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Q9Y9H1 (SYE_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:APE_2317.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119712

Regions

Motif109 – 11911"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q9Y9H1 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 8C86B100C8F01176

FASTA57466,034
        10         20         30         40         50         60 
MGSEDLERLL LGYALRDAVK HGGRASVGSV MSMLLGDHPE LRSRAREIAS LAARVVEQVN 

        70         80         90        100        110        120 
SMPAGEQKRL LSEQYPELAR FEEQREKGDK GLPPLPGAVE GRVKLRFAPN PDFVIHMGNA 

       130        140        150        160        170        180 
RPAIVNHEYA RMYKGRMVLR FEDTDPRTKT PLREAYDLIR QDLKWLGVSW DEEYIQSLRM 

       190        200        210        220        230        240 
EVFYSVARRA IERGCAYVDN CGREGKELLS RGEYCPTRDL GPEDNLELFE KMLEGEFYEG 

       250        260        270        280        290        300 
EAVVRMKTDP RHPNPSLRDW VAMRIIDTEK HPHPLVGSRY LVWPTYNFAV SVDDHMMEIT 

       310        320        330        340        350        360 
HVLRGKEHQL NTEKQLAVYR CMGWRPPYFI HFGRLKLEGF ILSKSKIRKL LEERPGEFMG 

       370        380        390        400        410        420 
YDDPRFGTIA GLRRRGVLAE AIRQIILEVG VKPTDATISW ANLAAANRKL LDERADRIMY 

       430        440        450        460        470        480 
VEDPVEMEVE LAQVECRAAE IPFHPSRPQR KRRITLCTGD KVLLTREDAV EGRQLRLMGL 

       490        500        510        520        530        540 
SNFTVSQGIL REVDPSLEYA RRMKLPIVQW VKKGGEASVE VLEPVELELR RHQGYAEDAI 

       550        560        570 
RGYGVDSRLQ FVRYGFVRVD SVEDGVYRVI YTHK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA81329.2.
PIRA72459.
RefSeqNP_148534.2. NC_000854.2.

3D structure databases

ProteinModelPortalQ9Y9H1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_2317.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA81329; BAA81329; APE_2317.1.
GeneID1445342.
KEGGape:APE_2317.1.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAAFRIIDT.

Enzyme and pathway databases

BioCycAPER272557:GJD6-1563-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYE_AERPE
AccessionPrimary (citable) accession number: Q9Y9H1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 30, 2003
Last modified: May 14, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries