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Q9FEA2 (SYE_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. HAMAP-Rule MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022_B

Subcellular location

Plastidchloroplast. Mitochondrion Potential Ref.5.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast and mitochondrion Potential
Chain? – 570Glutamate--tRNA ligase, chloroplastic/mitochondrial HAMAP-Rule MF_00022_BPRO_0000119735

Regions

Nucleotide binding301 – 3055ATP By similarity
Region57 – 593Glutamate binding By similarity
Region245 – 2495Glutamate binding By similarity
Motif60 – 7011"HIGH" region HAMAP-Rule MF_00022_B
Motif301 – 3055"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site671ATP By similarity
Binding site931Glutamate By similarity
Binding site2631Glutamate By similarity
Binding site2661ATP By similarity

Experimental info

Sequence conflict741A → V in AAL06875. Ref.4
Sequence conflict741A → V in AAL32638. Ref.4
Sequence conflict741A → V in AAM47995. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9FEA2 [UniParc].

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

FASTA57063,466
        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' 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. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., 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].
+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.
RefSeqNP_201210.1. NM_125801.3.
UniGeneAt.8457.

3D structure databases

ProteinModelPortalQ9FEA2.
SMRQ9FEA2. Positions 54-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9FEA2. 1 interaction.

Proteomic databases

PaxDbQ9FEA2.
PRIDEQ9FEA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G64050.1; AT5G64050.1; AT5G64050.
GeneID836526.
KEGGath:AT5G64050.

Organism-specific databases

GeneFarm2420.
TAIRAT5G64050.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
InParanoidQ9FEA2.
KOK01885.
OMAKHYDGDF.
PhylomeDBQ9FEA2.

Enzyme and pathway databases

BioCycARA:AT5G64050-MONOMER.

Gene expression databases

GenevestigatorQ9FEA2.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_ARATH
AccessionPrimary (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: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries