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

Araha.7890s0002.1.p

Organism

Arabidopsis halleri

Taxonomic ID

81970

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis

Family

GeBP

Protein Properties

Length: 1007aa MW: 115229 Da PI: 5.5175

Description

GeBP family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Araha.7890s0002.1.p	genome	JGI	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	DUF573	99.5	3.1e-31	267	358	2	98
DUF573 2 lfqrlwseeDeivlLqGlidfkaktgkspsddidafyefvkksisfkvsk.sqlveKirrLKkKfkkkvkkaksgkepsfskehdqkife 90 +fqrlwseeDei+lL G+idf+ +tg+s++dd+++f+e+ k+s+sf+v++ sq+++Ki +LK+K+ k++ + +++hdq+++e Araha.7890s0002.1.p 267 RFQRLWSEEDEILLLEGMIDFNRDTGTSVYDDMNGFFEKYKDSLSFDVKSvSQFTKKIWSLKNKYIVKRRS------LVSTNDHDQNCLE 350 79*******************************************96539**********99999......999****** PP DUF573 91 lskkiWgs 98 l+kkiWgs Araha.7890s0002.1.p 351 LAKKIWGS 358 ****95 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Pfam	PF04504	3.7E-24	268	357	IPR007592	Protein of unknown function DUF573
SuperFamily	SSF53756	7.53E-195	381	716	No hit	No description
Gene3D	G3DSA:3.40.50.2000	8.8E-64	383	549	No hit	No description
Pfam	PF00343	3.2E-32	475	550	IPR000811	Glycosyl transferase, family 35
Gene3D	G3DSA:3.40.50.2000	2.7E-107	551	716	No hit	No description
Pfam	PF00343	6.2E-165	552	1005	IPR000811	Glycosyl transferase, family 35
Gene3D	G3DSA:3.40.50.2000	2.7E-107	768	831	No hit	No description
SuperFamily	SSF53756	7.53E-195	768	1005	No hit	No description
Gene3D	G3DSA:3.40.50.2000	4.6E-68	832	1005	No hit	No description

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0005975	Biological Process	carbohydrate metabolic process
GO:0008184	Molecular Function	glycogen phosphorylase activity

Sequence ? help Back to Top
Protein Sequence Length: 1007 aa Download sequence Send to blast
MALRFLLMGF ERNRLLASSF GITQGSLPMS GLSINAVVRD TIRGNDWWIA PSRSRNSIIL 60 LLKNTLPDAV NIIDCQHDDS YLWKIDQHVP SNKFSTAATW HSLHPPTITV PWHRAIWFKD 120 RIHKHAFIAS VYFIWKERNL RIHTGLERPS SLIINEIKLI IRARLDLLSR EQQIPMTKKR 180 QIEEDPSTEV EVKRAKTENK PIFQRIKDFV PKFVSFISEI YLSTDEEDEV EEEEEEEDLV 240 SESQTHSQTE PAATKTTPLA AMAKYPRFQR LWSEEDEILL LEGMIDFNRD TGTSVYDDMN 300 GFFEKYKDSL SFDVKSVSQF TKKIWSLKNK YIVKRRSLVS TNDHDQNCLE LAKKIWGSGV 360 DATLKVDGVK VECEEVFSLM SPFAPDAASV ASSIKSHAEF TPLFSPEKFE LPKAFFATAQ 420 SVRDALIMNW NATYEYYNRV NVKQAYYLSM EFLQGRALSN AVGNLGLNGA YADALKRLGF 480 DLESVASQEP DPALGNGGLG RLASCFLDSM ATLNYPAWGY GLRYKYGLFK QRITKDGQEE 540 AAEDWLEAAE ALFNAEKICF VLYPGDESLE GKALRLKQQY TLCSASLQDI IARFETRSGG 600 NVNWEEFPEK VAVQMNDTHP TLCIPELMRI LMDLKELSWE DAWKITQRTV AYTNHTVLRE 660 ALEKWSLELL EKLLPRHVEI IEKIDEELVR TIVSECGTAD PDLLEEKLKA MRILENVELP 720 SAFADVILKP ENKPVTAKDA QNGVKTEQEE EKIAGEEEEE EVIPEPIKPP KMVRMANLAV 780 VGGHAVNGVA EIHSEIVKQD VFNDFVQLWP EKFQNKTNGV TPRRWIRFCN PYLSDIITNW 840 IGTEDWVLNT EKLAELRKFA DNEDLQSEWR AAKKKNKLKV VALIKERTWY TVSPDAMFDI 900 QIKRIHEYKR QLLNILGIVY RYKKMKEMSA CEREKAYVPR VCIFGGKAFA TYVQAKRIVK 960 FITDVASTIN HDPEIGDMLK VIFVPDYNVS VAELLIPASE LSQHIR*

