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 29929.m004634
Common NameRCOM_1079700
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae; Ricinus
Family CAMTA
Protein Properties Length: 924aa    MW: 102966 Da    PI: 5.0463
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
29929.m004634genomeJCVIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-157.62.5e-186110275116
           CG-1  75 vggvevlycyYahseenptfqrrcywlLeeelekivlvhyle 116
                    vg+ve+l+cyYah+e+np+fqrr+yw+L+ ++e+ivlvhy+e
  29929.m004634  61 VGNVEALNCYYAHGEQNPNFQRRSYWMLDPAYEHIVLVHYRE 102
                    99**************************************98 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143731.1718109IPR005559CG-1 DNA-binding domain
SMARTSM010762.6E-2611104IPR005559CG-1 DNA-binding domain
PfamPF038597.1E-1560102IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.107.9E-9353446IPR013783Immunoglobulin-like fold
CDDcd001029.70E-6362447No hitNo description
SuperFamilySSF812965.74E-19363446IPR014756Immunoglobulin E-set
PfamPF018331.6E-7365445IPR002909IPT domain
Gene3DG3DSA:1.25.40.203.1E-15542651IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.91559651IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.2E-15563653IPR020683Ankyrin repeat-containing domain
CDDcd002042.39E-9579651No hitNo description
PfamPF127963.0E-7580652IPR020683Ankyrin repeat-containing domain
SMARTSM002484.4E-4592621IPR002110Ankyrin repeat
PROSITE profilePS5008811.381592624IPR002110Ankyrin repeat
SMARTSM002483700631660IPR002110Ankyrin repeat
SMARTSM0001518709731IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.62710739IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525405.84E-7757819IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000154.5767789IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.584768797IPR000048IQ motif, EF-hand binding site
PfamPF006120.019770788IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0014790812IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.846792815IPR000048IQ motif, EF-hand binding site
PfamPF006122.8E-5793812IPR000048IQ 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: 924 aa     Download sequence    Send to blast
MSQSGYDINA LFQEAQMRWL KPAEVQFILQ NHEKYQLNQE PPQKPTKLHG IHPKYAMSCM  60
VGNVEALNCY YAHGEQNPNF QRRSYWMLDP AYEHIVLVHY REISEGKSTP GSAAQLSPSS  120
FSPSPSSYTT QNQDSTSIFS DSHDPYHNSS SPGSVEVSSG IVIQDDGLIS IEELTSSREN  180
ENSQFFRRLE EQLSLNEDSI NDVPLDYNQE GAVEDLELLA YEGQFSKKSL SSNLLPGSEY  240
IANNQGYGGH ARMQLQTNSL VHHEDADGSK ESISWNDVLE FQVKHIASCH IYDFLVTIFL  300
ATNTSTLLTQ EVENFDIPAY SSISETYDTN PEYYSVLYDQ GQLEVPIEAD SSLTVAQQQK  360
FRICEISPEW GYNTEVTKVI IIGSFLCDPS ESAWTCMFGN IEVPVEIIQE GVLRCEAPPH  420
LPGKVTFCIT IGNRESCSEI REFEYRSKNG SCAHCNSQME VAKSPEELLL LVRFVQMLLS  480
DSSLLKEDSI ETGIDLLRKL KTDDDSWGSV IEALLVGNGT SSGTVDWLLQ QLLKDKLQQW  540
FSSKSQDIQN RPSCPLSKKE QGIIHMVAGL GFEWALSPIL SHGVSIDFRD INGWTALHWA  600
ARFGREKMVA ALLASGASAG AVTDPTSQDP IGKTPASIAA NNGYKGLAGY LSELALTSHL  660
SSLTLEESEL SKGSAQVEAE RTVDSIAKGS FAANEDQVSL KDTLAAVRNA AQAAARIQSA  720
FRAHSFRKRQ EKEAAVSANC IDEYGVNIGD IQGLSAVSKL AFRNARDYNS AALSIQKKYR  780
GWKGRKDFLA FRQKVVKIQA HVRGYQVRKH YKVICWAVGI LDKVVLRWRR KGVGLRGFRN  840
ETEHVDESED EDILKVFRKQ KVDGAIDEAV SRVLSMVDSP DARQQYHRML ERYRLAKAEL  900
GETSEAVGSG SAANMENDNI YYLE
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}.
Cis-element ? help Back to Top
SourceLink
PlantRegMap29929.m004634
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_015572144.10.0calmodulin-binding transcription activator 4, partial
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLB9RMC90.0B9RMC9_RICCO; Calmodulin-binding transcription activator (Camta), plants, putative
STRINGXP_002514898.10.0(Ricinus communis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF45482950
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]