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 Lsa004189
Organism
Lactuca sativa
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae; Lactucinae; Lactuca
Family CAMTA
Protein Properties Length: 944aa    MW: 105233 Da    PI: 5.3642
Description CAMTA family protein
Gene Model
Gene Model ID Type Source Coding Sequence
PUT-187a-Lactuca_sativa-44304PU_refplantGDBView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1165.96.8e-52121263116
       CG-1   3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrcywl 101
                +e + rwl++ e+  iL+n+e+ +l ++++++p+sgs++L+n++++r+frkDG+sw++kkdgk v E+he+LKvg+ve+l+cyYah+e+np+fqrr+yw+
  Lsa004189  12 QEaQYRWLRPGEVFFILQNYEEKQLNHAPPQKPPSGSVFLFNKRVLRFFRKDGHSWRRKKDGKNVGEAHERLKVGNVEALSCYYAHGEQNPNFQRRSYWM 111
                56599*********************************************************************************************** PP

       CG-1 102 Leeelekivlvhyle 116
                L+  +e+ivlvhy++
  Lsa004189 112 LDPGMEHIVLVHYRD 126
                *************97 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143775.1197133IPR005559CG-1 DNA-binding domain
SMARTSM010761.6E-7210128IPR005559CG-1 DNA-binding domain
PfamPF038592.9E-4713126IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.106.7E-7375466IPR013783Immunoglobulin-like fold
PfamPF018331.0E-6379465IPR002909IPT domain
SuperFamilySSF812961.87E-17379466IPR014756Immunoglobulin E-set
CDDcd001020.00124379466No hitNo description
Gene3DG3DSA:1.25.40.201.8E-16568667IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029716.361574678IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484032.8E-15576669IPR020683Ankyrin repeat-containing domain
CDDcd002047.12E-13594666No hitNo description
PfamPF127968.5E-8595668IPR020683Ankyrin repeat-containing domain
SMARTSM002480.0038607636IPR002110Ankyrin repeat
PROSITE profilePS5008810.339607639IPR002110Ankyrin repeat
SMARTSM00248610646675IPR002110Ankyrin repeat
SMARTSM00015160724746IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500967.657725754IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525401.06E-7776844IPR027417P-loop containing nucleoside triphosphate hydrolase
SMARTSM000150.2792814IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500968.023793822IPR000048IQ motif, EF-hand binding site
PfamPF006120.011794813IPR000048IQ motif, EF-hand binding site
SMARTSM000153.3E-4815837IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.157816840IPR000048IQ motif, EF-hand binding site
PfamPF006122.2E-5818836IPR000048IQ 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: 944 aa     Download sequence    Send to blast
MMSGYNLQDL IQEAQYRWLR PGEVFFILQN YEEKQLNHAP PQKPPSGSVF LFNKRVLRFF  60
RKDGHSWRRK KDGKNVGEAH ERLKVGNVEA LSCYYAHGEQ NPNFQRRSYW MLDPGMEHIV  120
LVHYRDITIG KHSAGPISTL MLGSSNIVQG SNSYTTSASE YYEHYNSTSG PSSLEVSPDV  180
VITSNGATHF NQTESIDGSP DFEINQALRK LEEQLSLDHM KDIGTFYSEN ENEYANELGF  240
TISEQDLGGS ERLQYGSDNY VSLPKDEFAI PSQQTLFWKD MQKSNESTTY DGSLESYGYP  300
LDENEVLLPR PRTDTGASND SSILASQELD ISTFPKYVPA NNMYQSDADI YSTLFDLGQI  360
ETPLASDSSL TIAQEQKFTI REISPDWGYA TEPTKVLIVG SFTCDPSVAD SEWICCMFGD  420
TEVPVEIIQE GVICCRAPPH LPGKVTICIT SGNREACSEV REFEYRPKDT DKDKDKPTNL  480
TENESTRTHQ ELSLLVRFVH LLLLSDTKNT TTDLPEGSIA ADSWAQVIEA LSDGSLASSK  540
ATDWLLEQLL KDKFQRWISN KSMDENALPT LSKKEQEIIH MVSGLGFVWA LTPILKAGVG  600
INFRDSNGWT ALHWAARFGR EKMVAEVLAC GANAGAVTDP CQQDPNGQTP ATIAAQYGHQ  660
GLAGYLSEMA LTAHLSSLTL QESQLSKGSA DVEAERTVNS ISDSYLDSTK DQVSLKSTLA  720
AVRNAAQAAA RIQAAFRAHS FKKRKQKEAA AEAASASAVG EVEDEYGILP SEIQGLSTAS  780
KAVFANSRDR DLHHAAALSI QKKYRGWKGR KDFLALRQKV VKIQAHVRGY QARKNYETIC  840
WAVGIVEKIV LRWYRKGVGL RGFHVDSIIG EDEEEEDFVK ALRKQKVDAA LTEAVSRVLS  900
MVQSQPARQQ YQRMLHKYRL AKEQRGDLQS EGASTSEGGM NEFM
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_023741813.10.0calmodulin-binding transcription activator 4-like
SwissprotQ9FYG20.0CMTA4_ARATH; Calmodulin-binding transcription activator 4
TrEMBLA0A2J6JY320.0A0A2J6JY32_LACSA; Uncharacterized protein
STRINGXP_009617256.10.0(Nicotiana tomentosiformis)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G67310.10.0Calmodulin-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]