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 Cotton_A_34645_BGI-A2_v1.0
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium
Family CAMTA
Protein Properties Length: 907aa    MW: 102260 Da    PI: 7.1411
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Cotton_A_34645_BGI-A2_v1.0genomeBGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1135.41.9e-42291392118
                        CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlyc 83 
                                 ++e k+rwl+++ei+aiL n++ + +  ++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++
  Cotton_A_34645_BGI-A2_v1.0  29 MEEaKSRWLRPNEIHAILSNYKYFPILVKPVNLPQSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHV 111
                                 55669****************************************************************************** PP

                        CG-1  84 yYahseenptfqrrcywlLeeelekivlvhylevk 118
                                 yYah+ +nptf rr+        e+ivlvhy+e+k
  Cotton_A_34645_BGI-A2_v1.0 112 YYAHGLDNPTFVRRTL-------ENIVLVHYRETK 139
                                 *************976.......68*******985 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143761.91325144IPR005559CG-1 DNA-binding domain
SMARTSM010765.2E-6428139IPR005559CG-1 DNA-binding domain
PfamPF038591.9E-3731137IPR005559CG-1 DNA-binding domain
SuperFamilySSF812962.94E-12354439IPR014756Immunoglobulin E-set
SuperFamilySSF484032.02E-18526650IPR020683Ankyrin repeat-containing domain
PfamPF127961.1E-7539618IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.1E-17541651IPR020683Ankyrin repeat-containing domain
CDDcd002041.41E-15544648No hitNo description
PROSITE profilePS5029716.069556660IPR020683Ankyrin repeat-containing domain
SMARTSM002481.7E-6589618IPR002110Ankyrin repeat
PROSITE profilePS5008812.155589621IPR002110Ankyrin repeat
SMARTSM002482700628659IPR002110Ankyrin repeat
SMARTSM00015210733755IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.815737763IPR000048IQ motif, EF-hand binding site
SMARTSM000156.1E-4775797IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.402776800IPR000048IQ motif, EF-hand binding site
PfamPF006125.1E-4777797IPR000048IQ motif, EF-hand binding site
SMARTSM000159855877IPR000048IQ motif, EF-hand binding site
PfamPF006120.077857877IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.206857884IPR000048IQ 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: 907 aa     Download sequence    Send to blast
MDGSGSGQLA GTEIHGFHTL EDLDVRTMME EAKSRWLRPN EIHAILSNYK YFPILVKPVN  60
LPQSGTIVLF DRKMLRNFRK DGHNWKKKKD GKTVKEAHEH LKVGNEERIH VYYAHGLDNP  120
TFVRRTLENI VLVHYRETKE GSPATPVNSN SCLTTDQSTP LLVTEDFDSG AANAYYEDLS  180
DSIKANHEMT LHEINTLEWD ELLVTNDSND SAVSSGDMNA CFDQWNQKTV NGLSNDGGPI  240
SAYNSSPDIS LLDNLVDPVA QSNNAYLNTR GGVCYQTPGT EVNSTMQRED SSAIGMGKPL  300
DLLINNGLES QDSFGKWINC TVTESPCSMG DPVLESSSSS GQDSFTSPEE IFSITEVSPA  360
WAYSTEKTKI LVTGVFHQAY QHLAKSNLFC VCGDVCYPAE AIQVGVYRCL LSQHAPGLVK  420
LYMSLDGHKP ISQVLNFEYI APLLHDPVVP LEDKSRWEEF RLQMRLAYLL FSTSKSLNIL  480
SGKVSPNSLK EAKKFAQKTS NISNSWTYLI QSIEENRASF TQAKDSLFEI ALKNRLKDWL  540
LERIIYGSKT TEYDAQGQGV IHLCAILGYT WAIYLFSWSG LSLDFRDKHG WTALHWAAYY  600
GREKMVAVLL SAGAKPNLVT DPTTQNPSGC TAADLASLNG YDGLAAYLSE EALVAQFNDM  660
ALAGNASGSL QTSRIEATNL VNLNEDELYL RETLAAYRTA ADAAARINTA FRAHSFKVRA  720
KAVESYNAED EARSIIAAMK IQHAFRNYEA KRKMAAAARI QYRFRTWKMH KDFLNMRRQA  780
IKIQAAFRGF QARRQYRKIV WSVGVLEKAI LRWRLRRKGF RGLQITTDEA VEEQRQETYI  840
EEAYYISSRK QAEERVEKAV IRVQSMFRSK KAQQEYRRMK LAHDLATLEY ESLIGPLSDM  900
MPKDHRN
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 -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankJX5884741e-130JX588474.1 Gossypium hirsutum clone NBRI_GE22909 microsatellite sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_017649374.10.0PREDICTED: calmodulin-binding transcription activator 5-like isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A1U8IGT60.0A0A1U8IGT6_GOSHI; calmodulin-binding transcription activator 5-like
STRINGGorai.011G198600.10.0(Gossypium raimondii)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM40212758
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]