PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Zmw_sc00816.1.g00110.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; PACMAD clade; Chloridoideae; Zoysieae; Zoysiinae; Zoysia
Family ERF
Protein Properties Length: 778aa    MW: 86002.5 Da    PI: 8.7881
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Zmw_sc00816.1.g00110.1genomeZGD-
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP262.41e-19671721155
                           AP2   1 sgykGVrwdkkrgrWvAeIrdpsengkr..krfslgkfgtaeeAakaaiaarkkleg 55 
                                   s+++GVr+++ +g+WvAeIrdp     +   r +lg+f+taeeAa+a++ a+ +++g
  Zmw_sc00816.1.g00110.1.am.mk 671 SKFRGVRRRP-WGKWVAEIRDP-----HraVRKWLGTFDTAEEAARAYDVAAVEFRG 721
                                   79********.**********7.....338***********************9998 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM006427.4E-46148484IPR006047Glycosyl hydrolase, family 13, catalytic domain
SuperFamilySSF514451.5E-63148481IPR017853Glycoside hydrolase superfamily
CDDcd113143.30E-145149495No hitNo description
Gene3DG3DSA:3.20.20.802.2E-61150489IPR013781Glycoside hydrolase, catalytic domain
PfamPF001281.7E-10171465IPR006047Glycosyl hydrolase, family 13, catalytic domain
PRINTSPR001106.4E-5238249IPR006046Alpha amylase
PRINTSPR001106.4E-5338349IPR006046Alpha amylase
PRINTSPR001106.4E-5422434IPR006046Alpha amylase
SMARTSM008108.7E-23485545IPR012850Alpha-amylase, C-terminal beta-sheet
PfamPF078216.7E-13486541IPR012850Alpha-amylase, C-terminal beta-sheet
SuperFamilySSF510111.04E-12489540No hitNo description
Gene3DG3DSA:2.60.40.11807.7E-20490540IPR013780Glycosyl hydrolase, all-beta
SuperFamilySSF541711.31E-22671730IPR016177DNA-binding domain
PfamPF008472.0E-12671721IPR001471AP2/ERF domain
CDDcd000185.43E-31671731No hitNo description
Gene3DG3DSA:3.30.730.109.2E-31672730IPR001471AP2/ERF domain
PROSITE profilePS5103225.343672729IPR001471AP2/ERF domain
SMARTSM003801.5E-36672735IPR001471AP2/ERF domain
PRINTSPR003674.6E-10673684IPR001471AP2/ERF domain
PRINTSPR003674.6E-10695711IPR001471AP2/ERF domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0005975Biological Processcarbohydrate metabolic process
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0003677Molecular FunctionDNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0004556Molecular Functionalpha-amylase activity
GO:0005509Molecular Functioncalcium ion binding
Sequence ? help Back to Top
Protein Sequence    Length: 778 aa     Download sequence    Send to blast
MFMGFCSEDV FLVVMKEMCR LAWASSPLDY KEQTPLQLAL ATSRLIARHL HQINQRSSSL  60
VHSCLSRTPS LAIKSPTGSL WPIKQTPAAA GRYLFIHFSQ KQRRSATAPP QKVASGAPAV  120
LNNMVNRFLT LAVLIVFLGA SKNYAAGQIL FQGFNRESWK QQGGWYNLLM SKVEDIADAG  180
ITHVWLPPPS HSIAEQGALF SASRLRRYMP GRLYDLDASK YGNKAQLKSL IQAFHAKGVK  240
VIADIVINHR TAEHEDGRGI YCMFEGGTPD SRLDWGPHMI CRDDRQYADG TGNLDTGADF  300
GGAPDVDHLN SRVQRELVGW LNWLKTDVSF DAWLLDFAKG YSADVAKVYI DNTEPCFAVA  360
EIWTSLAYGG DGKPNYNQSA HRQELVNWVD RVGRSGPATV FDFTTKGILN VGVEGEPPTA  420
WRLAVTFVDN HDTGSTQHMW PFPSEKVMQG YAYILTHPGN PCIFYDHFFD WGLKNEIAHL  480
VSIRNRHGIH PESELRIIAS DADLYLTEID GKVITKLGPR YDIEHLIPKG FQIAAHGDGY  540
TRPCATFLRH RRTGASMVPR LERGGFTLPN AEQENSLFLR ALISVVSGDT AVPTLDDLAE  600
TKPHVAAATA PAAAAAYCPR CGVLGCPGCE PFAGNAAATT GLSSDSEEER ESASHVVTGC  660
VGKRRRRARA SKFRGVRRRP WGKWVAEIRD PHRAVRKWLG TFDTAEEAAR AYDVAAVEFR  720