Sequence ? help Back to Top

Protein Sequence Length: 1007 aa Download sequence Send to blast

MALRFLLMGF ERNRLLASSF GITQGSLPMS GLSINAVVRD TIRGNDWWIA PSRSRNSIIL  60
LLKNTLPDAV NIIDCQHDDS YLWKIDQHVP SNKFSTAATW HSLHPPTITV PWHRAIWFKD  120
RIHKHAFIAS VYFIWKERNL RIHTGLERPS SLIINEIKLI IRARLDLLSR EQQIPMTKKR  180
QIEEDPSTEV EVKRAKTENK PIFQRIKDFV PKFVSFISEI YLSTDEEDEV EEEEEEEDLV  240
SESQTHSQTE PAATKTTPLA AMAKYPRFQR LWSEEDEILL LEGMIDFNRD TGTSVYDDMN  300
GFFEKYKDSL SFDVKSVSQF TKKIWSLKNK YIVKRRSLVS TNDHDQNCLE LAKKIWGSGV  360
DATLKVDGVK VECEEVFSLM SPFAPDAASV ASSIKSHAEF TPLFSPEKFE LPKAFFATAQ  420
SVRDALIMNW NATYEYYNRV NVKQAYYLSM EFLQGRALSN AVGNLGLNGA YADALKRLGF  480
DLESVASQEP DPALGNGGLG RLASCFLDSM ATLNYPAWGY GLRYKYGLFK QRITKDGQEE  540
AAEDWLEAAE ALFNAEKICF VLYPGDESLE GKALRLKQQY TLCSASLQDI IARFETRSGG  600
NVNWEEFPEK VAVQMNDTHP TLCIPELMRI LMDLKELSWE DAWKITQRTV AYTNHTVLRE  660
ALEKWSLELL EKLLPRHVEI IEKIDEELVR TIVSECGTAD PDLLEEKLKA MRILENVELP  720
SAFADVILKP ENKPVTAKDA QNGVKTEQEE EKIAGEEEEE EVIPEPIKPP KMVRMANLAV  780
VGGHAVNGVA EIHSEIVKQD VFNDFVQLWP EKFQNKTNGV TPRRWIRFCN PYLSDIITNW  840
IGTEDWVLNT EKLAELRKFA DNEDLQSEWR AAKKKNKLKV VALIKERTWY TVSPDAMFDI  900
QIKRIHEYKR QLLNILGIVY RYKKMKEMSA CEREKAYVPR VCIFGGKAFA TYVQAKRIVK  960
FITDVASTIN HDPEIGDMLK VIFVPDYNVS VAELLIPASE LSQHIR*

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5lr8_A	0.0	386	1005	28	758	Alpha-1,4 glucan phosphorylase
5lr8_B	0.0	386	1005	28	758	Alpha-1,4 glucan phosphorylase
5lra_A	0.0	386	1005	28	758	Alpha-1,4 glucan phosphorylase
5lra_B	0.0	386	1005	28	758	Alpha-1,4 glucan phosphorylase
5lrb_A	0.0	386	1005	28	758	Alpha-1,4 glucan phosphorylase
5lrb_B	0.0	386	1005	28	758	Alpha-1,4 glucan phosphorylase
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Functional Description ? help Back to Top
Source	Description
UniProt	Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). May be not required for the degradation of starch, but the phosphorolysis of starch may play an important role in water stress tolerance. {ECO:0000250, ECO:0000269\|PubMed:15173560}.

