Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8U064 (SYE_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:PF1753
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length572 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.

Sequence caution

The sequence AAL81877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 572572Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119727

Regions

Motif107 – 11711"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q8U064 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 5057509BC4F69FC6

FASTA57266,563
        10         20         30         40         50         60 
MEVEKLALKY ALINAIEHDG KANPKAVIGK ILGENPELRK KAREIVPIVN KIVEEVNTLS 

        70         80         90        100        110        120 
LEEQKKKLEE IYPEYFMEGT KKEKEEKKQL PPLPKAEKGK VVTRFAPNPD GAFHLGNARA 

       130        140        150        160        170        180 
AILSYEYAKM YDGKFILRFD DTDPKVKRPE LIFYDMIIED LEWLGIKPDE IVYASDRLEI 

       190        200        210        220        230        240 
YYKYAEELIK MGKAYVCTCP PDEFRKLRDQ GIACPHRDEP VEVQLERWKK MLNGEYREGE 

       250        260        270        280        290        300 
AVVRIKTDLN HPNPAVRDWP ALRIVDEPNH PRTGNKYRVW PLYNFASAID DHELGVTHIF 

       310        320        330        340        350        360 
RGQEHSENET RQRYIYEYFG WEYPVTVHHG RLSIEGVILS KSKTRKGIEE GKYLGWDDPR 

       370        380        390        400        410        420 
LGTIRALRRR GILPEAIREL ILEVGLKKSD ATVSWDNLAA INRKLVDPIA NRYFFVADPI 

       430        440        450        460        470        480 
PMYIEEAEEF EAKIPLHPDH PERGYRVLKF EPGKPIYVSK DDLSLLKPGG FIRLKDLFNV 

       490        500        510        520        530        540 
EILEVGDTIK ARFHSHEYEV ARKNKWRMIH WVPEGKECEV IIPEGEELII RKGLLEKNAN 

       550        560        570 
VKEGEIVQFE RFGFVRIDKI ENDKVIAIYA HK 

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81877.1. Different initiation.
RefSeqNP_579482.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U064.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1753.

Proteomic databases

PRIDEQ8U064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81877; AAL81877; PF1753.
GeneID1469631.
KEGGpfu:PF1753.

Phylogenomic databases

eggNOGCOG0008.
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_PYRFU
AccessionPrimary (citable) accession number: Q8U064
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: February 19, 2014
This is version 70 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