PlantRegMap/PlantTFDB v5.0
Plant Transcription
Factor Database
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Transcription Factor Information
Basic Information? help Back to Top | |||||||||
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TF ID | Peinf101Scf00791g09030.1 | ||||||||
Organism | |||||||||
Taxonomic ID | |||||||||
Taxonomic Lineage |
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia; Petunia integrifolia
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Family | CAMTA | ||||||||
Protein Properties | Length: 1044aa MW: 117429 Da PI: 5.818 | ||||||||
Description | CAMTA family protein | ||||||||
Gene Model |
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Signature Domain? help Back to Top | |||||||
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No. | Domain | Score | E-value | Start | End | HMM Start | HMM End |
1 | CG-1 | 180 | 2.8e-56 | 20 | 136 | 3 | 118 |
CG-1 3 ke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYa 86 +e ++rwl++ ei++iL+n++++++t e++ rp sgs++L++rk++ryfrkDG++w+kkkdgktv+E+hekLKvg+++vl+cyYa Peinf101Scf00791g09030.1 20 SEaQHRWLRPAEICEILQNYRNFHITPEAPYRPVSGSVFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSIDVLHCYYA 104 4449********************************************************************************* PP CG-1 87 hseenptfqrrcywlLeeelekivlvhylevk 118 h+ee+ +fqrr+yw+Le++l +iv+vhylevk Peinf101Scf00791g09030.1 105 HGEEDDNFQRRSYWMLEQDLMHIVFVHYLEVK 136 *****************************985 PP |
Protein Features ? help Back to Top | ||||||
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Database | Entry ID | E-value | Start | End | InterPro ID | Description |
PROSITE profile | PS51437 | 81.47 | 15 | 141 | IPR005559 | CG-1 DNA-binding domain |
SMART | SM01076 | 8.2E-81 | 18 | 136 | IPR005559 | CG-1 DNA-binding domain |
Pfam | PF03859 | 7.5E-50 | 21 | 135 | IPR005559 | CG-1 DNA-binding domain |
Gene3D | G3DSA:2.60.40.10 | 4.8E-6 | 460 | 547 | IPR013783 | Immunoglobulin-like fold |
SuperFamily | SSF81296 | 6.86E-18 | 461 | 547 | IPR014756 | Immunoglobulin E-set |
Pfam | PF01833 | 9.3E-8 | 461 | 546 | IPR002909 | IPT domain |
SuperFamily | SSF48403 | 2.33E-16 | 651 | 752 | IPR020683 | Ankyrin repeat-containing domain |
Gene3D | G3DSA:1.25.40.20 | 1.7E-16 | 653 | 754 | IPR020683 | Ankyrin repeat-containing domain |
CDD | cd00204 | 1.30E-14 | 656 | 750 | No hit | No description |
PROSITE profile | PS50297 | 17.422 | 658 | 752 | IPR020683 | Ankyrin repeat-containing domain |
SMART | SM00248 | 4300 | 658 | 687 | IPR002110 | Ankyrin repeat |
PROSITE profile | PS50088 | 8.79 | 658 | 690 | IPR002110 | Ankyrin repeat |
PROSITE profile | PS50088 | 9.484 | 691 | 723 | IPR002110 | Ankyrin repeat |
SMART | SM00248 | 0.0036 | 691 | 720 | IPR002110 | Ankyrin repeat |
SMART | SM00248 | 3300 | 730 | 759 | IPR002110 | Ankyrin repeat |
SuperFamily | SSF52540 | 6.64E-7 | 861 | 916 | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
SMART | SM00015 | 7.3 | 865 | 887 | IPR000048 | IQ motif, EF-hand binding site |
PROSITE profile | PS50096 | 7.895 | 866 | 895 | IPR000048 | IQ motif, EF-hand binding site |
Pfam | PF00612 | 0.004 | 867 | 886 | IPR000048 | IQ motif, EF-hand binding site |
SMART | SM00015 | 0.0016 | 888 | 910 | IPR000048 | IQ motif, EF-hand binding site |
PROSITE profile | PS50096 | 9.432 | 889 | 913 | IPR000048 | IQ motif, EF-hand binding site |
Pfam | PF00612 | 1.9E-4 | 891 | 910 | IPR000048 | IQ motif, EF-hand binding site |
Gene Ontology ? help Back to Top | ||||||
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GO Term | GO Category | GO Description | ||||
GO:0009409 | Biological Process | response to cold | ||||
GO:0045893 | Biological Process | positive regulation of transcription, DNA-templated | ||||
GO:0071275 | Biological Process | cellular response to aluminum ion | ||||
GO:0005634 | Cellular Component | nucleus | ||||
GO:0003677 | Molecular Function | DNA binding | ||||
GO:0003700 | Molecular Function | transcription factor activity, sequence-specific DNA binding | ||||
GO:0005515 | Molecular Function | protein binding |
Sequence ? help Back to Top |
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Protein Sequence Length: 1044 aa Download sequence Send to blast |
