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 PK06349.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Cannabaceae; Cannabis
Family CAMTA
Protein Properties Length: 990aa    MW: 109900 Da    PI: 5.3692
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
PK06349.1genomeCCBRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1175.76.1e-55151293116
       CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywl 101
                +e ++rwlk+ e++ iL+n+ek++lt+e++++p+sgsl+Lyn++++r+fr+DG++w+kkkdg+tv E+he+LKvg+ve+l+cyYah+eenp+fqrr+yw+
  PK06349.1  15 QEaQSRWLKPAEVLFILQNHEKYKLTQEPPKKPPSGSLLLYNKRILRFFRRDGHNWRKKKDGRTVGEAHERLKVGNVETLNCYYAHGEENPSFQRRSYWI 114
                5669************************************************************************************************ PP

       CG-1 102 Leeelekivlvhyle 116
                L+ ++e+ivlvhy++
  PK06349.1 115 LDPAYEHIVLVHYRD 129
                *************97 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143781.65410136IPR005559CG-1 DNA-binding domain
SMARTSM010768.4E-7513131IPR005559CG-1 DNA-binding domain
PfamPF038591.3E-4716129IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.102.6E-10423511IPR013783Immunoglobulin-like fold
SuperFamilySSF812964.9E-19428511IPR014756Immunoglobulin E-set
PfamPF018335.3E-12428511IPR002909IPT domain
CDDcd001021.44E-6428511No hitNo description
Gene3DG3DSA:1.25.40.205.8E-15623718IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029715.884624718IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484038.71E-16628718IPR020683Ankyrin repeat-containing domain
CDDcd002041.60E-13629716No hitNo description
PfamPF127965.4E-8639718IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.22657689IPR002110Ankyrin repeat
SMARTSM002485.2E-4657686IPR002110Ankyrin repeat
SMARTSM002481700696725IPR002110Ankyrin repeat
SMARTSM0001513774796IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.675775804IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525409.29E-8781880IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000154.5828850IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.84829858IPR000048IQ motif, EF-hand binding site
PfamPF006120.021831849IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0016851873IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.846852876IPR000048IQ motif, EF-hand binding site
PfamPF006126.7E-4854873IPR000048IQ 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: 990 aa     Download sequence    Send to blast
MKAMQSGYDI NDLFQEAQSR WLKPAEVLFI LQNHEKYKLT QEPPKKPPSG SLLLYNKRIL  60
RFFRRDGHNW RKKKDGRTVG EAHERLKVGN VETLNCYYAH GEENPSFQRR SYWILDPAYE  120
HIVLVHYRDI TEGNSSSRSG SGSGSGSGSA TQLSPESFLS FSQSPSPSNT QNAGSLFVSD  180
YQSYSPGSIE VTSDSVIQSN GNGHYDSIDG TGGILSTTQG DVNQALRKLE VQLSLNEDSV  240
KDFESPSKLE DPNDPDLLEY ENQMYNPNTF LDFNEPGNLA VDQCYSGFDG VPGDSGGDHH  300
QLLEHEHRYG GKESVSWKEM LDSCNISSGV ECQNNHALLN GTHVEYTRNG PTEEQEYLQW  360
QKSSSSIVDN ASSVMCQEVD HLKISSYPSS SKVLDTNSEY YAMLFDQGQT GPLESGVSLT  420
TEQKQKFTIH EISPEWGYAT EATKIIIVGS FLCDSSESTW HCMFGDVEVP AQIIQDGVLR  480
CEAPPHPSGK VTICITAGNR QSCSEVKEFE YCLKPSSCAQ GNPPLTESTR SPEELLLLVR  540
FVQLLLSDSS MPRRDNKVLD APQKLIADVD SWDSLIESLL DGSGTLSSTI NLILEELLKD  600
KLLQWISSRS QEQQDQTGCP LSKKEQGIIH MIAGLGFEWA INPILSSGVS INFRDINGWT  660
ALHWAARFGR EKMVAALIAS GASAGAVTDP CSQDPIGKTA ASIAASNGHK GLAGYLAEVA  720
LTSHLSSLTL EESELYKGSA EIEAENTINS ISKHGLIAHE DQLSLEPTLA AVRNAAQAAA  780
RIQSAFRAHS FRKQQKEAID SNINEDEYGF SLNDISAMSK MKFRNPRDYN SAALSIQKKY  840
RGWKGRKDFL ALRQKVVKIQ AHVRGYQIRK SYKVICWAVG VLEKVVLRWR RKGSGLRGYR  900
PEIDPIDESE DILKVFRKQK VDGTIKEAFS RVMSMVKSSE ARQQYIRVFE KYCQVKAERG  960
DEDIEAAAAA ASSELADLYG LEDVDMFSFP
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_024017619.10.0calmodulin-binding transcription activator 4
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A2P5C1S10.0A0A2P5C1S1_TREOI; Serine/threonine protein kinase
STRINGXP_008222185.10.0(Prunus mume)
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]