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_000797-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: 926aa    MW: 105340 Da    PI: 7.986
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
AHYPO_000797-RAgenomeBYUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11642.6e-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+ p+f
  AHYPO_000797-RA  29 MKEaKSRWLRPNEIHAILFNYTYFDIHVKPVSLPKGGTIVLFDRKKLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGTEERIHVYYAHGEDSPNF 122
                      45559***************************************************************************************** PP

             CG-1  95 qrrcywlLeeelekivlvhylevk 118
                       rrcywlL+++le+ivlvhy+e++
  AHYPO_000797-RA 123 VRRCYWLLDKALEHIVLVHYRETQ 146
                      *********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143775.51525151IPR005559CG-1 DNA-binding domain
SMARTSM010769.3E-7328146IPR005559CG-1 DNA-binding domain
PfamPF038596.9E-4531144IPR005559CG-1 DNA-binding domain
SuperFamilySSF812962.8E-12378464IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.202.3E-17560674IPR020683Ankyrin repeat-containing domain
CDDcd002041.84E-17560670No hitNo description
SuperFamilySSF484034.82E-18561673IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.831569670IPR020683Ankyrin repeat-containing domain
PfamPF127966.9E-7583673IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.381611643IPR002110Ankyrin repeat
SMARTSM002483.4E-6611640IPR002110Ankyrin repeat
SMARTSM002483000650679IPR002110Ankyrin repeat
SuperFamilySSF525404.6E-6723825IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.668759783IPR000048IQ motif, EF-hand binding site
SMARTSM0001524774796IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.87775804IPR000048IQ motif, EF-hand binding site
SMARTSM000150.012797819IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908798822IPR000048IQ motif, EF-hand binding site
PfamPF006125.2E-4799819IPR000048IQ motif, EF-hand binding site
SMARTSM0001513877899IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.297879907IPR000048IQ 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: 926 aa     Download sequence    Send to blast
MENRSNGLLG GCEIHGFRTM EDLDIPNIMK EAKSRWLRPN EIHAILFNYT YFDIHVKPVS  60
LPKGGTIVLF DRKKLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGTEERIH VYYAHGEDSP  120
NFVRRCYWLL DKALEHIVLV HYRETQEASP ITPVDSGFRS DLSEYSASQL LSRGNETLVN  180
KVYYPAMKDL TESGESINVT NHEIQLHEIN TLDWDELLVS NDLNEATFIS KEQTPCLQQD  240
KHPAVNISKN NGDFLLTRTP HPDLLTSRNS MKPTPEISSS HMGDKFLPLF GLQTNQKDDS  300
RVCNMGTVDD RNFSDRMDKD GLLSQDSLGR WMNEIIVDSP ESVNDPSYES SVATSHGSIV  360
SSAAVDHEGP VPAQIFCITD VSPSWAYSTE ETKILVVGFF HQEYQHLAKS TIYCVCGDTL  420
YPAEIIQVGV FRCLVSPHSF GSVNFYLSID GKTPISQILT FEFRAPASTN VVRKDNSQWN  480
MFRIQIRLAH LLYSTSKSLD ILSSNISPSS LKEGKNFALK YSNISDSWAY FSKLIESGKI  540
SFDRAKDCLF ELSMKSRLKE WLLERVVDGS KISERDTEGQ GVLHLCAILG YTWAVYPFSC  600
CGLSLDFRDK FGWTALHWAA YYGREKMVAA LLSAGAKPNL VTDPTSDNPG GCTAADVAAK  660
QGFEGLAAYL SEKSLVQQFE DMKIAGNAGG SLETHTYESQ ITSDITEEDL YLKDTLAAYR  720
TAADAAARIQ VAFRETTLKQ RTKAVEGSNP ESEARYIVAA MKIQHAYRNY EVRKQIAAAA  780
RIQFRFRTWK LRKDFLNKRR QAIKIQAIFR GFRVRREYRK ITWSVGVLEK AILRWRRKRR  840
GFCGLKVEIK EPSDDQKRES DTEEDFYRAS RKQAEERVEK AVVRVQSMFR SKQAQQEYRR  900
MKLAHTQAQL GYGEAVDPYD FLSEM*
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]