GRRAKLNFPA DAAAVLSAHS SWAMVQPMAE SLRESCGRQP GGSEEEGRWR RTRRSGKG
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
3wn6_A0.01485402398Alpha-amylase
3wn6_B0.01485402398Alpha-amylase
3wn6_C0.01485402398Alpha-amylase
3wn6_D0.01485402398Alpha-amylase
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1662678KRRRRARASKFRGVRRR
2663679RRRRARASKFRGVRRRP
Functional Description ? help Back to Top
Source Description
UniProtImportant for breakdown of endosperm starch during germination.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_004954023.10.0alpha-amylase type B isozyme
SwissprotP176540.0AMY1_ORYSJ; Alpha-amylase
TrEMBLK3YSN80.0K3YSN8_SETIT; Alpha-amylase
STRINGPavir.J03217.1.p0.0(Panicum virgatum)
Publications ? help Back to Top
  1. Hwang YS,Thomas BR,Rodriguez RL
    Differential expression of rice alpha-amylase genes during seedling development under anoxia.
    Plant Mol. Biol., 1999. 40(6): p. 911-20
    [PMID:10527416]
  2. Kaneko M,Itoh H,Ueguchi-Tanaka M,Ashikari M,Matsuoka M
    The alpha-amylase induction in endosperm during rice seed germination is caused by gibberellin synthesized in epithelium.
    Plant Physiol., 2002. 128(4): p. 1264-70
    [PMID:11950975]
  3. Itoh K, et al.
    Developmental and Hormonal Regulation of Rice [alpha]-Amylase(RAmy1A)-gusA Fusion Genes in Transgenic Rice Seeds.
    Plant Physiol., 1995. 107(1): p. 25-31
    [PMID:12228339]
  4. Laurie S,McKibbin RS,Halford NG
    Antisense SNF1-related (SnRK1) protein kinase gene represses transient activity of an alpha-amylase (alpha-Amy2) gene promoter in cultured wheat embryos.
    J. Exp. Bot., 2003. 54(383): p. 739-47
    [PMID:12554717]
  5. Sutoh K,Yamauchi D
    Two cis-acting elements necessary and sufficient for gibberellin-upregulated proteinase expression in rice seeds.
    Plant J., 2003. 34(5): p. 635-45
    [PMID:12787245]
  6. Washio K
    Functional dissections between GAMYB and Dof transcription factors suggest a role for protein-protein associations in the gibberellin-mediated expression of the RAmy1A gene in the rice aleurone.
    Plant Physiol., 2003. 133(2): p. 850-63
    [PMID:14500792]
  7. Huang N,Stebbins GL,Rodriguez RL
    Classification and evolution of alpha-amylase genes in plants.
    Proc. Natl. Acad. Sci. U.S.A., 1992. 89(16): p. 7526-30
    [PMID:1502164]
  8. Zhang Y, et al.
    Gibberellin homeostasis and plant height control by EUI and a role for gibberellin in root gravity responses in rice.
    Cell Res., 2008. 18(3): p. 412-21
    [PMID:18268540]
  9. Karrer EE,Litts JC,Rodriguez RL
    Differential expression of alpha-amylase genes in germinating rice and barley seeds.
    Plant Mol. Biol., 1991. 16(5): p. 797-805
    [PMID:1859866]
  10. Kitajima A, et al.
    The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids.
    Plant Cell, 2009. 21(9): p. 2844-58
    [PMID:19767453]
  11. Huang N,Sutliff TD,Litts JC,Rodriguez RL
    Classification and characterization of the rice alpha-amylase multigene family.
    Plant Mol. Biol., 1990. 14(5): p. 655-68
    [PMID:2102847]
  12. Huang N,Koizumi N,Reinl S,Rodriguez RL
    Structural organization and differential expression of rice alpha-amylase genes.
    Nucleic Acids Res., 1990. 18(23): p. 7007-14
    [PMID:2263460]
  13. Hakata M, et al.
    Suppression of α-amylase genes improves quality of rice grain ripened under high temperature.
