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Q9V1E3 (SYE_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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:PYRAB04840
ORF Names:PAB0323
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length571 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 – 571571Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119725

Regions

Motif106 – 11611"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q9V1E3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D7BA5D954B1A8AC6

FASTA57165,920
        10         20         30         40         50         60 
MEVERIALKY ALINAIEHGG KANPKAVIGK VLGENPELRS KAREIVPIIN KVVEEVNSLS 

        70         80         90        100        110        120 
LDEQKAKLME IYPEYFEKKE EKKEEKKGLP PLPKAEKGKV VTRFAPNPDG AFHLGNARAA 

       130        140        150        160        170        180 
ILSYEYAKMY GGKFILRFDD TDPKVKRPEP IFYEMIIEDL EWLGIKPDEI VYASDRLELY 

       190        200        210        220        230        240 
YKYAEELIKM GKAYVCTCKP EKFRELRDKG IPCPHRDEPV EVQLERWRKM LNGEYKEGEA 

       250        260        270        280        290        300 
VVRIKTDLNH PNPAVRDWPA LRIVDNPNHP RAGNKYRVWP LYNFASAIDD HELGVTHIFR 

       310        320        330        340        350        360 
GQEHAENETR QRYIYEYFGW EYPVTVHHGR LSIEGVILSK SKTRKGIEEG KYLGWDDPRL 

       370        380        390        400        410        420 
GTIRALRRRG ILPEAIKELI IEVGLKKSDA TVSWDNLAAI NRKLVDPIAN RYFFVADPVP 

       430        440        450        460        470        480 
MEVEGAPEFI AKIPLHPDHP ERGTRELRFT PGKPIYVSKD DLDLLKPGSF VRLKDLFNVE 

       490        500        510        520        530        540 
IVEVGEKIKA KFHSFEYEIA RKNKWRMIHW VPEGRPCEVI IPEGDELIVR KGLLEKDANV 

       550        560        570 
KAGEIVQFER FGFVRIDKIE GEKVVAIYAH K 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49406.1.
HE613800 Genomic DNA. Translation: CCE69868.1.
PIRG75165.
RefSeqNP_126175.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V1E3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB0323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49406; CAB49406; PAB0323.
GeneID1495381.
KEGGpab:PAB0323.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 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.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
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_PYRAB
AccessionPrimary (citable) accession number: Q9V1E3
Secondary accession number(s): G8ZGI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 88 of the entry and version 1 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