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 XP_011100792.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Pedaliaceae; Sesamum
Family CAMTA
Protein Properties Length: 901aa    MW: 102078 Da    PI: 7.4578
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_011100792.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-11666.3e-5221192118
            CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfq 95 
                     ++e k+rwl+++ei+aiL n++ +++  ++ + pksg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+nptf 
  XP_011100792.1   2 MEEaKARWLRPNEIHAILCNHKYFTVYVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDNPTFV 96 
                     45669****************************************************************************************** PP

            CG-1  96 rrcywlLeeelekivlvhylevk 118
                     rrcywlL+++le+ivlvhy+e++
  XP_011100792.1  97 RRCYWLLDKSLEHIVLVHYRETQ 119
                     ********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM010763.5E-771119IPR005559CG-1 DNA-binding domain
PROSITE profilePS5143777.5841124IPR005559CG-1 DNA-binding domain
PfamPF038596.7E-464117IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.08E-9354439IPR014756Immunoglobulin E-set
CDDcd002041.25E-13538648No hitNo description
SuperFamilySSF484033.26E-16539652IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.9E-15539651IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.345547621IPR020683Ankyrin repeat-containing domain
SMARTSM002485.1E-6589618IPR002110Ankyrin repeat
PROSITE profilePS5008811.434589621IPR002110Ankyrin repeat
PfamPF000238.9E-5590620IPR002110Ankyrin repeat
SuperFamilySSF525405.31E-8696803IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.163737763IPR000048IQ motif, EF-hand binding site
SMARTSM0001514752774IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.089756782IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0012775797IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.091776800IPR000048IQ motif, EF-hand binding site
PfamPF006129.8E-4777797IPR000048IQ motif, EF-hand binding site
SMARTSM0001535855877IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.114857885IPR000048IQ 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: 901 aa     Download sequence    Send to blast
MMEEAKARWL RPNEIHAILC NHKYFTVYVK PVNLPKSGTI VLFDRKMLRN FRKDGHNWKK  60
KKDGKTVKEA HEHLKVGNEE RIHVYYAHGE DNPTFVRRCY WLLDKSLEHI VLVHYRETQE  120
LQGSPATPVN SNSNSAGSDL SATWPMSEES DSAVDRVYYG STGSYLECHD SVTVKHHEQR  180
LYEINTLEWD ELLVPDDPHR LITRQQGTTA GFELQNQYQM NSYRINDDAP SNNKVSPECS  240
TNSFSEPVAG RSSINYTSPN NMSYQTVEQD TIVNSETMVS GLMPSGGAGS LYNLGKDGLQ  300
SQDSFGRWVT HIIAESPESV DDHTLESSNL AGHQSSTYPL MDSHDSSPLG PIFTITDVSP  360
AWALSTEETK ILVVGFFNEG QLPYSESKLY LACGDSLLPV DVVQAGVFRC LIPPQAPKLG  420
NLYITFDGHK PISQVLTFEI RAPVQPGTVS FENKTDWEEF QLQMRLAHLL FSSSKGLSIY  480
STKLSPTALK EAKAFAQKTS HISDGWLHMA KVIEDTKMSF PQAKDKLFEL TLQNRLQEWL  540
LEKVVAGCKI SERDEQGLGV IHLCSILGYT WAVYPYSWSG LSLDYRDKFG WTALHWAAYY  600
GREKMVATLL SAGAKPNLVT DPTSQNPGGC SAHDLASKNG YDGLAAYLAE KALVAQFDDM  660
TLAGNVSGSL QTTTNETVNP GNFSEDELYL KDTLAAYRTA ADAAARIQTA FREHSLKIRT  720
KVVESSNPEL EARNIVAAMK IQHAFRNYET RKKIVAAARI QHRFRTWKIR KEFLNMRRQA  780
IKIQAMFRGF QVRRQYRKIV WSVGVLEKAI LRWRLKRKGF RGLQVQPAET PREPNEESDV  840
EEDFFQASRK QAEERVEQSV VRVQAMFRSK QAQEAYRRMK LEHNKAKLEY EGLLHPDLQM  900
G
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
Cis-element ? help Back to Top
SourceLink
PlantRegMapXP_011100792.1
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_011100788.10.0calmodulin-binding transcription activator 5 isoform X1
RefseqXP_011100789.10.0calmodulin-binding transcription activator 5 isoform X1
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A022RYH30.0A0A022RYH3_ERYGU; Uncharacterized protein
STRINGMigut.G00093.1.p0.0(Erythranthe guttata)
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]