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 cra_locus_4485_iso_5
Organism
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: 955aa    MW: 106591 Da    PI: 6.485
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
cra_locus_4485_iso_5genomeMPGR-
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1168.98.1e-53121272116
                                 CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLK 74 
                                          +ke + rwlk+ e+  iL+n+e h +t+e+++rp+ gsl+L+n++++r+fr+DG++w++k+dg++v E+he+LK
  cra_locus_4485_iso_5_len_4174_ver_3  12 VKEaQVRWLKPPEVFFILKNHEDHMITHEPPQRPTGGSLFLFNKRVLRFFRRDGHTWRRKRDGRAVGEAHERLK 85 
                                          667699******************************************************************** PP

                                 CG-1  75 vggvevlycyYahseenptfqrrcywlLeeelekivlvhyle 116
                                          vg+ve+++cyYah+e+np+fqrr+yw+L+ ++e+ivlvhy++
  cra_locus_4485_iso_5_len_4174_ver_3  86 VGNVEAINCYYAHGEQNPSFQRRSYWMLDPAYEHIVLVHYRD 127
                                          ****************************************98 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143777.118134IPR005559CG-1 DNA-binding domain
SMARTSM010765.6E-7311129IPR005559CG-1 DNA-binding domain
PfamPF038593.9E-4614127IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.102.3E-9393474IPR013783Immunoglobulin-like fold
PfamPF018333.2E-9393469IPR002909IPT domain
SuperFamilySSF812968.68E-19393477IPR014756Immunoglobulin E-set
Gene3DG3DSA:1.25.40.201.5E-13590683IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029714.212591683IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.71E-14595685IPR020683Ankyrin repeat-containing domain
PfamPF127962.9E-7612684IPR020683Ankyrin repeat-containing domain
CDDcd002047.10E-13612683No hitNo description
SMARTSM002480.0032624656IPR002110Ankyrin repeat
PROSITE profilePS5008810.392624656IPR002110Ankyrin repeat
SMARTSM002482900663692IPR002110Ankyrin repeat
SMARTSM000159.4741763IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.821742770IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525408.5E-6789845IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000154.5797819IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.584798827IPR000048IQ motif, EF-hand binding site
PfamPF006120.02800818IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0014820842IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.736822846IPR000048IQ motif, EF-hand binding site
PfamPF006122.9E-5823842IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0005634Cellular Componentnucleus
GO:0005829Cellular Componentcytosol
GO:0003677Molecular FunctionDNA binding
GO:0005515Molecular Functionprotein binding
Sequence ? help Back to Top
Protein Sequence    Length: 955 aa     Download sequence    Send to blast
MSQSGYNFGD LVKEAQVRWL KPPEVFFILK NHEDHMITHE PPQRPTGGSL FLFNKRVLRF  60
FRRDGHTWRR KRDGRAVGEA HERLKVGNVE AINCYYAHGE QNPSFQRRSY WMLDPAYEHI  120
VLVHYRDINE GRNSAGIISQ FSPASLSSLS QSPSSYTTQQ PGSSALISES FEQYQNLSSP  180
ASVEISSDAV IKTKGVNYSD NVERVDEVNS SSGLEMSQAL RMIEHQLSLN DDCLKEIDPF  240
CSENENSDLE NIIHDPSSSA STPGYMMQNH HQLGYEVNDW KNMLDVYSED VVSQVRHADK  300
VNENGNLLKS SMKGPAAGQE SSSWLNFTGS NSQMSSVPVT KEVEDFQYPV YSSNTGTYVN  360
NQDHYTTLFD QGQIGISFED DVSLTISQKQ RFTIREISPN WGYASETTKV VIIGSFLCDP  420
LECTWTCMFG DVEVPVQIIQ DGVISCHAPP HLPGKVTLCV TSANRESCSE VREFDYRVKP  480
SVCSHCSQPD ADATRSPEEL LLLVRFVQLL LSAASVQKGD SSESGIDLLG KLKTGEDSWG  540
QVIEALLVGS STSSVTKDWL LQELLKDKLQ NWLSSRSEEI SSHTSCYLSK KEQGIIHMIA  600
GLGLEWALHP VLKSGVSVNF RDINGWTALH WAARFGREKM VAALIASGAL AGAVTDPTPR  660
DPIGKTAAFI AATYGHKGLA GYLSEVALTS HLSSLTLEES ELSKGSADVE VERTLSSVPK  720
TNPLTNEDQL SLKDTLAAVR NAAQAAARIQ SAFRAHSFRK RLHRQASSAG LDEYGLLSDD  780
VQGLSAASKL AFRNSRDYNS AALSIQKKYR GWKGRKDFLA FRQKVVKIQA HVRGYQVRKH  840
YKVCWAVGIL EKVVLRWRRR GVGLRGFRNE NEPIDDSEDE DILRVFRKQK VDAAIDEAVS  900
RVLSMVESPN ARQQYRRLLE KYRQAKAALQ ESESETASAS YGFSNMENDD IYLLQ
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}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_027097389.10.0calmodulin-binding transcription activator 4-like isoform X2
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A068UXT90.0A0A068UXT9_COFCA; Uncharacterized protein
STRINGXP_009617256.10.0(Nicotiana tomentosiformis)
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]