PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Kalax.0401s0003.2.p
Organism
Kalanchoe marnieriana
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Saxifragales; Crassulaceae; Kalanchoe
Family CAMTA
Protein Properties Length: 900aa    MW: 100256 Da    PI: 6.2301
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0401s0003.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1149.21e-46121273117
                 CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseen 91 
                          +e + rwlk+ e++ i++n e  +l+++++++p+sg+++Lyn++++r+fr DG++w+kk+dg+tv E+he+LKv++ve+l+cyYa++een
  Kalax.0401s0003.2.p  12 REaEVRWLKPAEVYYIIQNCEDRHLQSKSAKKPPSGTFFLYNKRVLRNFRGDGHNWRKKRDGRTVGEAHERLKVDNVEALNCYYARGEEN 101
                          55589*****************999***************************************************************** PP

                 CG-1  92 ptfqrrcywlLeeelekivlvhylev 117
                          ++f+rr++w+L  e+++ivlv+yl+v
  Kalax.0401s0003.2.p 102 SSFRRRSFWMLSGERSHIVLVQYLDV 127
                          ***********************997 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143762.9487133IPR005559CG-1 DNA-binding domain
SMARTSM010761.8E-5210128IPR005559CG-1 DNA-binding domain
PfamPF038596.4E-4114127IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.107.8E-12348436IPR013783Immunoglobulin-like fold
PfamPF018331.4E-8350433IPR002909IPT domain
SuperFamilySSF812961.54E-18350434IPR014756Immunoglobulin E-set
CDDcd001027.77E-5350434No hitNo description
Gene3DG3DSA:1.25.40.201.7E-15549644IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.318550642IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.87E-16554644IPR020683Ankyrin repeat-containing domain
CDDcd002043.82E-15555642No hitNo description
PfamPF127967.7E-8570643IPR020683Ankyrin repeat-containing domain
SMARTSM002480.0014583618IPR002110Ankyrin repeat
PROSITE profilePS500889.938583615IPR002110Ankyrin repeat
SMARTSM002482700622651IPR002110Ankyrin repeat
SMARTSM0001511700722IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525401.27E-7700805IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.529701730IPR000048IQ motif, EF-hand binding site
SMARTSM000150.12756778IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.608757786IPR000048IQ motif, EF-hand binding site
PfamPF006120.0068759777IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0014779801IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.974781806IPR000048IQ motif, EF-hand binding site
PfamPF006127.2E-5782801IPR000048IQ 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: 900 aa     Download sequence    Send to blast
MQSEFDINEL VREAEVRWLK PAEVYYIIQN CEDRHLQSKS AKKPPSGTFF LYNKRVLRNF  60
RGDGHNWRKK RDGRTVGEAH ERLKVDNVEA LNCYYARGEE NSSFRRRSFW MLSGERSHIV  120
LVQYLDVANQ SPGSVSQPSF LLSPPSSLSP GISSATNQEF VSVSGGYDSN INLPSPVSAE  180
IGFEVGISNN MVEVNQASGH LEKQLSLNYE NLNGINSLSS QEGMLNSSNF EGYGMEIANQ  240
VWLDSLLDGS DYAACDGDSG MGRQQTSGRD EDCVSWTDVA NFGEDEQISL ELHEMFPLNT  300
DRFEGPPFSS FTSSQQRNLG YQGKYFETDQ TLIQPQANSN LFIDQNQKFT IRDVSPEWGY  360
SFETTKVIIV GSFLCHPSEH VWTCMFGGIE VPIEIIQEGV ILCEAPPNPS GKVTLCVTSG  420
NRETCSEVRE FEYRNKTGIC AQCSASKKET TMSSEELLLL VRLAQMLICD YSLGQRGGDS  480
KELGNGLSEK RNSDEDSWSL ILESLLVGSG TFAGTIYWLL EEFLKEKLVR WISSKTQEPT  540
GESTCLLSRK EQGIIHMIAG LGYEWALAPI LSSGVGINFR DINGWTALHW AARFGREKMV  600
ACLIASGALA GALTDPNVQD PTGKTAASIA AINGHKGLAG YLSEVALTSH LSSLKLQESE  660
LSKELAVSEA EHTVNCIAEA NMNTTEDQLS LNDTLTAVRN AASAAARIQA AFRAHSFRKR  720
QQEKAFKTIS IDDYGISSDV QVLSAVSKLA FRNTRDHNSA ALSIQKKYRG YKGRKEFLDF  780
RQKVVKIQAH VRGHQTRKNY KVCWAAGILE KIILRWLRKG VGLRGFKPEL ETIDEIDEED  840
FAKVFRKKNV EAALEEAVAR VLSMVASPEA RQQYRRMLER YRQAKAHLGN AANERLQHL*
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_022725126.10.0calmodulin-binding transcription activator 4-like isoform X3
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLD7TB030.0D7TB03_VITVI; Uncharacterized protein
STRINGVIT_01s0010g03850.t010.0(Vitis vinifera)
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]