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 Pbr011973.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Pyrus
Family CAMTA
Protein Properties Length: 915aa    MW: 102963 Da    PI: 7.1159
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Pbr011973.1genomeCPETRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1161.21.9e-50301443117
         CG-1   3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcyw 100
                  + k+rwl+++ei+aiL n++ ++++l++ + pksg+++L++rk +r+frkDG++wkkk dgktv+E+he+LKvg+ e +++yYah+e+ ptf rrcyw
  Pbr011973.1  30 EAKSRWLRPNEIHAILYNYKYFTVHLKPVNLPKSGTIVLFDRKLLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERVHVYYAHGEDSPTFVRRCYW 127
                  459*********************************************************************************************** PP

         CG-1 101 lLeeelekivlvhylev 117
                  lL+++le+ivlvhy+e+
  Pbr011973.1 128 LLDKSLEHIVLVHYRET 144
                  ***************97 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143773.9224150IPR005559CG-1 DNA-binding domain
SMARTSM010769.4E-7128145IPR005559CG-1 DNA-binding domain
PfamPF038598.7E-4530143IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.106.1E-6364456IPR013783Immunoglobulin-like fold
SuperFamilySSF812961.5E-14366453IPR014756Immunoglobulin E-set
PfamPF018332.0E-5367452IPR002909IPT domain
CDDcd002041.12E-12526660No hitNo description
Gene3DG3DSA:1.25.40.201.3E-15550663IPR020683Ankyrin repeat-containing domain
PfamPF127969.9E-7563630IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.03E-15563663IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.035568660IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.621601633IPR002110Ankyrin repeat
SMARTSM002489.2E-6601630IPR002110Ankyrin repeat
PROSITE profilePS500966.98749775IPR000048IQ motif, EF-hand binding site
SMARTSM0001542764786IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.87765794IPR000048IQ motif, EF-hand binding site
SMARTSM000150.097787809IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.743788812IPR000048IQ motif, EF-hand binding site
PfamPF006120.0023790809IPR000048IQ motif, EF-hand binding site
SMARTSM0001519867889IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.602869897IPR000048IQ 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: 915 aa     Download sequence    Send to blast
MHSTFGEQPS CWLSSYNESS DLDVATTMEE AKSRWLRPNE IHAILYNYKY FTVHLKPVNL  60
PKSGTIVLFD RKLLRNFRKD GHNWKKKNDG KTVKEAHEHL KVGNEERVHV YYAHGEDSPT  120
FVRRCYWLLD KSLEHIVLVH YRETREGSPV TPVNSNSSSV SDPSAPSSLS EEHDSVANNA  180
YCAGENELQE LGDGLTVNNH EQRLHDINTL EWDELLVKND SKGDNISGYD QQNQVVGNGS  240
ISGGASSLSA EISSFGNLTN LTAGSENIQF NLSGTPCVET LLGDVNSNVQ RRDFIAKATC  300
GSVDVLHNNG LHSQDSFGRW INQIMTESTA SVEDPVLDCS FSAAQNSFAS PTMDHLQSSV  360
PQQIFNITDI SPTWAFSNEK TKILITGFLH QEFFQLAKSD LLCVCGDVCL PAEIVQAGVY  420
RCFVPPHSPR VVNLFMSIDG HKPISQELNF EYRAPVLSDT LVSSEGNKRE EFQVQMRLAY  480
LLFSSSHSLN IISSKVPPNA LKEAKKFSHR TSHMSNHWPY LMKAVEDNKT PLPLAKDSLF  540
ELILKNRLKD WLLEKVVQVS KTKEYDAHGL GVIHLCAILE YTWAVRLFSW SGLSLDFRDR  600
RGWTALHWAA YCGREKMVAV LLSAGAKPNL VTDPTPDNPG GSTAADFASM KGYDGLAAYL  660
SEKALVEQFN AMSVAGNVSG SLEISSSYAA NSENLSEEDL YLKDTLAAYR TTADAAARIQ  720
AAFRENSLKQ KTKAVQYSTP EAEARGIIAA LKIQHAFRNY ETKKKIQAAA RIQYRFRTWK  780
MRQDFLSLRR QTIKIQAAFR GFQVRRQYRK VLWSVGVLEK AVLRWRFKRR GLRGLNVAPA  840
EVSVDQVQES DTEEDFYRAS QKQAEERVER SVIRVQAMFR SKKAQEEYAR MKMAHNQATL  900
EFDDFLDPDA IMDN*
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
17086RKLLRNFRKDGHNWKKK
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
PlantRegMapPbr011973.1
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
PlantRegMap-Retrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_018505906.10.0PREDICTED: calmodulin-binding transcription activator 5 isoform X2
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A498IFY70.0A0A498IFY7_MALDO; Uncharacterized protein
STRINGXP_009369951.10.0(Pyrus x bretschneideri)
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]