PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; Asparagales; Orchidaceae; Epidendroideae; Vandeae; Aeridinae; Phalaenopsis

Family

G2-like

Protein Properties

Length: 588aa MW: 64331.9 Da PI: 5.3254

Description

G2-like family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
PEQU_16234	genome	BGI	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	G2-like	77.5	1.7e-24	135	186	1	53
G2-like 1 kprlrWtpeLHerFveaveqLGGsekAtPktilelmkvkgLtlehvkSHLQkY 53 k++++Wt eLH+rFv+aveqL G ekA+P++ilelm++++Lt+++v+SHLQ + PEQU_16234 135 KKKVDWTAELHRRFVQAVEQL-GVEKAVPSRILELMGIDCLTRHNVASHLQTF 186 6899***************.***************************87 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
PROSITE profile	PS51294	12.673	132	189	IPR017930	Myb domain
Gene3D	G3DSA:1.10.10.60	8.7E-22	133	186	IPR009057	Homeodomain-like
TIGRFAMs	TIGR01557	2.2E-23	135	186	IPR006447	Myb domain, plants
SuperFamily	SSF46689	6.99E-15	135	186	IPR009057	Homeodomain-like
Pfam	PF00249	5.4E-6	138	185	IPR001005	SANT/Myb domain
SMART	SM01329	1.5E-75	235	580	IPR024084	Isopropylmalate dehydrogenase-like domain
Pfam	PF00180	1.6E-71	258	580	IPR024084	Isopropylmalate dehydrogenase-like domain
Gene3D	G3DSA:3.40.718.10	1.7E-139	261	586	IPR024084	Isopropylmalate dehydrogenase-like domain
TIGRFAMs	TIGR00127	3.8E-191	261	588	IPR004790	Isocitrate dehydrogenase NADP-dependent
SuperFamily	SSF53659	1.06E-118	261	587	No hit	No description
PROSITE pattern	PS00470	0	451	470	IPR019818	Isocitrate/isopropylmalate dehydrogenase, conserved site

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0006102	Biological Process	isocitrate metabolic process
GO:0055114	Biological Process	oxidation-reduction process
GO:0000287	Molecular Function	magnesium ion binding
GO:0003677	Molecular Function	DNA binding
GO:0004450	Molecular Function	isocitrate dehydrogenase (NADP+) activity
GO:0051287	Molecular Function	NAD binding

Sequence ? help Back to Top
Protein Sequence Length: 588 aa Download sequence Send to blast
MLAVTPLRTS TPGDLAGEVG GAAANLPTSD DFSLDFDFDF SELFAGFDDA ETLPALDGDA 60 ADLPAARAET NGGGANTQQD EREEKIALID PEEVLNCEVK DEPSASSDIS SPAPDKHKER 120 GRKSSAGQHK GSNGKKKVDW TAELHRRFVQ AVEQLGVEKA VPSRILELMG IDCLTRHNVA 180 SHLQTFPAVP VPGIPPLPMC RPDGVIPTAA PPGPPPCKQT GWLHQLEAHP SKESIDAALG 240 VVLAQPWLPL PLGLKPPSLE NEARVKEFSL KAMWKSPNGT IRNILNGTVF REPILCKNVP 300 RLVPGWTKPI CIGRHAFGDQ YRATDLVIKG PGKLRLVFEG KEEQIDLEVF NFTGEGGVAL 360 SMYNTDESIR AFADSSMNTA YQKKWPLYLS TKNTILKKYD GRFKDIFQEV YESKWKSLFE 420 ESGIWYEHRL IDDMVAYAVK SEGGYVWACK NYDGDVQSDF LAQGFGSLGL MTSVLVCPDG 480 KTIEAEAAHG TVTRHYRVHQ KGGETSTNSI ASIFAWTRGL AHRAKLDDNA ELLAFTEKLE 540 AACVETVESG KMTKDLALII HGSKLSREQY LTTEEFIDAV AQGLKAKL

