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

CCG032957.1

Organism

Populus euphratica

Taxonomic ID

75702

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus

Family

ERF

Protein Properties

Length: 1121aa MW: 125845 Da PI: 6.2772

Description

ERF family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
CCG032957.1	genome	LZU	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	AP2	38.9	2.1e-12	889	934	7	55
AP2 7 rwdkkrgrWvAeIrd.psengkrkrfslgkfgtaeeAakaaiaarkkleg 55 r+++ +grW+A+I + g +k+ +lg++ t eeAa a++ a+ +++g CCG032957.1 889 RRHHHNGRWEARIGRvF---G-NKYLYLGTYSTQEEAAHAYDIAAIEYRG 934 89999*****99966...3.6***********************97 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
SuperFamily	SSF51445	3.94E-69	525	845	IPR017853	Glycoside hydrolase superfamily
SMART	SM00642	2.0E-44	526	855	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
CDD	cd11314	9.47E-170	527	864	No hit	No description
Gene3D	G3DSA:3.20.20.80	1.7E-68	528	860	IPR013781	Glycoside hydrolase, catalytic domain
Pfam	PF00128	1.4E-18	547	837	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
PROSITE profile	PS51032	16.344	883	942	IPR001471	AP2/ERF domain
Pfam	PF00847	3.0E-8	889	934	IPR001471	AP2/ERF domain
SuperFamily	SSF54171	2.81E-14	890	944	IPR016177	DNA-binding domain
SMART	SM00380	1.0E-20	890	948	IPR001471	AP2/ERF domain
CDD	cd00018	8.11E-20	890	944	No hit	No description
Gene3D	G3DSA:3.30.730.10	1.5E-14	890	943	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:0009570	Cellular Component	chloroplast stroma
GO:0003677	Molecular Function	DNA binding
GO:0003700	Molecular Function	transcription factor activity, sequence-specific DNA binding
GO:0004556	Molecular Function	alpha-amylase activity

Sequence ? help Back to Top
Protein Sequence Length: 1121 aa Download sequence Send to blast
MSAVSVEPFL RYPRFEKPGF ARSRRKAAIT VTTAALFKSP SSFNCCCSLI PRRKLLSNAS 60 SFPFLDLHRV KTHTARASST DTAVLESTND VVFKETFPLS RTETTEGKIF VRLDQSKAKE 120 KEDQWQQLTV GCSLPGKWIL HWGVSYVDDT GSEWDQPPEN MRPPGSIPVK DYAIETPLKK 180 ASEGDKFHQV KIEIDPKSPV AALNFVLKDE ETGVWYQHKG RDFKVPLVDC SLDSGGGNVI 240 GAKGGFSMWP GTMLSNMFLK ADALASEGKD SSSRSKDPKQ ETRKVEGFYE ELPIAKFAVI 300 ENSVTVSVSK CLKTAKNLLY LVTDLPGEVV VHWGVCRDDA KKWEIPAAPH PPETTVFKDK 360 ALRTVLQAKE DGNGRSGSFT LDGDLVGFLF VLKLNESTWL NCMGNDFYIP LPISSSLPAL 420 SGTGQSEVPP VSENTVGADQ EVSHAIYTDG IINEIRSLVS DFSSEKRQKT KTKEAQESIL 480 QEIEKLAAEA YSIFRSSIPT FMDETALESE ATEAPKICSG TGTGYEILLQ GFNWESHKLG 540 HWYMELKQKV EEISSLGFTV IWLPPPTESV SPEGYMPKDL YNLNSRYGNI DELKDLVKRF 600 HGKGVKVLGD AVLNHRCAHY KNGNGVWNIF GGRLNWDDRA VVADDPHFQG RGNKSSGDNF 660 HAAPNIDHSQ EFVRKDLKEW LLWLRKEIGY DGWRLDFVRG FWGGYVKDYL DASEPYFAVG 720 EYWDSLSYTY GEMDHNQDAH RQRIVDWINA TSGTAGAFDV TTKGILHTTL ERCEYWRLSD 780 EKGKPPGVVG WWPSRAVTFI ENHDTGSTQG HWRFPGGKEM QGYAYILTHP GTPAVFYDHI 840 FSHYQSEIAA LISLRNRNKI HCRSTESDYE KEIEIMKTVT KEEYLASLRR HHHNGRWEAR 900 IGRVFGNKYL YLGTYSTQEE AAHAYDIAAI EYRGINAVTN FDLSTYIRWL KPEASLPAPQ 960 ESKPASGPPP MATFSNHLPI EKPTQLSVLQ MDPSLIDNLS TPKNEDVFHR KTLPASPLTR 1020 SSSSTALSLL FKSSIFKELV EKNLNTTCEE TEENDSKNQH NGNNNAGEAF YDGFSPIPHP 1080 GTSNEDRFLC SEQGERNTLP PYNEMEPSLW NGALSMPSRF H

