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 Kaladp0018s0264.2.p
Organism
Kalanchoe laxiflora
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: 771aa    MW: 87349.2 Da    PI: 6.3541
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kaladp0018s0264.2.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1158.41.4e-49281424117
                 CG-1   4 e.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenp 92 
                          e k+rwl+++ei+aiL n+  + ++ ++ + pksg++ L++rkk+r+frkDG++wkkk dgktv+E+he+LKvg+ e +++yYah+++n+
  Kaladp0018s0264.2.p  28 EaKSRWLRPNEIHAILFNHMYFPIHVKPVNLPKSGEIHLFDRKKLRNFRKDGHNWKKKNDGKTVKEAHEHLKVGNEERIHVYYAHGQDNA 117
                          559*************************************************************************************** PP

                 CG-1  93 tfqrrcywlLeeelekivlvhylev 117
                          tf rrcywlL++++e+ivlvhy+e+
  Kaladp0018s0264.2.p 118 TFVRRCYWLLDKSMEHIVLVHYRET 142
                          **********************986 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143772.25722148IPR005559CG-1 DNA-binding domain
SMARTSM010761.2E-7025143IPR005559CG-1 DNA-binding domain
PfamPF038591.6E-4428141IPR005559CG-1 DNA-binding domain
CDDcd002041.56E-17397514No hitNo description
PfamPF127962.5E-8397484IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.26E-17397515IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.204.3E-17413516IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.52422514IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.728455487IPR002110Ankyrin repeat
SMARTSM002483.5E-6455484IPR002110Ankyrin repeat
PROSITE profilePS500966.504603629IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525404.6E-7605666IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM0001538618640IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.071619648IPR000048IQ motif, EF-hand binding site
PfamPF006120.05621639IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0017641663IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.908642666IPR000048IQ motif, EF-hand binding site
PfamPF006122.9E-4645663IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525404.6E-7723750IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000157723745IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.517725753IPR000048IQ motif, EF-hand binding site
PfamPF006120.068726745IPR000048IQ 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: 771 aa     Download sequence    Send to blast
MESVLLDGFQ IHGFRTMNEL DLKSIFEEAK SRWLRPNEIH AILFNHMYFP IHVKPVNLPK  60
SGEIHLFDRK KLRNFRKDGH NWKKKNDGKT VKEAHEHLKV GNEERIHVYY AHGQDNATFV  120
RRCYWLLDKS MEHIVLVHYR ETCELLDPSA APVNSNSSSG LTELHVPFLT YEETESGSQQ  180
SNTSNQLEYI ESIENVTAVT LERRLREINT LDWDELLVDT DPSVPIAYEE GKSGGVQQQN  240
PVMINVSKDD GSALLMNLPT ELSSGWHSAC PETRSDSING DILDGSYNHA VHSQLMMEAA  300
PNNSGTLFGG QSFSITQGGG QDQDRRWMNS SLTVESPGSV NDSIHESSIS SAQNSMVPTI  360
MDQPQSADQI FTITDISPEW AFSCEKTKAE EILFEQAIRN RLQDWLLERI IEEQSPSDYD  420
EQGLGVLHLC AILNYTWAVY LYSKSGLSLD FRDKYGWTAL HWAAYYGRED IVGALLSAGA  480
RPNLVTDPTP LIPGGCTASD LAAQKGHNGL AAYLGEEALV DHFNDMALAG NASGSIEFQR  540
TCSVKRETVY DEASCLKDTL AAYRTAADAA ARINAAFREQ SLKLRTEAVQ GSNPEDEART  600
IISAMKIQHA FRSFESRKKM AAALRIQYGF RTWKTRRDFL NMRQQAIKIQ AVFRGFQVRR  660
HYRKIIWSVG VLEKAVLRWR FKRRGFRGLQ VAPVQEITSV AQEQENDVEE DFFVLGRKQA  720
EDRVESAVIK VQAMFRSKQA QQEYRRMKLA HNQAKIEYEG FFNHNAKMES *
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
16984KKLRNFRKDGHNWKKK
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator (PubMed:14581622). 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 in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:14581622, ECO:0000269|PubMed:28351986, ECO:0000305|PubMed:11925432}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat shock, UVB, wounding, abscisic acid, H(2)O(2) and salicylic acid. {ECO:0000269|PubMed:12218065}.
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_021637034.10.0calmodulin-binding transcription activator 5-like isoform X4
SwissprotO234631e-150CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2G2VJP00.0A0A2G2VJP0_CAPBA; Uncharacterized protein (Fragment)
STRINGGLYMA07G37090.21e-169(Glycine max)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT4G16150.11e-146calmodulin binding;transcription regulators
Publications ? help Back to Top
  1. Ye J, et al.
    Arabidopsis formin3 directs the formation of actin cables and polarized growth in pollen tubes.
    Plant Cell, 2009. 21(12): p. 3868-84
    [PMID:20023198]
  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]
  3. Lan Y,Liu X,Fu Y,Huang S
    Arabidopsis class I formins control membrane-originated actin polymerization at pollen tube tips.
    PLoS Genet., 2018. 14(11): p. e1007789
    [PMID:30418966]