Sequence ? help Back to Top

Protein Sequence Length: 588 aa Download sequence Send to blast

MLAVTPLRTS TPGDLAGEVG GAAANLPTSD DFSLDFDFDF SELFAGFDDA ETLPALDGDA  60
ADLPAARAET NGGGANTQQD EREEKIALID PEEVLNCEVK DEPSASSDIS SPAPDKHKER  120
GRKSSAGQHK GSNGKKKVDW TAELHRRFVQ AVEQLGVEKA VPSRILELMG IDCLTRHNVA  180
SHLQTFPAVP VPGIPPLPMC RPDGVIPTAA PPGPPPCKQT GWLHQLEAHP SKESIDAALG  240
VVLAQPWLPL PLGLKPPSLE NEARVKEFSL KAMWKSPNGT IRNILNGTVF REPILCKNVP  300
RLVPGWTKPI CIGRHAFGDQ YRATDLVIKG PGKLRLVFEG KEEQIDLEVF NFTGEGGVAL  360
SMYNTDESIR AFADSSMNTA YQKKWPLYLS TKNTILKKYD GRFKDIFQEV YESKWKSLFE  420
ESGIWYEHRL IDDMVAYAVK SEGGYVWACK NYDGDVQSDF LAQGFGSLGL MTSVLVCPDG  480
KTIEAEAAHG TVTRHYRVHQ KGGETSTNSI ASIFAWTRGL AHRAKLDDNA ELLAFTEKLE  540
AACVETVESG KMTKDLALII HGSKLSREQY LTTEEFIDAV AQGLKAKL

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5yzh_A	1e-164	252	588	69	409	Isocitrate dehydrogenase [NADP] cytoplasmic
5yzh_B	1e-164	252	588	69	409	Isocitrate dehydrogenase [NADP] cytoplasmic
5yzi_A	1e-164	252	588	69	409	Isocitrate dehydrogenase [NADP] cytoplasmic
5yzi_B	1e-164	252	588	69	409	Isocitrate dehydrogenase [NADP] cytoplasmic
Search in ModeBase

Functional Description ? help Back to Top
Source	Description
UniProt	May supply 2-oxoglutarate for amino acid biosynthesis and ammonia assimilation via the glutamine synthetase/glutamate synthase (GS/GOGAT) pathway. May be involved in the production of NADPH to promote redox signaling or homeostasis in response to oxidative stress. {ECO:0000269\|PubMed:20199623}.

Regulation -- PlantRegMap ? help Back to Top
Source	Upstream Regulator	Target Gene
PlantRegMap	Retrieve	-

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_020575133.1	0.0	cytosolic isocitrate dehydrogenase [NADP]
Refseq	XP_020672354.1	0.0	cytosolic isocitrate dehydrogenase [NADP]
Swissprot	Q9SRZ6	0.0	ICDHC_ARATH; Cytosolic isocitrate dehydrogenase [NADP]
TrEMBL	A0A2I0WM61	0.0	A0A2I0WM61_9ASPA; Isocitrate dehydrogenase [NADP]
STRING	GSMUA_Achr4P00910_001	0.0	(Musa acuminata)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT2G20570.1	3e-23	GBF's pro-rich region-interacting factor 1