    Plant Biotechnol. J., 2012. 10(9): p. 1110-7
    [PMID:22967050]
  14. Ochiai A, et al.
    α-Amylase is a potential growth inhibitor of Porphyromonas gingivalis, a periodontal pathogenic bacterium.
    J. Periodont. Res., 2014. 49(1): p. 62-8
    [PMID:23550921]
  15. O'Neill SD, et al.
    The alpha-amylase genes in Oryza sativa: characterization of cDNA clones and mRNA expression during seed germination.
    Mol. Gen. Genet., 1990. 221(2): p. 235-44
    [PMID:2370848]
  16. Schmidt R, et al.
    SALT-RESPONSIVE ERF1 is a negative regulator of grain filling and gibberellin-mediated seedling establishment in rice.
    Mol Plant, 2014. 7(2): p. 404-21
    [PMID:24046061]
  17. Zhang D, et al.
    OsRACK1 is involved in abscisic acid- and H2O2-mediated signaling to regulate seed germination in rice (Oryza sativa, L.).
    PLoS ONE, 2014. 9(5): p. e97120
    [PMID:24865690]
  18. Ochiai A, et al.
    Crystal structure of α-amylase from Oryza sativa: molecular insights into enzyme activity and thermostability.
    Biosci. Biotechnol. Biochem., 2014. 78(6): p. 989-97
    [PMID:25036124]
  19. Taniguchi M, et al.
    Antimicrobial activity and mechanism of action of a novel cationic α-helical octadecapeptide derived from α-amylase of rice.
    Biopolymers, 2015. 104(2): p. 73-83
    [PMID:25581614]
  20. Celińska E,Borkowska M,Białas W
    Evaluation of a recombinant insect-derived amylase performance in simultaneous saccharification and fermentation process with industrial yeasts.
    Appl. Microbiol. Biotechnol., 2016. 100(6): p. 2693-707
    [PMID:26545757]
  21. Taniguchi M, et al.
    Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice.
    Peptides, 2016. 75: p. 101-8
    [PMID:26643956]
  22. Taniguchi M, et al.
    Effect of alanine, leucine, and arginine substitution on antimicrobial activity against candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice.
    Biopolymers, 2016. 106(2): p. 219-229
    [PMID:26850838]
  23. Taniguchi M, et al.
    AmyI-1-18, a cationic α-helical antimicrobial octadecapeptide derived from α-amylase in rice, inhibits the translation and folding processes in a protein synthesis system.
    J. Biosci. Bioeng., 2016. 122(4): p. 385-92
    [PMID:27038670]
  24. Taniguchi M, et al.
    Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-18 and its amino acid-substituted analogs.
    J. Biosci. Bioeng., 2016. 122(6): p. 652-659
    [PMID:27478151]
  25. Terashima M,Kubo A,Suzawa M,Itoh Y,Katoh S
    The roles of the N-linked carbohydrate chain of rice alpha-amylase in thermostability and enzyme kinetics.
    Eur. J. Biochem., 1994. 226(1): p. 249-54
    [PMID:7957256]
  26. Mitsunaga S,Rodriguez RL,Yamaguchi J
    Sequence-specific interactions of a nuclear protein factor with the promoter region of a rice gene for alpha-amylase, RAmy3D.
    Nucleic Acids Res., 1994. 22(11): p. 1948-53
    [PMID:8028999]
  27. Terashima M,Katoh S,Thomas BR,Rodriguez RL
    Characterization of rice alpha-amylase isozymes expressed by Saccharomyces cerevisiae.
    Appl. Microbiol. Biotechnol., 1995. 43(6): p. 1050-5
    [PMID:8590656]
  28. Mitsui T,Yamaguchi J,Akazawa T
    Physicochemical and serological characterization of rice alpha-amylase isoforms and identification of their corresponding genes.
    Plant Physiol., 1996. 110(4): p. 1395-404
    [PMID:8934629]
  29. Terashima M,Hosono M,Katoh S
    Functional roles of protein domains on rice alpha-amylase activity.
    Appl. Microbiol. Biotechnol., 1997. 47(4): p. 364-7
    [PMID:9163949]
  30. Kashem MA, et al.
    Effects of (+)-8',8',8'-trifluoroabscisic acid on alpha-amylase expression and sugar accumulation in rice cells.
    Planta, 1998. 205(3): p. 319-26
    [PMID:9640660]