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 MDP0000233860
Organism
Malus domestica
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Malus
Family CAMTA
Protein Properties Length: 866aa    MW: 98732.2 Da    PI: 8.0746
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
MDP0000233860genomeGDRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1165.31e-51261423118
           CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrr 97 
                    +e k+rwl+++ei+aiL n++ ++++ ++ + pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+ ptf rr
  MDP0000233860  26 EEaKSRWLRPNEIHAILYNHKYFTIHVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERVHVYYAHGEDSPTFVRR 121
                    4559******************************************************************************************** PP

           CG-1  98 cywlLeeelekivlvhylevk 118
                    cywlL+++le+ivlvhy+e++
  MDP0000233860 122 CYWLLDKSLEHIVLVHYRETQ 142
                    ******************986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.36221147IPR005559CG-1 DNA-binding domain
SMARTSM010762.0E-7624142IPR005559CG-1 DNA-binding domain
PfamPF038596.2E-4627140IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.102.3E-4316408IPR013783Immunoglobulin-like fold
SuperFamilySSF812964.83E-14318405IPR014756Immunoglobulin E-set
CDDcd002042.63E-12478612No hitNo description
Gene3DG3DSA:1.25.40.201.8E-16502615IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484034.04E-16515615IPR020683Ankyrin repeat-containing domain
PfamPF127964.1E-7515582IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.167520585IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.621553585IPR002110Ankyrin repeat
SMARTSM002489.2E-6553582IPR002110Ankyrin repeat
PROSITE profilePS500967.309701727IPR000048IQ motif, EF-hand binding site
SMARTSM0001521716738IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.54717746IPR000048IQ motif, EF-hand binding site
SMARTSM000150.022739761IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.164740764IPR000048IQ motif, EF-hand binding site
PfamPF006127.7E-4741761IPR000048IQ motif, EF-hand binding site
SMARTSM0001537819841IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.876820849IPR000048IQ 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: 866 aa     Download sequence    Send to blast
MENQLVGSEI HGFHTMQDLD VPTIMEEAKS RWLRPNEIHA ILYNHKYFTI HVKPVNLPKS  60
GTIVLFDRKM LRNFRKDGHN WKKKKDGKTV KEAHEHLKVG NEERVHVYYA HGEDSPTFVR  120
RCYWLLDKSL EHIVLVHYRE TQEVVQGSPV TPVNSNSSSV SDPSAPWFLS EELDSGANNA  180
YCAGENELPE LGDRLTVNNH EQRLHDINTL EWEELLVTND SXEKPDNISG YDQQNQVVGN  240
GSNSGRRDSI AKEDKTVLDT NGLHSQDSFG RWINEIMTDS QPSVEDPVLG SSLSAAQNSF  300
ASPAMDHLQS SVPQQIFNIT DISPTWAFSN EKTKILITGF LHKEFFHLAK SDLLCVCGDV  360
CLRAEIIQTG VYRCFVPPHL PRIVNLFMSI DGHKPISQVL NFEYRAPVLS DTVVSSEDNK  420
WEEFQVQMRL AYLLFSSSKS LNIISNKVPP NALKEAKKFS HRTSHISNSW PYLMKAIEEN  480
KTPLPLAKDS LFELILRNRL KDWLLEKVVE VSKTKEYDAH GQGVIHLCAI LEYTWAVRLF  540
SWSGLSLDFR DKRGWTALHW AAYCGREKMV AVLLSAGAKP NLVTDPTKDN PGGSNAADLA  600
FMKGHDGLAA YLSEXALVEQ FKDMRMAGNA SGSLEIRSNY AANSENLSEE ELYLKDTLAA  660
YRTAADAAAR IQAAFRENSL KQKTKAIQYS IPEAEARGII AALKIQHAFR NYEAKKKIKA  720
AAHIQYRFRT WKMRQEFLSL RRQAIKIQAA FRGFQVRRQY RKVLWSVGVL EKAVLRWRFK  780
RRGLRGLKVA PAEVSADXNP ESDTEEDFYR ASRKQAEERI ERSVVRVQAM FRSKKAQQEY  840
SRMKMAHNEA TLEFDDFLDP DAIMDN
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Mdo.165400.0root| stem
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Expressed in roots, stems, leaves, pollen, top of sepals and siliques. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
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_028951238.10.0calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A498HK700.0A0A498HK70_MALDO; Uncharacterized protein
STRINGXP_008368335.10.0(Malus domestica)
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]