Publications ? help Back to Top
Rajjou L, et al. The effect of alpha-amanitin on the Arabidopsis seed proteome highlights the distinct roles of stored and neosynthesized mRNAs during germination. Plant Physiol., 2004. 134(4): p. 1598-613 [PMID:15047896] 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] Reumann S,Ma C,Lemke S,Babujee L AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes. Plant Physiol., 2004. 136(1): p. 2587-608 [PMID:15333753] Marchand C, et al. New targets of Arabidopsis thioredoxins revealed by proteomic analysis. Proteomics, 2004. 4(9): p. 2696-706 [PMID:15352244] Job C,Rajjou L,Lovigny Y,Belghazi M,Job D Patterns of protein oxidation in Arabidopsis seeds and during germination. Plant Physiol., 2005. 138(2): p. 790-802 [PMID:15908592] Noir S,Bräutigam A,Colby T,Schmidt J,Panstruga R A reference map of the Arabidopsis thaliana mature pollen proteome. Biochem. Biophys. Res. Commun., 2005. 337(4): p. 1257-66 [PMID:16242667] Holmes-Davis R,Tanaka CK,Vensel WH,Hurkman WJ,McCormick S Proteome mapping of mature pollen of Arabidopsis thaliana. Proteomics, 2005. 5(18): p. 4864-84 [PMID:16247729] Kung CC,Huang WN,Huang YC,Yeh KC Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry. Proteomics, 2006. 6(9): p. 2746-58 [PMID:16526091] Chivasa S, et al. Proteomic analysis of differentially expressed proteins in fungal elicitor-treated Arabidopsis cell cultures. J. Exp. Bot., 2006. 57(7): p. 1553-62 [PMID:16547123] Rajjou L, et al. Proteomic investigation of the effect of salicylic acid on Arabidopsis seed germination and establishment of early defense mechanisms. Plant Physiol., 2006. 141(3): p. 910-23 [PMID:16679420] Gibon Y, et al. Integration of metabolite with transcript and enzyme activity profiling during diurnal cycles in Arabidopsis rosettes. Genome Biol., 2006. 7(8): p. R76 [PMID:16916443] Chibani K, et al. Proteomic analysis of seed dormancy in Arabidopsis. Plant Physiol., 2006. 142(4): p. 1493-510 [PMID:17028149] Marchand C,Le Maréchal P,Meyer Y,Decottignies P Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. Proteomics, 2006. 6(24): p. 6528-37 [PMID:17163439] Marmagne A, et al. A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome. Mol. Cell Proteomics, 2007. 6(11): p. 1980-96 [PMID:17644812] Espagne C,Martinez A,Valot B,Meinnel T,Giglione C Alternative and effective proteomic analysis in Arabidopsis. Proteomics, 2007. 7(20): p. 3788-99 [PMID:17828791] Jiang Y,Yang B,Harris NS,Deyholos MK Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. J. Exp. Bot., 2007. 58(13): p. 3591-607 [PMID:17916636] Casasoli M, et al. Identification by 2-D DIGE of apoplastic proteins regulated by oligogalacturonides in Arabidopsis thaliana. Proteomics, 2008. 8(5): p. 1042-54 [PMID:18324730] Bindschedler LV,Palmblad M,Cramer R Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. Phytochemistry, 2008. 69(10): p. 1962-72 [PMID:18538804] Garmier M, et al. Complex I dysfunction redirects cellular and mitochondrial metabolism in Arabidopsis. Plant Physiol., 2008. 148(3): p. 1324-41 [PMID:18784283] Aceituno FF,Moseyko N,Rhee SY,Gutiérrez RA The rules of gene expression in plants: organ identity and gene body methylation are key factors for regulation of gene expression in Arabidopsis thaliana. BMC Genomics, 2008. 9: p. 438 [PMID:18811951] Fukao Y,Ferjani A,Fujiwara M,Nishimori Y,Ohtsu I Identification of zinc-responsive proteins in the roots of Arabidopsis thaliana using a highly improved method of two-dimensional electrophoresis. Plant Cell Physiol., 2009. 50(12): p. 2234-9 [PMID:19880396] Hajduch M, et al. Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression. Plant Physiol., 2010. 152(4): p. 2078-87 [PMID:20118269] Mhamdi A, et al. Cytosolic NADP-dependent isocitrate dehydrogenase contributes to redox homeostasis and the regulation of pathogen responses in Arabidopsis leaves. Plant Cell Environ., 2010. 33(7): p. 1112-23 [PMID:20199623] Fares A,Rossignol M,Peltier JB Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem. Biophys. Res. Commun., 2011. 416(3-4): p. 331-6 [PMID:22115780] Boex-Fontvieille ER,Gauthier PP,Gilard F,Hodges M,Tcherkez GG A new anaplerotic respiratory pathway involving lysine biosynthesis in isocitrate dehydrogenase-deficient Arabidopsis mutants. New Phytol., 2013. 199(3): p. 673-82 [PMID:23718121]