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_010926833.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Arecales; Arecaceae; Arecoideae; Cocoseae; Elaeidinae; Elaeis
Family CAMTA
Protein Properties Length: 940aa    MW: 105240 Da    PI: 6.3505
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_010926833.1genomeOGView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1156.74.9e-49131274117
            CG-1   4 e.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrr 97 
                       ++rwlk+ e++ iL+n+e+++l+++++++p+sgsl+L+nr+++r++r+DGy w+kk +g+t  E he+LKvg+ evl+cyYa++e+np fqrr
  XP_010926833.1  13 DaQTRWLKPVEVLFILHNHESFQLSNKPPDKPPSGSLLLFNRRVLRNYRNDGYLWRKKNNGRTLAESHEHLKVGAAEVLSCYYARGEQNPCFQRR 107
                     4499******************************************************************************************* PP

            CG-1  98 cywlLeeelekivlvhylev 117
                     +yw+L+ + e+iv+vhy++v
  XP_010926833.1 108 IYWMLDPANEHIVFVHYRDV 127
                     ******************97 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143770.3827133IPR005559CG-1 DNA-binding domain
SMARTSM010762.7E-6610128IPR005559CG-1 DNA-binding domain
PfamPF038591.5E-4414127IPR005559CG-1 DNA-binding domain
SuperFamilySSF812964.02E-15375459IPR014756Immunoglobulin E-set
CDDcd001021.82E-4376459No hitNo description
Gene3DG3DSA:2.60.40.105.1E-5376467IPR013783Immunoglobulin-like fold
PfamPF018335.2E-4378451IPR002909IPT domain
SuperFamilySSF484031.71E-13527670IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.205.1E-14559671IPR020683Ankyrin repeat-containing domain
CDDcd002049.52E-7564668No hitNo description
PROSITE profilePS5029714.53576668IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008810.499609641IPR002110Ankyrin repeat
SMARTSM002480.0011609638IPR002110Ankyrin repeat
SMARTSM0001579729751IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.852730759IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525407.7E-5774826IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000150.22779801IPR000048IQ motif, EF-hand binding site
PfamPF006120.014781800IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500966.632781809IPR000048IQ motif, EF-hand binding site
SMARTSM000150.11802824IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.919803828IPR000048IQ motif, EF-hand binding site
PfamPF006128.4E-4804823IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0005634Cellular Componentnucleus
GO:0005829Cellular Componentcytosol
GO:0003677Molecular FunctionDNA binding
GO:0005515Molecular Functionprotein binding
Sequence ? help Back to Top
Protein Sequence    Length: 940 aa     Download sequence    Send to blast
MQEGFDINKL CKDAQTRWLK PVEVLFILHN HESFQLSNKP PDKPPSGSLL LFNRRVLRNY  60
RNDGYLWRKK NNGRTLAESH EHLKVGAAEV LSCYYARGEQ NPCFQRRIYW MLDPANEHIV  120
FVHYRDVAEG RFVPEPIFSV STESPSTFNQ TNSITDAQVQ GFPTQINELN EQCQNPCSSV  180
SVEEASSEFV TGKTEKPLLI KMDTSETYNQ PLLPEVNHAL RKLEEQLSLD DDDDGNGYIY  240
SEEKLHPSCN QNEKSEDLGI LNHETRDFVQ ETLDSLLDQL KHEANDHVEE GGQQDGSHAL  300
QMVKSPEFSR WSHGSHSLIN STSTINSCGA LSGLLTPGND NNTHGLETVL LTGNSVCSSS  360
GADFGLPVAQ KPWFNICEIS PEWAFSFERT KVIITGHFLC NPPGHSWAIL FGDAEVPLEI  420
VQEGVFRCLA PKHDPGKVKL RITSGNGEPC SDVREFEFRA NPGTSSFSST SKQGYAVMGT  480
EELLLLVRFV QLLLYGHDRT SIPQEGDVET CIDRSRKLKR NDDRLGEIVE ALLAGRETSA  540
NTMDWILQEL LKDKLQQWLL SKHLENADQT CVLSKQEQCI IHMISGLGYE WALNPILTSG  600
TGINFRDTKG WTALHWAACF GREKMVAALL AAGASAGAVT DPTPQEPAGK TPGSLAAAND  660
HKGLAGYLSE AALTNHLFSL AMGKSEISKT SGPVEADGGV ESISQRSAHL QGGTEDQLLL  720
KDSLAAVRNA TQAAARIQST FRAYSFWKKH QNADQDKDGF SPEDINGVFV AFRGLCDRAF  780
HKAALSIQKN YRCWKRRKEF VTLRKHVIKI QARVRAHQAR KKYELLLTVG ILEKIILRWC  840
RRRVGLRGFR ADPESINKEE ENDILKVFRK QKVDAALDEA VSSVLSMVDC PEAQQQYRRM  900
LESYRQAKAD LSKVETATSR VSGDWVSREL EDYLNQLGHE
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}.
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_010926833.10.0calmodulin-binding transcription activator 4 isoform X2
SwissprotQ9FYG21e-168CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A2H3ZYH70.0A0A2H3ZYH7_PHODC; calmodulin-binding transcription activator 4-like isoform X4
STRINGXP_008806417.10.0(Phoenix dactylifera)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.11e-153Calmodulin-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]