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 FANhyb_rscf00000366.1.g00004.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae; Fragaria
Family CAMTA
Protein Properties Length: 1103aa    MW: 123110 Da    PI: 7.7021
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
FANhyb_rscf00000366.1.g00004.1genomekazusaView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-191.67.2e-292699375
                            CG-1  3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKv 75
                                    +e k rwl+++ei+a+L n++ ++++ ++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LK 
  FANhyb_rscf00000366.1.g00004.1 26 EEaKGRWLRPNEIHALLYNYKYFTIHVKPVNLPPSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKA 99
                                    45499********************************************************************7 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143743.7221152IPR005559CG-1 DNA-binding domain
SMARTSM010763.1E-3824331IPR005559CG-1 DNA-binding domain
PfamPF038591.3E-2427100IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.109.9E-4555644IPR013783Immunoglobulin-like fold
PfamPF018331.2E-5555641IPR002909IPT domain
SuperFamilySSF812962.16E-15556642IPR014756Immunoglobulin E-set
CDDcd002042.79E-15715849No hitNo description
Gene3DG3DSA:1.25.40.202.0E-16740853IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484037.0E-17751852IPR020683Ankyrin repeat-containing domain
PfamPF127962.9E-7752819IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.857757822IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008812.155790822IPR002110Ankyrin repeat
SMARTSM002482.4E-6790819IPR002110Ankyrin repeat
SMARTSM002484400829859IPR002110Ankyrin repeat
PROSITE profilePS500966.742938964IPR000048IQ motif, EF-hand binding site
SMARTSM0001588953975IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.181954983IPR000048IQ motif, EF-hand binding site
SMARTSM000150.097976998IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.0489771001IPR000048IQ motif, EF-hand binding site
PfamPF006120.022978998IPR000048IQ motif, EF-hand binding site
SMARTSM000151110561078IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.20610581086IPR000048IQ 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: 1103 aa     Download sequence    Send to blast
MDKPLVGSEI HGFHTMQDLD VDTIMEEAKG RWLRPNEIHA LLYNYKYFTI HVKPVNLPPS  60
GTIVLFDRKM LRNFRKDGHN WKKKKDGKTV KEAHEHLKAC YEADVHNGLK VRTSIRSPPS  120
GADDGAPPPE RIPKASPTTF PSRRDRFEGL GSNLHPKLQP RSISPENWNS ADSPGRESGR  180
GRLWCSSSFC SFSGAGPSSS ITLAFNLMPM ASEDGRSTAD RAGVPPFATV QRGHASTPAD  240
SSSVLDHFPS PASPPNSSFP ARLILFEVWG DLAEKLEFGG LTGEGKLVMK KGYMYTMPMV  300
RIAQPLSGGV IGCLISMSLE HIVLVHYRET QEVQGPATPV NSNSNSSSVS DPSAPWRLSE  360
ELDSGAKNSY YGGENELLEP GSGSTVNNHE QRLHDINTLE WDELLVTYDS RGDKVSGFDQ  420
QNQLVGNGTI SGGTSGLAAE VSSFGNLLNS SARTGSIHFD LPDSNYVQTL GGEVNSNAQR  480
RDSVVKGPCN SLNILGNDGL RSQDSFGRWI NQIMTDSPGS VDDHLLDSSF IAAQSSFTSP  540
AMEHIQSSVP EQIFIITDVS PSWAFSNEKT KILITGFFHQ EFLDLAKSNL LCICGDVCIP  600
AEIVQVGVYR CFIPPHVAGL VNLFISLDGH KPISQVLNFE YRSPVTSNSV VPSEENKWEE  660
FQLQMRLANL LFSSSKSLSI VSSKVSPYTL KEAKKFSHRT SHISNSWQYL IKSIEDNNTP  720
LPLAKDSLFE LILKNRLKDW LLEKVLDSSK TKEYDSHGQG VIHLCAILDY TWAVRLFSWS  780
GLSLDFRDRR GWTALHWAAY HGREKMVAVL LSAGAKPNLV TDPTSENPGG CTVADIASMN  840
GYDGLAAYLS EKALVEQFKD MSIAGNVSGS LQTNTNYYGN SENLSEEDLY LKDTLTAYQT  900
AADAAARIQA AIRENTLKLK TKAVQYSTPE DEARSIIAAL KIQHAFRHYD TRKKMAAAAR  960
IQYRFRTWKM RQEFLNMRRQ AVKIQAAFRA FQTRRQYQKI LWGVGVLEKA VLRWRLKRKG  1020
LRGLQVDPIE ANGDEKQESD TEEDFYRNSR KQAEERVERS VVRVQAMFRS KKAQQEYRRM  1080
KLTHNETKLE YDDFFDPDNS MRG
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}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_004295103.10.0PREDICTED: calmodulin-binding transcription activator 5
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2P6QYW40.0A0A2P6QYW4_ROSCH; Putative transcription factor CG1-CAMTA family
STRINGXP_004295103.10.0(Fragaria vesca)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF42883459
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]