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 HL.SW.v1.0.G019033.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Cannabaceae; Humulus
Family CAMTA
Protein Properties Length: 880aa    MW: 98934.8 Da    PI: 7.275
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
HL.SW.v1.0.G019033.1genomeHOPBASEView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1162.86.1e-51291434118
                  CG-1   4 ekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenp 92 
                             +rwl+++ei+a+L n++ ++++ ++ + pk g+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+++ p
  HL.SW.v1.0.G019033.1  29 APSRWLRPNEIYAMLSNYKYFTIHVKPMNLPKGGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEEKIHVYYAHGQDCP 117
                           479************************************************************************************** PP

                  CG-1  93 tfqrrcywlLeeelekivlvhylevk 118
                           tf rrcywlL+++le+ivlvhy+e++
  HL.SW.v1.0.G019033.1 118 TFVRRCYWLLDKSLEHIVLVHYRETQ 143
                           ***********************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143774.19122148IPR005559CG-1 DNA-binding domain
SMARTSM010761.5E-7025143IPR005559CG-1 DNA-binding domain
PfamPF038599.0E-4529141IPR005559CG-1 DNA-binding domain
SuperFamilySSF812965.32E-14358445IPR014756Immunoglobulin E-set
PfamPF018336.0E-4359444IPR002909IPT domain
PROSITE profilePS5029713.337555598IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.202.2E-12555629IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484034.82E-13555628IPR020683Ankyrin repeat-containing domain
CDDcd002041.03E-10555625No hitNo description
PfamPF000231.5E-5566597IPR002110Ankyrin repeat
SMARTSM002487.1E-6566595IPR002110Ankyrin repeat
PROSITE profilePS5008811.888566598IPR002110Ankyrin repeat
SuperFamilySSF525402.1E-10655780IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.584714740IPR000048IQ motif, EF-hand binding site
SMARTSM000157.4729751IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.474730759IPR000048IQ motif, EF-hand binding site
SMARTSM000150.01752774IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.651753777IPR000048IQ motif, EF-hand binding site
PfamPF006129.5E-4757774IPR000048IQ 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: 880 aa     Download sequence    Send to blast
MEGGQLVDSN IHGFHTLQDL DVPTIMAEAP SRWLRPNEIY AMLSNYKYFT IHVKPMNLPK  60
GGTIVLFDRK MLRNFRKDGH NWKKKKDGKT VKEAHEHLKV GNEEKIHVYY AHGQDCPTFV  120
RRCYWLLDKS LEHIVLVHYR ETQELQGSPI TLVHTPVHSH SSSSSDPHAR VLSEELDSGS  180
GNSLTVKNYE QSLHDINTLE WDELLDPNDP INSALGDTVS CFNQQNQGVG KGSSSGGASD  240
MVPMHSSFDH LTNPIATGGN TPGDHRNNVY VQTMGAQMNS DFQRRDSVGV VTGDSDILVN  300
NGLHSQDSFG RWIDGILIDS PGSVIDPLLE TSISSAQDSF VSPATGHIQS PVLEHMFNIT  360
DVSPEWAYSN EKTKILVTGF FHEQYQQFAK CNLLCVCDDV SVSAECIQVG VYRCLIPPHS  420
PGFINLFLSV DGHKPISQIV NLEYRPPVTS LDVKNNWDKF RLQMRLAQLL FSSSKCLNIL  480
SSKVSPNTLK EAKKFAEKVP NFSKAWDNFI NSTENGKTLF PQAQDKLFNL ILRDRLKDWL  540
IEKVIEGSKP TEFDDHGLSL DFRDKHGWTA LHWAAFYGNA KMVAVLLTLG AKPNLVTDPT  600
SANPAGCTAG DLALFRGYEG LAGYLSEKAL VEQFKDMSMA GNASGTLDTS ANDTVYPETL  660
SEEQLFLKDT LAAYRTAADA AARIQVAFRE HSLKVRTKEV EGSSPEEEAR NIVAAMKIQH  720
AFRNFETRKK IKAAARIQDR FRSWKIRRHF LNLRQQTIKI QAAFRGFQVR KQYRKILWSV  780
GVLEKLVLRW RLKRKGFRGL QVAPVEVDQG RESDTEEDFY KASQKQAGER VGRSMGQVKN  840
MFASAKAQEE YHRVKVAHNQ VKLEYEDLFD TDPDSDITS*
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}.
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00435DAPTransfer from AT4G16150Download
Motif logo
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
PlantRegMapRetrieveRetrieve
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_024019984.10.0calmodulin-binding transcription activator 5
RefseqXP_024019986.10.0calmodulin-binding transcription activator 5
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A2P5F6180.0A0A2P5F618_TREOI; Notch
STRINGXP_008223308.10.0(Prunus mume)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF42883459
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT4G16150.10.0calmodulin 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]