Cis-element ? help Back to Top
Source	Link
PlantRegMap	Araha.7890s0002.1.p

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

Annotation -- Nucleotide ? help Back to Top
Source	Hit ID	E-value	Description
GenBank	AY049235	0.0	AY049235.1 Arabidopsis thaliana AT3g29320/MUO10_2 mRNA, complete cds.
GenBank	KJ138807	0.0	KJ138807.1 Arabidopsis thaliana glycosyltransferase (AT3G29320) mRNA, partial cds.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_028082799.1	0.0	alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic-like isoform X2
Swissprot	Q9LIB2	0.0	PHS1_ARATH; Alpha-glucan phosphorylase 1
TrEMBL	A0A2P5SDD2	0.0	A0A2P5SDD2_GOSBA; Alpha-1,4 glucan phosphorylase
STRING	AT3G29320.1	0.0	(Arabidopsis thaliana)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT4G00610.1	2e-28	DNA-binding storekeeper protein-related transcriptional regulator

Link Out ? help Back to Top
Phytozome	Araha.7890s0002.1.p

Publications ? help Back to Top
Rook F,Bevan MW Genetic approaches to understanding sugar-response pathways. J. Exp. Bot., 2003. 54(382): p. 495-501 [PMID:12508060] 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] Zeeman SC, et al. Plastidial alpha-glucan phosphorylase is not required for starch degradation in Arabidopsis leaves but has a role in the tolerance of abiotic stress. Plant Physiol., 2004. 135(2): p. 849-58 [PMID:15173560] Smith AM,Zeeman SC,Smith SM Starch degradation. Annu Rev Plant Biol, 2005. 56: p. 73-98 [PMID:15862090] Delvallé D, et al. Soluble starch synthase I: a major determinant for the synthesis of amylopectin in Arabidopsis thaliana leaves. Plant J., 2005. 43(3): p. 398-412 [PMID:16045475] Fettke J,Eckermann N,Tiessen A,Geigenberger P,Steup M Identification, subcellular localization and biochemical characterization of water-soluble heteroglycans (SHG) in leaves of Arabidopsis thaliana L.: distinct SHG reside in the cytosol and in the apoplast. Plant J., 2005. 43(4): p. 568-85 [PMID:16098110] Peltier JB, et al. The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts. Mol. Cell Proteomics, 2006. 5(1): p. 114-33 [PMID:16207701] Lundmark M,Cavaco AM,Trevanion S,Hurry V Carbon partitioning and export in transgenic Arabidopsis thaliana with altered capacity for sucrose synthesis grown at low temperature: a role for metabolite transporters. Plant Cell Environ., 2006. 29(9): p. 1703-14 [PMID:16913860] Roldán I, et al. The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggests a novel function of elongation enzymes in the control of starch granule formation. Plant J., 2007. 49(3): p. 492-504 [PMID:17217470] 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] 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] Ma J, et al. Structure and expression of barley starch phosphorylase genes. Planta, 2013. 238(6): p. 1081-93 [PMID:24002549] Malinova I, et al. Double knockout mutants of Arabidopsis grown under normal conditions reveal that the plastidial phosphorylase isozyme participates in transitory starch metabolism. Plant Physiol., 2014. 164(2): p. 907-21 [PMID:24302650] Schwarte S, et al. Sequence variation, differential expression, and divergent evolution in starch-related genes among accessions of Arabidopsis thaliana. Plant Mol. Biol., 2015. 87(4-5): p. 489-519 [PMID:25663508] Malinova I, et al. Starch Synthase 4 and Plastidal Phosphorylase Differentially Affect Starch Granule Number and Morphology. Plant Physiol., 2017. 174(1): p. 73-85 [PMID:28275148] Malinova I,Fettke J Reduced starch granule number per chloroplast in the dpe2/phs1 mutant is dependent on initiation of starch degradation. PLoS ONE, 2017. 12(11): p. e0187985 [PMID:29155859]