PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

PlantRegMap/PlantTFDB v5.0

Plant Transcription Factor Database

Transcription Factor Information

Basic Information | Signature Domain | Sequence |

Basic Information? help Back to Top

TF ID

Zmw_sc00816.1.g00110.1

Organism

Zoysia matrella

Taxonomic ID

38722

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.g00110.1	genome	ZGD	-

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	AP2	62.4	1e-19	671	721	1	55
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

Database	Entry ID	E-value	Start	End	InterPro ID	Description
SMART	SM00642	7.4E-46	148	484	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
SuperFamily	SSF51445	1.5E-63	148	481	IPR017853	Glycoside hydrolase superfamily
CDD	cd11314	3.30E-145	149	495	No hit	No description
Gene3D	G3DSA:3.20.20.80	2.2E-61	150	489	IPR013781	Glycoside hydrolase, catalytic domain
Pfam	PF00128	1.7E-10	171	465	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
PRINTS	PR00110	6.4E-5	238	249	IPR006046	Alpha amylase
PRINTS	PR00110	6.4E-5	338	349	IPR006046	Alpha amylase
PRINTS	PR00110	6.4E-5	422	434	IPR006046	Alpha amylase
SMART	SM00810	8.7E-23	485	545	IPR012850	Alpha-amylase, C-terminal beta-sheet
Pfam	PF07821	6.7E-13	486	541	IPR012850	Alpha-amylase, C-terminal beta-sheet
SuperFamily	SSF51011	1.04E-12	489	540	No hit	No description
Gene3D	G3DSA:2.60.40.1180	7.7E-20	490	540	IPR013780	Glycosyl hydrolase, all-beta
SuperFamily	SSF54171	1.31E-22	671	730	IPR016177	DNA-binding domain
Pfam	PF00847	2.0E-12	671	721	IPR001471	AP2/ERF domain
CDD	cd00018	5.43E-31	671	731	No hit	No description
Gene3D	G3DSA:3.30.730.10	9.2E-31	672	730	IPR001471	AP2/ERF domain
PROSITE profile	PS51032	25.343	672	729	IPR001471	AP2/ERF domain
SMART	SM00380	1.5E-36	672	735	IPR001471	AP2/ERF domain
PRINTS	PR00367	4.6E-10	673	684	IPR001471	AP2/ERF domain
PRINTS	PR00367	4.6E-10	695	711	IPR001471	AP2/ERF domain

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0005975	Biological Process	carbohydrate metabolic process
GO:0006355	Biological Process	regulation of transcription, DNA-templated
GO:0003677	Molecular Function	DNA binding
GO:0003700	Molecular Function	transcription factor activity, sequence-specific DNA binding
GO:0004556	Molecular Function	alpha-amylase activity
GO:0005509	Molecular Function	calcium 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

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

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
3wn6_A	0.0	148	540	2	398	Alpha-amylase
3wn6_B	0.0	148	540	2	398	Alpha-amylase
3wn6_C	0.0	148	540	2	398	Alpha-amylase
3wn6_D	0.0	148	540	2	398	Alpha-amylase
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Nucleic Localization Signal ? help Back to Top

No.	Start	End	Sequence
1	662	678	KRRRRARASKFRGVRRR
2	663	679	RRRRARASKFRGVRRRP

Functional Description ? help Back to Top
Source	Description
UniProt	Important for breakdown of endosperm starch during germination.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_004954023.1	0.0	alpha-amylase type B isozyme
Swissprot	P17654	0.0	AMY1_ORYSJ; Alpha-amylase
TrEMBL	K3YSN8	0.0	K3YSN8_SETIT; Alpha-amylase
STRING	Pavir.J03217.1.p	0.0	(Panicum virgatum)

Publications ? help Back to Top
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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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]