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 cra_locus_7165_iso_4
Organism
Catharanthus roseus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae; Catharanthinae; Catharanthus
Family CAMTA
Protein Properties Length: 995aa    MW: 112467 Da    PI: 7.5609
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
cra_locus_7165_iso_4genomeMPGR-
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1160.43.4e-50471593114
                                 CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKv 75 
                                          +e k+rwl+++ei+aiL n++ ++++ ++ + p sg+++L++rk++r+frkDG++wkkkkdgktv+E+he+LKv
  cra_locus_7165_iso_4_len_3425_ver_3  47 EEaKARWLRPNEIHAILYNYKYFNVQVKPVNLPASGTMVLFDRKMLRNFRKDGHNWKKKKDGKTVKEAHEHLKV 120
                                          45599********************************************************************* PP

                                 CG-1  76 ggvevlycyYahseenptfqrrcywlLeeelekivlvhy 114
                                          g+ e +++yYah+e+nptf rrcywlL+++le+ivlv y
  cra_locus_7165_iso_4_len_3425_ver_3 121 GNEERIHVYYAHGEDNPTFVRRCYWLLDKSLEHIVLVPY 159
                                          *************************************98 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143772.07442168IPR005559CG-1 DNA-binding domain
SMARTSM010761.5E-7145163IPR005559CG-1 DNA-binding domain
PfamPF038591.3E-4448160IPR005559CG-1 DNA-binding domain
SuperFamilySSF812964.48E-10446532IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.201.3E-17628743IPR020683Ankyrin repeat-containing domain
CDDcd002045.99E-17630740No hitNo description
SuperFamilySSF484032.64E-18630743IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.335639743IPR020683Ankyrin repeat-containing domain
PfamPF127962.6E-6654743IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5008811.487681713IPR002110Ankyrin repeat
SMARTSM002481.3E-4681710IPR002110Ankyrin repeat
SMARTSM00248270720749IPR002110Ankyrin repeat
SMARTSM00015430792816IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.035830856IPR000048IQ motif, EF-hand binding site
SMARTSM0001561845867IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.346846875IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0019868890IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.834869893IPR000048IQ motif, EF-hand binding site
PfamPF006123.8E-4870890IPR000048IQ motif, EF-hand binding site
SMARTSM0001514948970IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.297950978IPR000048IQ 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: 995 aa     Download sequence    Send to blast
LKXSVGDSSR VEKEFISMDN IIAGRLVGTE IHGFRTMGDL DMANILEEAK ARWLRPNEIH  60
AILYNYKYFN VQVKPVNLPA SGTMVLFDRK MLRNFRKDGH NWKKKKDGKT VKEAHEHLKV  120
GNEERIHVYY AHGEDNPTFV RRCYWLLDKS LEHIVLVPYF XILSLDISIL LMIKFLMHFY  180
DHDIFGLKSF LIRILYQVPG THSPCSLSGN SRGAASPATP GNSNSSSGNS DPSASLVLSE  240
ESDSVVDRAY YTSHRADLVQ DESANIKDHE LRLHEINTLE WDDLLVPDDS NRRITTQEGG  300
YSVRLPYQYE TNGYRINSLP ANKLPAEDYL VNFPGLGLGN PVNNFNVPAD IGRQSMQGQI  360
TSTSLQNNFG KTALSLGNSI DNLIKDGLQT QDSFGRWIND IIIESPVSAD DMTLGSSVST  420
SHQSFTSPSM GPNLSSIPEQ YQIFYITDIS PSWASSTEPT KILVVGFFHE GLADVVKSSV  480
FCNCGDVCAP ATAIQPGVFR ILIPPQAPGV VDLFLSFDAE KPISQVVTFE FRAPRIENNL  540
ISSSEKSNWE EFQVQLRLAR LLFSTSRIFD IVSSKISPYT LKEAKTFARK TSNIADGWTR  600
LDKSIKAKEV PFPEAKDSLF ELTLQNRLYE WLLERVIEGC KITERDEQGQ GVIHLCAILG  660
YTWAVYPFSW SGLSLDYRDK LGWTALHWAA YYGREKMVAK LLSAGAKANL VSDPTSENPG  720
GCTAADLASK NGHEGLAAYL AEKALVQHFE AMTLAGNVSG SLQAPAAIDS ENPGNFTEEE  780
LNLKETLAAY RTAADAAARI QAAFREHSFK VRSKVVESSN PELEARNIIA AMKIQHAFRN  840
YETRKQMAAA ARIQYRFRTW KMRRDFLNMR RQAIKIQSVF RGFQVRRQYR KIIWSVGVLE  900
KAILRWRLKR KGFRGLQVQS DEAVKDQTQA SDTEEDFFHA SRKQAEERVE RSVVRVQAMF  960
RSKHAQEEYR RMKLEHNSAT LEYQELQNPD EMREV
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}.
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)
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]