PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Home  TFext  BLAST  Prediction  Download  Help  About  Links  PlantRegMap
(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID AHYPO_004790-RA
Organism
Amaranthus hypochondriacus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Caryophyllales; Amaranthaceae; Amaranthus
Family CAMTA
Protein Properties Length: 915aa    MW: 101414 Da    PI: 6.8858
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
AHYPO_004790-RAgenomeBYUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-193.91.4e-291384374
             CG-1  3 kekkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLK 74
                       ++rwlk+ e+  iL+n++++++t+e++++p+sgsl L+n++++r+frkDG+sw+kkkdg++v E+he+LK
  AHYPO_004790-RA 13 AAHTRWLKPAEVFFILQNHANYKITQEAPQKPPSGSLYLFNKRVLRFFRKDGHSWRKKKDGRSVGEAHERLK 84
                     3489*******************************************************************9 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143739.6217143IPR005559CG-1 DNA-binding domain
SMARTSM010761.1E-2310138IPR005559CG-1 DNA-binding domain
PfamPF038593.7E-241484IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.101.1E-8338434IPR013783Immunoglobulin-like fold
CDDcd001028.74E-5349434No hitNo description
SuperFamilySSF812963.92E-17350433IPR014756Immunoglobulin E-set
PfamPF018331.7E-7350432IPR002909IPT domain
PROSITE profilePS5029714.212543635IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.202.1E-12543637IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484037.93E-14547637IPR020683Ankyrin repeat-containing domain
CDDcd002047.89E-12548635No hitNo description
PfamPF127964.9E-7560636IPR020683Ankyrin repeat-containing domain
SMARTSM002480.049576605IPR002110Ankyrin repeat
PROSITE profilePS500889.805576608IPR002110Ankyrin repeat
SMARTSM00248620615644IPR002110Ankyrin repeat
SMARTSM0001521693715IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.602694723IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525408.23E-9752805IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000150.12753775IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.352755783IPR000048IQ motif, EF-hand binding site
PfamPF006120.004756774IPR000048IQ motif, EF-hand binding site
SMARTSM000151.5E-4776798IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.048777801IPR000048IQ motif, EF-hand binding site
PfamPF006123.5E-5779798IPR000048IQ 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: 915 aa     Download sequence    Send to blast
MQSEFDMNEL LQAAHTRWLK PAEVFFILQN HANYKITQEA PQKPPSGSLY LFNKRVLRFF  60
RKDGHSWRKK KDGRSVGEAH ERLKGRLSSG PTLEFRPGAS STISQSPTAY TIQNLGSSSL  120
AINESYQSHS SPVSVEVSSD ATMEKRIECL NGSNLTGSSS MMSVDQALRR LEVQLSLDDD  180
DSLQKYAPVD DQDGNEDILT LNDLCDSSYF GVSTIPNGLS QQQDSGGIEV HHHSTSGMAR  240
SIDDGESLLW IDLLYSGPLN QNVEKEKRDA LNGKDLFFSE RPVEHQPQHS GALATGKWTA  300
AHKDINNLTY SSPTYSATPK MSTMFLDPSL GMPLSTGSSW TVTKEQKFSI HEVCPEWGYT  360
NDSTKVIIIG SFLCDPSESE WHCMFGDVEV PLKFIQNGVF SCRAPPHVSG KVALCITSGN  420
RKPCSESREF EYRDKDITGV NHNKQGETNR STEEMLLLVK LVQMLLSNSS LRRGENNSVG  480
ADIQKCNDDM WNKIIEDLLV DGTSLMDTLN WLLQQLLKDK LLQWLSSASM ERGRCGECSL  540
SRKEQGIIHL IAGLGYEWAL IPILDCGVGI NFRDINGWTA LHWAGKFGRE KMVAALIASG  600
ASAVALTDPS SLDPTGRSAA YIAAENGHKG LAGYLSELAL TSHLSSLTLE QSENSKDAAN  660
VGAESTVNNI SKEEVNSCED KVTLKQILTA VRNAAQAAAR IQAAFRAHSF RKRQLKEAAC  720
SRAVSDLDEY GFTVNDIPVL SAASKLAFHN SHDCQKAALS IQKNFRGWKG RKDFLTLRQK  780
VVKIQAHVRG YQARKQFKVI CWAVGILDKA VLRWRRKGAG LRGFRSEFCD EEEDDDIIKV  840
FRKEKVDVAI DEAVKRVLSM AESPEARQQY QRMLARTQEA KAELQGITSS GTSGFQDTVH  900
YMDKDDIHTS SRKS*
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}.
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_021723085.10.0calmodulin-binding transcription activator 4-like isoform X1
RefseqXP_021745199.10.0calmodulin-binding transcription activator 4-like isoform X1
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A0K9QIH30.0A0A0K9QIH3_SPIOL; Uncharacterized protein
STRINGXP_010682739.10.0(Beta vulgaris)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.11e-158Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains
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]