Sequence ? help Back to Top

Protein Sequence Length: 1121 aa Download sequence Send to blast

MSAVSVEPFL RYPRFEKPGF ARSRRKAAIT VTTAALFKSP SSFNCCCSLI PRRKLLSNAS  60
SFPFLDLHRV KTHTARASST DTAVLESTND VVFKETFPLS RTETTEGKIF VRLDQSKAKE  120
KEDQWQQLTV GCSLPGKWIL HWGVSYVDDT GSEWDQPPEN MRPPGSIPVK DYAIETPLKK  180
ASEGDKFHQV KIEIDPKSPV AALNFVLKDE ETGVWYQHKG RDFKVPLVDC SLDSGGGNVI  240
GAKGGFSMWP GTMLSNMFLK ADALASEGKD SSSRSKDPKQ ETRKVEGFYE ELPIAKFAVI  300
ENSVTVSVSK CLKTAKNLLY LVTDLPGEVV VHWGVCRDDA KKWEIPAAPH PPETTVFKDK  360
ALRTVLQAKE DGNGRSGSFT LDGDLVGFLF VLKLNESTWL NCMGNDFYIP LPISSSLPAL  420
SGTGQSEVPP VSENTVGADQ EVSHAIYTDG IINEIRSLVS DFSSEKRQKT KTKEAQESIL  480
QEIEKLAAEA YSIFRSSIPT FMDETALESE ATEAPKICSG TGTGYEILLQ GFNWESHKLG  540
HWYMELKQKV EEISSLGFTV IWLPPPTESV SPEGYMPKDL YNLNSRYGNI DELKDLVKRF  600
HGKGVKVLGD AVLNHRCAHY KNGNGVWNIF GGRLNWDDRA VVADDPHFQG RGNKSSGDNF  660
HAAPNIDHSQ EFVRKDLKEW LLWLRKEIGY DGWRLDFVRG FWGGYVKDYL DASEPYFAVG  720
EYWDSLSYTY GEMDHNQDAH RQRIVDWINA TSGTAGAFDV TTKGILHTTL ERCEYWRLSD  780
EKGKPPGVVG WWPSRAVTFI ENHDTGSTQG HWRFPGGKEM QGYAYILTHP GTPAVFYDHI  840
FSHYQSEIAA LISLRNRNKI HCRSTESDYE KEIEIMKTVT KEEYLASLRR HHHNGRWEAR  900
IGRVFGNKYL YLGTYSTQEE AAHAYDIAAI EYRGINAVTN FDLSTYIRWL KPEASLPAPQ  960
ESKPASGPPP MATFSNHLPI EKPTQLSVLQ MDPSLIDNLS TPKNEDVFHR KTLPASPLTR  1020
SSSSTALSLL FKSSIFKELV EKNLNTTCEE TEENDSKNQH NGNNNAGEAF YDGFSPIPHP  1080
GTSNEDRFLC SEQGERNTLP PYNEMEPSLW NGALSMPSRF H

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
3bsg_A	1e-115	525	865	1	353	Alpha-amylase type A isozyme
Search in ModeBase

Functional Description ? help Back to Top
Source	Description
UniProt	Possesses endoamylolytic activity in vitro, but seems not required for breakdown of transitory starch in leaves. May be involved in the determination of the final structure of glucans by shortening long linear phospho-oligosaccharides in the chloroplast stroma. Can act on both soluble and insoluble glucan substrates to release small linear and branched malto-oligosaccharides (PubMed:24089528). Works synergistically with beta-amylase toward efficient starch degradation (PubMed:24089528). Has activity against p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528). Involved in stress-induced starch degradation (PubMed:27436713). {ECO:0000269\|PubMed:15637061, ECO:0000269\|PubMed:19074683, ECO:0000269\|PubMed:19141707, ECO:0000269\|PubMed:21294843, ECO:0000269\|PubMed:24089528, ECO:0000269\|PubMed:27436713}.

