Glutamate--tRNA ligase, chloroplastic/mitochondrial precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q9FEA2 (SYE_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase, chloroplastic/mitochondrial
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS

Gene names

Ordered Locus Names:	At5g64050
ORF Names:	MHJ24.3

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
Subcellular location	Plastid › chloroplast. Mitochondrion Potential Ref.5.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Chloroplast Mitochondrion Plastid
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chloroplast organization Traceable author statement PubMed 16107332. Source: TAIR glutamyl-tRNA aminoacylation Inferred from sequence or structural similarity PubMed 16297076. Source: TAIR mitochondrion organization Traceable author statement PubMed 16107332. Source: TAIR ovule development Inferred from mutant phenotype PubMed 16297076. Source: TAIR
Cellular_component	chloroplast stroma Inferred from direct assay PubMed 20061580. Source: TAIR mitochondrion Inferred from direct assay PubMed 16107332 PubMed 16251277. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Chloroplast and mitochondrion Potential

Chain

? – 570

Glutamate--tRNA ligase, chloroplastic/mitochondrial

PRO_0000119735

Regions

Nucleotide binding

301 – 305

ATP By similarity

Region

57 – 59

Glutamate binding By similarity

Region

245 – 249

Glutamate binding By similarity

Motif

60 – 70

"HIGH" region

Motif

301 – 305

"KMSKS" region

Sites

Binding site

ATP By similarity

Binding site

Glutamate By similarity

Binding site

263

Glutamate By similarity

Binding site

266

ATP By similarity

Experimental info

Sequence conflict

A → V in AAL06875. Ref.4

Sequence conflict

A → V in AAL32638. Ref.4

Sequence conflict

A → V in AAM47995. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FEA2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5EA70E3595F53587
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FASTA

570

63,466

        10         20         30         40         50         60 
MASLVYGTPW LRVRSLPELA PAFLRRRQSS LFYCSRRSFA VVACSTPVNN GGSVRVRFAP 

        70         80         90        100        110        120 
SPTGNLHVGG ARTALFNYLF ARSKGGKFVL RIEDTDLERS TRESEAAVLQ DLSWLGLDWD 

       130        140        150        160        170        180 
EGPGVSGDFG PYRQSERNAL YKQYAEKLLE SGHVYRCFCS SEELVKMKEN AKLKQLPPVY 

       190        200        210        220        230        240 
TGKWATASDA EIEQELEKGT PFTYRFRVPK EGSLKINDLI RGEVCWNLDT LGDFVVMRSN 

       250        260        270        280        290        300 
GQPVYNFCVT VDDATMAISH VIRAEEHLPN TLRQALIYKA LKFPMPQFAH VSLILAPDRS 

       310        320        330        340        350        360 
KLSKRHGATS VGQYREMGYL PQGMVNYLAL LGWGDGTENE FFTLEDLVEK FSIERVNKSG 

       370        380        390        400        410        420 
AIFDSTKLRW MNGQHLRALP NEKLTKLVGE RWKSAGILTE SEGSFVNEAV ELLKDGIELV 

       430        440        450        460        470        480 
TDSDKVLLNL LSYPLHATLA SPEAKPAVED KLHEVAASLI AAYDSGEIPS ALEEGQGAWQ 

       490        500        510        520        530        540 
KWVKAFGKSL KRKGKSLFMP LRVLLTGKLH GPEMGTSIVL IYKAGSPGIV VPQAGFVSME 

       550        560        570 
ERFKILREID WEALNKDESV PLESTATVST

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of Arabidopsis thaliana Glu-tRNA(Glu) synthetase mRNA." Chang W., Soell D. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones." Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF241841 mRNA. Translation: AAG29098.1. AB008266 Genomic DNA. Translation: BAB10273.1. CP002688 Genomic DNA. Translation: AED97834.1. AY054215 mRNA. Translation: AAL06875.1. AY062560 mRNA. Translation: AAL32638.1. AY114676 mRNA. Translation: AAM47995.1.
IPI	IPI00541346.
RefSeq	NP_201210.1. NM_125801.3.
UniGene	At.8457.
3D structure databases
ProteinModelPortal	Q9FEA2.
SMR	Q9FEA2. Positions 54-523.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FEA2. 1 interaction.
Proteomic databases
PaxDb	Q9FEA2.
PRIDE	Q9FEA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G64050.1; AT5G64050.1; AT5G64050.
GeneID	836526.
KEGG	ath:AT5G64050.
Organism-specific databases
GeneFarm	2420.
TAIR	At5g64050.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
InParanoid	Q9FEA2.
KO	K01885.
OMA	LYPCYET.
PhylomeDB	Q9FEA2.
ProtClustDB	PLN02627.
Gene expression databases
ArrayExpress	Q9FEA2.
Genevestigator	Q9FEA2.
GermOnline	AT5G64050. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-ligase_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_ARATH

Accession

Primary (citable) accession number: Q9FEA2
Secondary accession number(s): Q940P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents