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 462962708
Organism
Eragrostis tef
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; PACMAD clade; Chloridoideae; Eragrostideae; Eragrostidinae; Eragrostis
Family C2H2
Protein Properties Length: 799aa    MW: 87231.9 Da    PI: 8.0902
Description C2H2 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
462962708genomeTefView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-C2H214.30.00012159182123
                EEETTTTEEESSHHHHHHHHHH.T CS
    zf-C2H2   1 ykCpdCgksFsrksnLkrHirt.H 23 
                ++C+ Cg++ +r+ +L+ H  t H
  462962708 159 FPCKVCGEVLTRPQQLELHHATnH 182
                89*****************99988 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS501578.891159187IPR007087Zinc finger, C2H2
PROSITE patternPS000280161182IPR007087Zinc finger, C2H2
SuperFamilySSF563992.39E-6184234No hitNo description
Gene3DG3DSA:3.90.228.105.3E-5184353IPR012317Poly(ADP-ribose) polymerase, catalytic domain
SuperFamilySSF563992.39E-6261398No hitNo description
PfamPF047156.2E-24352472IPR006805Anthranilate synthase component I, N-terminal
SuperFamilySSF563223.4E-104352765IPR005801ADC synthase
Gene3DG3DSA:3.60.120.101.8E-55354606IPR005801ADC synthase
PfamPF004251.3E-15533607IPR015890Chorismate-utilising enzyme, C-terminal
PfamPF004252.5E-41604753IPR015890Chorismate-utilising enzyme, C-terminal
Gene3DG3DSA:3.60.120.101.2E-61607767IPR005801ADC synthase
PRINTSPR000954.6E-5677691IPR019999Anthranilate synthase component I-like
PRINTSPR000954.6E-5692706IPR019999Anthranilate synthase component I-like
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0009058Biological Processbiosynthetic process
GO:0003950Molecular FunctionNAD+ ADP-ribosyltransferase activity
GO:0016833Molecular Functionoxo-acid-lyase activity
GO:0046872Molecular Functionmetal ion binding
Sequence ? help Back to Top
Protein Sequence    Length: 799 aa     Download sequence    Send to blast
MAAGSGSLLR GFLSLFFLLF IHIGHASCCF SPGPASRQRE EDGAADAASA DGVVAGGRGG  60
GKRRKISPLA FSPAASSSAA AADDRDIRGR IHRIFASAAG AKNGAVVAGR EAEEEGEAVT  120
TTTVSSPQAQ SLAPQPSASL KASRRSSSRS FAARGDVLFP CKVCGEVLTR PQQLELHHAT  180
NHSLSELSHL DSSTNIIRMI FLAGWKSGAG GDAPAAVVRR VLRIHHNPRA LARFEEYRDL  240
VRARAARRCV EAAGAGVAEE ERCVADGNER LRFHCSTMLC PQLGAGGGAC RSPYCCVCST  300
LRHGFAGKQA DVDGVATYAS AWAAHAALPD DVEREFAFLQ VRRAMLVCRV VAGRGRYSMV  360
GAHPVMEIVA KEHKVTIMDH EKGEVTEQIV EDPMQVPRSM MEGWNPQQID ELPDSFSGGW  420
VGFFSYDTVR YVEKKKLPFS GAPQDDRNLP DVHLGLYDDV LVFDNVEKKV YVIHWVNLDR  480
HASAEEAYED GRSRLNLLLS KVHNSNVPTL SPGFVKLHTR QFGTPLNKST MTSDEYKNAV  540
MKAKEHIVAG DIFQIVLSQR FERRTYANPF EVYRALRIVN PSPYMAYVQA RGCVLVASSP  600
EILTRVKKVS KPGSVKVEKL MNIERYSHVM HISSTVSGQL DDHLQSWDAL RAALPVGTVS  660
GAPKVKAMEL IDELEVTRRG PYSGGLGGIS FDGDMQIALS LRTIVFSTAP SHNTMYSFKA  720
ADRRREWVAH LQAGAGIVAD SSPDDEQREC ENKAAALARA IDLAESAFVD KEYRGYKKLL  780
FVQEVYLSEH RIPHAGNDY
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5kck_A3e-5235675940449Anthranilate synthase component I
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtPart of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate. {ECO:0000269|PubMed:15159631}.
Cis-element ? help Back to Top
SourceLink
PlantRegMap462962708
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By chitin oligosaccharide elicitor and the phytopathogenic fungus Bipolaris oryzae. {ECO:0000269|PubMed:11500548, ECO:0000269|PubMed:18266919}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAB0226030.0AB022603.1 Oryza sativa Japonica Group OsASA2 mRNA for anthranilate synthase alpha 2 subunit, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_025795999.10.0anthranilate synthase alpha subunit 2, chloroplastic
SwissprotQ9XJ290.0ASA2_ORYSJ; Anthranilate synthase alpha subunit 2, chloroplastic
TrEMBLA0A2S3IS580.0A0A2S3IS58_9POAL; Uncharacterized protein
TrEMBLA0A2T7CEN70.0A0A2T7CEN7_9POAL; Uncharacterized protein
TrEMBLA0A3L6S6C20.0A0A3L6S6C2_PANMI; Anthranilate synthase alpha subunit 2, chloroplastic
STRINGGRMZM2G161337_P010.0(Zea mays)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G29660.18e-30C2H2 family protein
Publications ? help Back to Top
  1. Tozawa Y,Hasegawa H,Terakawa T,Wakasa K
    Characterization of rice anthranilate synthase alpha-subunit genes OASA1 and OASA2. Tryptophan accumulation in transgenic rice expressing a feedback-insensitive mutant of OASA1.
    Plant Physiol., 2001. 126(4): p. 1493-506
    [PMID:11500548]
  2. Kanno T,Kasai K,Ikejiri-Kanno Y,Wakasa K,Tozawa Y
    In vitro reconstitution of rice anthranilate synthase: distinct functional properties of the alpha subunits OASA1 and OASA2.
    Plant Mol. Biol., 2004. 54(1): p. 11-22
    [PMID:15159631]
  3. Kim DS,Lee IS,Jang CS,Kang SY,Seo YW
    Characterization of the altered anthranilate synthase in 5-methyltryptophan-resistant rice mutants.
    Plant Cell Rep., 2005. 24(6): p. 357-65
    [PMID:15776237]
  4. Kanno T, et al.
    Structure-based in vitro engineering of the anthranilate synthase, a metabolic key enzyme in the plant tryptophan pathway.
    Plant Physiol., 2005. 138(4): p. 2260-8
    [PMID:16040654]
  5. Ishihara A, et al.
    The tryptophan pathway is involved in the defense responses of rice against pathogenic infection via serotonin production.
    Plant J., 2008. 54(3): p. 481-95
    [PMID:18266919]
  6. Saika H, et al.
    Application of gene targeting to designed mutation breeding of high-tryptophan rice.
    Plant Physiol., 2011. 156(3): p. 1269-77
    [PMID:21543727]