MAGSGSDPPG FRLDIKQILS EAQHRWLRPA EICEILQNYR NFHITPEAPY RPVSGSVFLF 60 DRKVLRYFRK DGHNWRKKKD GKTVKEAHEK LKVGSIDVLH CYYAHGEEDD NFQRRSYWML 120 EQDLMHIVFV HYLEVKGNKA NVSSNRSIES AHSNYVKEYS LSDTFHGSHK KLASLKADSA 180 SLASTVTSAY EEAESEDSHQ VCSRFHSYPE LVSGMDSRLV ENRDTISKSY GSPLSSVEYP 240 SLPGIDGGGK CDLGNSASGP RRTNDLGSRA PVFERCSNGE VVSTHDFKNN MPVHGNWQFL 300 GQTVNQDLIA DSCYDLLNGF HSENLSSNQY TVRGQSYLYP DEQDEQQTEL NFQNLNSPME 360 VQADIIQENF MDMLGLGDYS TIKQPRLGSV KLEEGLNKSD SFSRWVAKEL EDVEELHMQS 420 TDRLSWNVID IEDDRSCVPS QLHVDSDSLV PSLSQEQLFS IIDFSPNWAY SSLETKVLIT 480 GRFLKSDCKV VECKWSCMFG EVEVPAEVLA DGVLRCHAPP HKPGVLPFYV TCSNRLACSE 540 VREFEYRLGP SREFGASNVS AIERHLLERF ESVMSLEPVS SCYSSDSPEA APEKQSTVNK 600 IICMMEEDMA DRPSDFDTSQ SKVKEDLFLE RKLRQNFYVW LVHQVTADGK GRTVLDDEGQ 660 GVLHLAAALG YDWALRPILA SGVSVDFRDM NGWTALHWAA FYGREKTVVG LVSLGASPGA 720 LTDPSAEFPL GRTPADLASA NRHKGISGFL AESSLTSHLS KLTVTDAKEE LASEVLGAKV 780 GETVTERVAV TSTGDDVPDV LSLKDSLAAI RNATQAAARI HQIFRVQSFQ RKQIIENNDN 840 ELSSDEHALS VVASRTCKLA QNNGIAHAAA IQIQKKFRGW NRRKEFLLIR QRIVKIQAHV 900 RGHQVRKKYK PIIWSVGILE KVILRWRRKG SGLRGFRSEA VMNKPSTEDD SLPEDDYDFL 960 KEGRKQTEVR MQKALARVKS MTQYPEARAQ YRRLLTAAEG LRETKEDGPT QVLENQKDAS 1020 YAEEDLFDVD NLLDEDTFMS IAFD |
3D Structure ? help Back to Top | ||||||
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PDB ID | Evalue | Query Start | Query End | Hit Start | Hit End | Description |
2cxk_A | 1e-13 | 461 | 551 | 9 | 93 | calmodulin binding transcription activator 1 |
2cxk_B | 1e-13 | 461 | 551 | 9 | 93 | calmodulin binding transcription activator 1 |
2cxk_C | 1e-13 | 461 | 551 | 9 | 93 | calmodulin binding transcription activator 1 |
2cxk_D | 1e-13 | 461 | 551 | 9 | 93 | calmodulin binding transcription activator 1 |
2cxk_E | 1e-13 | 461 | 551 | 9 | 93 | calmodulin binding transcription activator 1 |
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Functional Description ? help Back to Top | ||||||
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Source | Description | |||||
UniProt | Transcription 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 in freezing tolerance in association with CAMTA1 and CAMTA3. Contributes together with CAMTA1 and CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:23581962). Involved together with CAMTA3 and CAMTA4 in the positive regulation of a general stress response (PubMed:25039701). Involved in tolerance to aluminum. Binds to the promoter of ALMT1 transporter and contributes to the positive regulation of aluminum-induced expression of ALMT1 (PubMed:25627216). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:23581962, ECO:0000269|PubMed:25039701, ECO:0000269|PubMed:25627216, ECO:0000305|PubMed:11925432}. |
Binding Motif ? help Back to Top | |||
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Motif ID | Method | Source | Motif file |
MP00043 | PBM | Transfer from AT5G64220 | Download |
Regulation -- Description ? help Back to Top | ||||||
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Source | Description | |||||
UniProt | INDUCTION: By salt, wounding, abscisic acid, H(2)O(2) and salicylic acid (PubMed:12218065). Induced by aluminum (PubMed:25627216). {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:25627216}. |
Regulation -- PlantRegMap ? help Back to Top | ||||||
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Source | Upstream Regulator | Target Gene | ||||
PlantRegMap | Retrieve | Retrieve |
Annotation -- Protein ? help Back to Top | |||||||
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Source | Hit ID | E-value | Description | ||||
Refseq | XP_009600617.1 | 0.0 | PREDICTED: calmodulin-binding transcription activator 2-like isoform X1 | ||||
Swissprot | Q6NPP4 | 0.0 | CMTA2_ARATH; Calmodulin-binding transcription activator 2 | ||||
TrEMBL | A0A1S4BAF3 | 0.0 | A0A1S4BAF3_TOBAC; calmodulin-binding transcription activator 2-like isoform X1 | ||||
STRING | XP_009600617.1 | 0.0 | (Nicotiana tomentosiformis) |
Orthologous Group ? help Back to Top | |||
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Lineage | Orthologous Group ID | Taxa Number | Gene Number |
Asterids | OGEA2230 | 21 | 46 |
Best hit in Arabidopsis thaliana ? help Back to Top | ||||||
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Hit ID | E-value | Description | ||||
AT5G64220.2 | 0.0 | Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains |
Publications ? help Back to Top | |||
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