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: Circadian-regulation. Expression increases during the light phase and decreases during the dark phase. Up-regulated during osmotic stress and by abscisic acid (PubMed:27436713). {ECO:0000269\|PubMed:15347792, ECO:0000269\|PubMed:15637061, ECO:0000269\|PubMed:27436713}.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_011021595.1	0.0	PREDICTED: alpha-amylase 3, chloroplastic isoform X1
Swissprot	Q94A41	0.0	AMY3_ARATH; Alpha-amylase 3, chloroplastic
TrEMBL	A0A2K1YRA8	0.0	A0A2K1YRA8_POPTR; Uncharacterized protein
STRING	POPTR_0010s10300.1	0.0	(Populus trichocarpa)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT3G54320.2	3e-32	ERF family protein

Publications ? help Back to Top
Wienkoop S, et al. Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins. Rapid Commun. Mass Spectrom., 2004. 18(6): p. 643-50 [PMID:15052571] Yu TS, et al. alpha-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves. J. Biol. Chem., 2005. 280(11): p. 9773-9 [PMID:15637061] Weise SE,Kim KS,Stewart RP,Sharkey TD beta-Maltose is the metabolically active anomer of maltose during transitory starch degradation. Plant Physiol., 2005. 137(2): p. 756-61 [PMID:15665241] Smith AM,Zeeman SC,Smith SM Starch degradation. Annu Rev Plant Biol, 2005. 56: p. 73-98 [PMID:15862090] Kim YC,Nakajima M,Nakayama A,Yamaguchi I Contribution of gibberellins to the formation of Arabidopsis seed coat through starch degradation. Plant Cell Physiol., 2005. 46(8): p. 1317-25 [PMID:15927942] Delatte T, et al. Evidence for distinct mechanisms of starch granule breakdown in plants. J. Biol. Chem., 2006. 281(17): p. 12050-9 [PMID:16495218] Doyle EA,Lane AM,Sides JM,Mudgett MB,Monroe JD An alpha-amylase (At4g25000) in Arabidopsis leaves is secreted and induced by biotic and abiotic stress. Plant Cell Environ., 2007. 30(4): p. 388-98 [PMID:17324226] Rutschow H,Ytterberg AJ,Friso G,Nilsson R,van Wijk KJ Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiol., 2008. 148(1): p. 156-75 [PMID:18633119] Covington MF,Maloof JN,Straume M,Kay SA,Harmer SL Global transcriptome analysis reveals circadian regulation of key pathways in plant growth and development. Genome Biol., 2008. 9(8): p. R130 [PMID:18710561] Lohmeier-Vogel EM, et al. Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein. BMC Plant Biol., 2008. 8: p. 120 [PMID:19038037] Streb S, et al. Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase. Plant Cell, 2008. 20(12): p. 3448-66 [PMID:19074683] Kötting O, et al. STARCH-EXCESS4 is a laforin-like Phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana. Plant Cell, 2009. 21(1): p. 334-46 [PMID:19141707] Jie W,Dashi Y,XinHong G,Xuanming L Arabidopsis AMY1 expressions and early flowering mutant phenotype. BMB Rep, 2009. 42(2): p. 101-5 [PMID:19250611] Purdy SJ,Bussell JD,Nelson DC,Villadsen D,Smith SM A nuclear-localized protein, KOLD SENSITIV-1, affects the expression of cold-responsive genes during prolonged chilling in Arabidopsis. J. Plant Physiol., 2011. 168(3): p. 263-9 [PMID:20674078] Glaring MA, et al. Starch-binding domains in the CBM45 family--low-affinity domains from glucan, water dikinase and α-amylase involved in plastidial starch metabolism. FEBS J., 2011. 278(7): p. 1175-85 [PMID:21294843] Glaring MA,Skryhan K,Kötting O,Zeeman SC,Blennow A Comprehensive survey of redox sensitive starch metabolising enzymes in Arabidopsis thaliana. Plant Physiol. Biochem., 2012. 58: p. 89-97 [PMID:22789914] Streb S,Eicke S,Zeeman SC The simultaneous abolition of three starch hydrolases blocks transient starch breakdown in Arabidopsis. J. Biol. Chem., 2012. 287(50): p. 41745-56 [PMID:23019330] Seung D, et al. Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic α-amylase. J. Biol. Chem., 2013. 288(47): p. 33620-33 [PMID:24089528] Horrer D, et al. Blue Light Induces a Distinct Starch Degradation Pathway in Guard Cells for Stomatal Opening. Curr. Biol., 2016. 26(3): p. 362-70 [PMID:26774787] Thalmann M, et al. Regulation of Leaf Starch Degradation by Abscisic Acid Is Important for Osmotic Stress Tolerance in Plants. Plant Cell, 2016. 28(8): p. 1860-78 [PMID:27436713] Seung D,Lu KJ,Stettler M,Streb S,Zeeman SC Degradation of Glucan Primers in the Absence of Starch Synthase 4 Disrupts Starch Granule Initiation in Arabidopsis. J. Biol. Chem., 2016. 291(39): p. 20718-28 [PMID:27458017] Baslam M, et al. Genetic and isotope ratio mass spectrometric evidence for the occurrence of starch degradation and cycling in illuminated Arabidopsis leaves. PLoS ONE, 2017. 12(2): p. e0171245 [PMID:28152100]