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 EcC053945.20
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus
Family CAMTA
Protein Properties Length: 891aa    MW: 99492.9 Da    PI: 6.8817
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
EcC053945.20genomeECGDView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1168.41.1e-52211362116
          CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrr 97 
                   ++e + rwlk+ e++ iL+n+e+ +lt+++++rp+sgsl+L+n++++r+fr+DG++w+kkkd +tv E+he+LKvg+ve l+cyYah+e+np+fqrr
  EcC053945.20  21 YQEaQYRWLKPAEVLYILQNHESCQLTQQPPERPSSGSLFLFNKRVLRFFRRDGHNWRKKKDQRTVGEAHERLKVGNVEKLNCYYAHGEDNPNFQRR 117
                   566699******************************************************************************************* PP

          CG-1  98 cywlLeeelekivlvhyle 116
                   +yw+L+ + ++ivlvhy++
  EcC053945.20 118 SYWMLDPACDHIVLVHYRD 136
                   *****************98 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.9817143IPR005559CG-1 DNA-binding domain
SMARTSM010762.9E-7520138IPR005559CG-1 DNA-binding domain
PfamPF038591.9E-4723136IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.101.2E-10357445IPR013783Immunoglobulin-like fold
SuperFamilySSF812969.52E-20361445IPR014756Immunoglobulin E-set
CDDcd001022.14E-6361445No hitNo description
PfamPF018331.8E-10361444IPR002909IPT domain
Gene3DG3DSA:1.25.40.202.2E-16558654IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.069559651IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484035.44E-16562654IPR020683Ankyrin repeat-containing domain
CDDcd002042.11E-13564651No hitNo description
PfamPF127963.3E-9571653IPR020683Ankyrin repeat-containing domain
SMARTSM002489.3E-4592621IPR002110Ankyrin repeat
PROSITE profilePS5008811.033592624IPR002110Ankyrin repeat
SMARTSM002481300631660IPR002110Ankyrin repeat
SMARTSM000157709731IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.712710739IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525402.66E-9750813IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000150.17761783IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.224762791IPR000048IQ motif, EF-hand binding site
PfamPF006120.025764782IPR000048IQ motif, EF-hand binding site
SMARTSM000153.8E-4784806IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.993786809IPR000048IQ motif, EF-hand binding site
PfamPF006122.7E-5787806IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006810Biological Processtransport
GO:0005634Cellular Componentnucleus
GO:0005829Cellular Componentcytosol
GO:0003677Molecular FunctionDNA binding
GO:0005515Molecular Functionprotein binding
Sequence ? help Back to Top
Protein Sequence    Length: 891 aa     Download sequence    Send to blast
MKVLSILLFS EFSGYNISDL YQEAQYRWLK PAEVLYILQN HESCQLTQQP PERPSSGSLF  60
LFNKRVLRFF RRDGHNWRKK KDQRTVGEAH ERLKVGNVEK LNCYYAHGED NPNFQRRSYW  120
MLDPACDHIV LVHYRDINEG KHSSGSKALF SPGSSAALSP SPSPSPYSNQ NQGSASLDSC  180
QTHSSPSSAE VSSINAIINH GTDNLDGVEG AALCSSSDLD VSKALRRIEE QLSLNDDAIK  240
EIVPVFDDDE YFNSVGLLDY EREISQQDQH EALLQVSDPV NCQFLSENDG VRNVSSNYMP  300
LKDTVASLLE LDNFEVSAYP SFGETHGANP EYYPVSFGQG QPGTSVVGNS CLTVVKTQKY  360
TIREISPEWG YTTEATKIVI VGSFLCDPSE SVWSCMFGDI EVPVEIIQQG VIRCEAPPHS  420
PGKVTLCITS SNRQSCSEVR EFEYRVKSNF CAHCNLEQTK AARHTEELLL LVRFVQMLLC  480
DSAMQKEDGV TLGIHVPRNS KAEDDPWSHI IDGLLVGHEN SSETSNWLLQ ELLKDKLQQW  540
IALRSRQEHD QGGCFLSKKE QGIIHMIAGL GFEWALNSIL GCGVNVNFRD INGWTALHWA  600
ARFGREKMVA ALVASGASAG AVTDPRCQDP AGKTPASIAA SSGHKGLAGY LSEQALTSHL  660
SSLTVKESEL SRGSAELEAE RTINSITNQT LATDEDQLSL KDTLAAVRNA TQAAARIQSA  720
FRAHSFRKRQ QMQVAAAIDD YGSSGDIQGF TGMLKLSSRN TRDSAALSIQ KKFRGWKGRK  780
DFLRFRQKVV KIQAHVRGYQ VRKHYKVLCW AVGILDKVVL RWRRKGVGLR SFQKEAESIE  840
DSDDEDILKV FRKQKVDATV DEAVSRVLGM VDSPNARQQY RRMLERYRQA K
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator that 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 together with CAMTA2 and CAMTA3 in the positive regulation of a general stress response (PubMed:25039701). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:25039701, ECO:0000305|PubMed:11925432}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, salt, wounding, ethylene, methyl jasmonate, abscisic acid, H(2)O(2) and salicylic acid (PubMed:12218065). Induced by cold stress (PubMed:28351986). {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:28351986}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_010025296.10.0PREDICTED: calmodulin-binding transcription activator 4
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A059B6X20.0A0A059B6X2_EUCGR; Uncharacterized protein
STRINGXP_010025296.10.0(Eucalyptus grandis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM64762642
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.10.0Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains
Publications ? help Back to Top
  1. Benn G, et al.
    A key general stress response motif is regulated non-uniformly by CAMTA transcription factors.
    Plant J., 2014. 80(1): p. 82-92
    [PMID:25039701]
  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]