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 AHYPO_018297-RA
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Caryophyllales; Amaranthaceae; Amaranthus
Family CAMTA
Protein Properties Length: 924aa    MW: 105278 Da    PI: 7.9795
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
AHYPO_018297-RAgenomeBYUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1162.48.1e-51291462118
             CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptf 94 
                      +ke k+rwl+++ei+aiL n++ ++++ ++ + pk g+++L++rkk+r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+np+f
  AHYPO_018297-RA  29 MKEaKSRWLRPNEIHAILFNYTYFDIKVKPVSLPKGGTIVLFDRKKLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGAEERIHVYYAHGEDNPSF 122
                      45559***************************************************************************************** PP

             CG-1  95 qrrcywlLeeelekivlvhylevk 118
                       rrcywlL+++le++vlvhy+e++
  AHYPO_018297-RA 123 VRRCYWLLDKALEHVVLVHYRETQ 146
                      *********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143773.6425151IPR005559CG-1 DNA-binding domain
SMARTSM010762.2E-7228146IPR005559CG-1 DNA-binding domain
PfamPF038592.2E-4431144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812964.67E-14378464IPR014756Immunoglobulin E-set
SuperFamilySSF484031.01E-18502672IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.205.1E-18560673IPR020683Ankyrin repeat-containing domain
CDDcd002041.53E-17560670No hitNo description
PROSITE profilePS5029715.857569670IPR020683Ankyrin repeat-containing domain
PfamPF127966.6E-8583673IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.461611643IPR002110Ankyrin repeat
SMARTSM002489.9E-6611640IPR002110Ankyrin repeat
SMARTSM002483300650679IPR002110Ankyrin repeat
SuperFamilySSF525404.25E-6724825IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.504759785IPR000048IQ motif, EF-hand binding site
SMARTSM0001591774796IPR000048IQ motif, EF-hand binding site
SMARTSM000151.9E-4797819IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.377798822IPR000048IQ motif, EF-hand binding site
PfamPF006123.7E-5799819IPR000048IQ motif, EF-hand binding site
SMARTSM0001513877899IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.535879907IPR000048IQ 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: 924 aa     Download sequence    Send to blast
MENRSNGLLA GCEIHGFRTM EDLDIFNIMK EAKSRWLRPN EIHAILFNYT YFDIKVKPVS  60
LPKGGTIVLF DRKKLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGAEERIH VYYAHGEDNP  120
SFVRRCYWLL DKALEHVVLV HYRETQEVSS ITPVNSSIHS DLSDHSASQL LSKGNNRLVD  180
QVYYPSTKEF GDSGDSINVT NHEIRLQEIN TLDWDELLMS NDLNQETIAT EGQSPYFQQD  240
KGLAKNFSEE NGMFSLTRNS QADVLSSRSS INPIVEICST HMGDMSLPLL KVQNDQKEES  300
RIYNTGTVGA GDFSDNMAKD GLLSQDSFGR WINEIIVDSP ESVEDPTYES SGATSHGSLV  360
SSGAVNNEGP VPSQIFCITD VSPSWAYSTE ETKILVVGFF HQEYQQLAKS NVYCVFGDTL  420
YPAEMIQAGV FRCLVSPHSC GFVNFFLSFD GRTPISQVLT FEFRAPASTN VVRREKSDWD  480
MFRIQIRLAH LLYSTSKSLD ILSNKISPTA LKEGKKFALK HSNISDNWAY FSKLIEYGKI  540
SFERAKDSLF ELSMKSRLKE WLLERVVDGS KILERDSEGQ GVLHLCAILG YKWAVNQFSC  600
CGLSLDFRDK FGWTALHWAA YYGRERMVAI LLSTGAKPNL VTDPTSENPG GCTAADLAAK  660
QGFEGLAAYL SEKALVQQFE DMRIAGNAVG SLETHIYESS TTSCVTEDDL YLKDTLAAYR  720
TAADAAARIQ VAFRENTLKK RTKDIEVSNP EREARYIVAA MKIQHAYRKY EVRKQMVAAA  780
RIQHRFKTWK LRKEFLNMRQ KAIKIQSVFR GFRVRREYRK ICWSVGVLEK AILRWRRKRR  840
GLCGLKIDLN EPADDQRSDS DTEEDFYRAS RKQAEERVEK AVVRVQAMFR SKQAQQEYRR  900
MKLAHTQAQL GYVEAIDPYD FLE*
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}.
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_021730253.10.0calmodulin-binding transcription activator 5-like 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]