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 Cc03_g01050
Common NameGSCOC_T00025708001
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Coffeeae; Coffea
Family CAMTA
Protein Properties Length: 920aa    MW: 104100 Da    PI: 6.8875
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Cc03_g01050genomeCGSCView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1166.15.8e-52251413118
         CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcy 99 
                  +e k rwl+++ei+aiL n+++++++ ++ + p+sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKvg+ e +++yYah+e+nptf rrcy
  Cc03_g01050  25 EEaKGRWLRPNEIHAILCNYKHFNVQVKPVNLPPSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKVGNEERIHVYYAHGEDNPTFVRRCY 122
                  45599********************************************************************************************* PP

         CG-1 100 wlLeeelekivlvhylevk 118
                  wlL+++le++vlvhy+e++
  Cc03_g01050 123 WLLDKSLEHVVLVHYRETQ 141
                  ****************986 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143778.41520146IPR005559CG-1 DNA-binding domain
SMARTSM010767.4E-7523141IPR005559CG-1 DNA-binding domain
PfamPF038591.7E-4626139IPR005559CG-1 DNA-binding domain
SuperFamilySSF812963.64E-11371458IPR014756Immunoglobulin E-set
CDDcd002043.46E-15550665No hitNo description
SuperFamilySSF484033.73E-18551670IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.201.5E-16553669IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.069561677IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008810.873606638IPR002110Ankyrin repeat
SMARTSM002483.4E-4606635IPR002110Ankyrin repeat
SMARTSM002483800645674IPR002110Ankyrin repeat
SuperFamilySSF525407.43E-6717820IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500966.888754780IPR000048IQ motif, EF-hand binding site
SMARTSM0001529769791IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.272770796IPR000048IQ motif, EF-hand binding site
SMARTSM000150.006792814IPR000048IQ motif, EF-hand binding site
PROSITE profilePS5009610.036793817IPR000048IQ motif, EF-hand binding site
PfamPF006120.002794814IPR000048IQ motif, EF-hand binding site
SMARTSM000158.7872894IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.718874902IPR000048IQ 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: 920 aa     Download sequence    Send to blast
MAAIAGSEIH GFRTMKDLDI GNILEEAKGR WLRPNEIHAI LCNYKHFNVQ VKPVNLPPSG  60
TIVLFDRKML RNFRKDGHNW KKKKDGKTVK EAHEHLKVGN EERIHVYYAH GEDNPTFVRR  120
CYWLLDKSLE HVVLVHYRET QEGSPSTPLN SNSSSALSDP SQSLVISEES DSAADRAYYS  180
RERADLDPNC SVNIKDHELR LHEINTLEWD ELLVQDDPNK LIGPQEGKYS SELSYQYGMN  240
GYGITSDSIS DNKLPVESYL EKFPGQVSMN NSGNLNVPAN LCFQTMGAPT ANLLLKDSEQ  300
MTLFAGDSLE HASKDGLQTQ DSFGKWISNV IADSPLPLDD TTLDSSMSTN QSFASPHMNI  360
PQFSAAKQIF NITEISPSWA LSSEETKILV VGYFHEGQSN LSRPNLFCIC GNACAHAEPV  420
QSGVFRCVVS PQAPAFVNLF LSFDGHTSIS QVVMFEFRAP IVDNPAISEE RSSWEEFEVQ  480
MRLAHLLFST SRSFNILSTK VTPTALKEAK NFARKTSHIK NHWEFLTKSI KAKEMSFPDA  540
KNCLFELTLQ NRLLEWLLER VAEGCQISER DEQGQGVIHL CAILGYTWAV YPFSWSGLSI  600
DYRDKFGWTA LHWAAYYGRE PMVAKLLTAG AKANLVTDPT SENPGGFTAA DLASKNGHEG  660
LGAYLAEKAL VQHFQDMTLA GNVSGSLQTA KSDSVEPGNF SEDELYLKDT LAAYRTAADA  720
AARIQAAFRE HSLKVQTLAV ESSNPEIEAR NIVAAMKIQH AFRNFETRKK MAAAARIQHS  780
FRTWKMRRDF LNMRRQAIRI QAVFRGFQVR KQYRKIIWSV GVLEKAILRW RLKRKGFRGL  840
HVNPDEVVNN QKEENDVEED FFRASRKQAE ERVERSVVRV QAMFRSKLAQ EEYRRMKLAY  900
NNAAREYEEF ENPDGMRED*
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_027115917.10.0calmodulin-binding transcription activator 5-like
SwissprotO234630.0CMTA5_ARATH; Calmodulin-binding transcription activator 5
TrEMBLA0A068TRD50.0A0A068TRD5_COFCA; Uncharacterized protein
STRINGXP_009609050.10.0(Nicotiana tomentosiformis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA45652232
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]