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 Sp_174400_uesu.t2
Common NameSOVF_174400
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia
Family CAMTA
Protein Properties Length: 931aa    MW: 105947 Da    PI: 7.9062
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Sp_174400_uesu.t2genomeTBVRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1164.71.6e-51291462118
               CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenp 92 
                        +ke k+rwl+++ei+aiL n+++++++ ++ + p+ g+++L++rkk+r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+np
  Sp_174400_uesu.t2  29 MKEaKSRWLRPNEIHAILFNYTNFTIHVKPVSLPRGGTIVLFDRKKLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGTEERIHVYYAHGEDNP 120
                        45559*************************************************************************************** PP

               CG-1  93 tfqrrcywlLeeelekivlvhylevk 118
                        +f rrcywlL+++le+ivlvhy+e++
  Sp_174400_uesu.t2 121 KFVRRCYWLLDKALEHIVLVHYRETQ 146
                        ***********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143775.68925151IPR005559CG-1 DNA-binding domain
SMARTSM010761.3E-7128146IPR005559CG-1 DNA-binding domain
PfamPF038592.4E-4531144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812965.74E-12383469IPR014756Immunoglobulin E-set
CDDcd002041.84E-15566676No hitNo description
Gene3DG3DSA:1.25.40.204.2E-15566679IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484037.31E-16567679IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029713.39575649IPR020683Ankyrin repeat-containing domain
SMARTSM002482.9E-5617646IPR002110Ankyrin repeat
PROSITE profilePS500889.858617649IPR002110Ankyrin repeat
PfamPF136378.7E-5619674No hitNo description
SuperFamilySSF525404.51E-7730831IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.272765791IPR000048IQ motif, EF-hand binding site
SMARTSM0001520780802IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.492781810IPR000048IQ motif, EF-hand binding site
SMARTSM000152.0E-4803825IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.56804828IPR000048IQ motif, EF-hand binding site
PfamPF006122.1E-4805825IPR000048IQ motif, EF-hand binding site
SMARTSM0001513883905IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.297885913IPR000048IQ 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: 931 aa     Download sequence    Send to blast
MESGFNGGLG GYDIHGFRTM EDLDVPNIMK EAKSRWLRPN EIHAILFNYT NFTIHVKPVS  60
LPRGGTIVLF DRKKLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGTEERIH VYYAHGEDNP  120
KFVRRCYWLL DKALEHIVLV HYRETQESQV SPSTPTNSSF RSDLTDYSAS QLLSRGNDCV  180
VNQVYYPSMK ERTEFGDGVS MNNLDMRLHE INTLDWDELL VSNNPTEATL TTREQNPYLQ  240
QDKQPSTFSS ENNGSSLLTG HPHPGMLTSR NSMNPVADTS LAQVTHVGDM FLPLTVVQTH  300
QKEEGRIYGM GAVGAGDLSD KMAKDGLQSQ DSFGKWMNEI IVDSPESVGD PSFESSLETS  360
HGSLMSSGAV NHEGPYPAQI FCITDISPTW AYSTEETKIL VVGFYHQEYR QLAKATVYCV  420
CGDTCVPAEI IQVGVFRCMV SPQSPGSVNF YLSIDCSTPI SQVLTFEFRS PAMTNPVVRQ  480
DKSQWDMFRI QMRLAYLLFT TSKSLDILSS KVSQSALKEG KKFALKYSNT ADSWAYFTKL  540
TESGKITFER AKDNLFELSM KSRLKEWLLE RVVGGSKISE RDAEGQGVLH LCAILDYTWA  600
VYPFSCCGLS LDFRDKFGWT ALHWAAYYGR EKMVAALLSA RAKPNLVTDP TSENPGGCTS  660
ADLAAKQGFE GLAAYLSEKA LVQQFEDMRI AGNAGGSLET QTYETSNANN ITEEELDLKD  720
TLTAYRTAAD AAARIQVAFR EQTLKQRSKI VEFLNPETEA QYIVAAMKIQ HAFRNYELRK  780
QMAAALRIQH RFRTWKLRKD FLNMRRKVIK IQAAFRGFLL RQQYQKFVWS VGVLEKAILR  840
WRLRRKGFRG LKVEIQEPVD DQRQESDTEE DFYRASRKQA EERVEKAVVR VQSMFRSKQA  900
QQEYRRMKLA HTQAQLEFED SVNPNGFMNE M
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
17188RKKLRNFRKDGHNWKKKK
27287KKLRNFRKDGHNWKKK
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_021835012.10.0calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A0K9QKS60.0A0A0K9QKS6_SPIOL; Uncharacterized protein
STRINGXP_010671665.10.0(Beta vulgaris)
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]