICGDAF  420
VRAEIVQVGV YSCMLPSHSP GLVNFCLSLD GLEPTSQILN FEYRAPSVHD PVVSSEDKSK  480
WEEFHLQMRL AYLLFSTSKT LDVLSNKLSP TNLKEAKNFT RKTSNVSNSW AYLIKAIEDG  540
EISVAQAKDG FFELSLKNTL KEWLSERILE GCKTTGYDAQ GLGVIHLCAI IGYTWAVYLF  600
SWSGLSLDFR DKHGWTALHW AAYYGREKMV AALLSAGAMP NLVTDPTKEN PGGCTAADLA  660
SARGYDGLAA YLSEKALVAQ FESMIIAGNI TGSLQTTATD TVNSENLSEE ELYLKDTLAA  720
YRTAADAAAR IQVAFREHSL KVRTKAVQLS SPEDEARNII AAMKIQHAFR NHDSKKKMAA  780
AARIQHRFRT WKIRRDFLNM RHHAIKIQAV FRGFQVRRQF IKIIWSVGVL EKAVLRWRLK  840
RRGFRGLRVE PVEAVVDQTH ESDTEEDFYK LSQKQAEERV ERSVIRVQAM FRSKKAQEEY  900
WRMKLTHKQA KVEYEGLLDS DMNVDR*
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.0050s0650.2.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_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]