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Q9HJM5 (SYE_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:Ta0942
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length548 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 CAC12071.1 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 – 548548Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119733

Regions

Motif102 – 11211"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q9HJM5 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 1736628A27C73D60

FASTA54863,450
        10         20         30         40         50         60 
MYEDDIRRIA LINAYQHEGK ADLKSVMGKV MAEIPDLRRD PRSAREMVSR IVDEVNSMSA 

        70         80         90        100        110        120 
YEIRETVETR YTSSIRKEKK VEEHRLPDLE GVNGPVVMRM APSPSGPLHI GHTRMAILND 

       130        140        150        160        170        180 
EYVKRYGGEL ILRIEDTNPK NIDPDAYHMI PEDLEWLGVN VTKIVIQSDR FDLYYAEAKK 

       190        200        210        220        230        240 
LMENGHMYVC TCPREEFKKR KLESIPCKDR DNPPETNLEL FDKMIDGTIK EGDAVAVVKT 

       250        260        270        280        290        300 
DLKHPNPSVR DWIAFRIIEA RHPRVDDKYR VYPMMSFSVA VDDHYLGLTH VLRGKDQLTN 

       310        320        330        340        350        360 
TDKQRYIFDY NGWKKPYYYH YGMIKFPGIK LKTSLMKKGI LSGQYEGWSD IRLGTVRAFA 

       370        380        390        400        410        420 
KRGYRPETFR RYWINSGLRE IDAIFSIEIF DSINREIVDP RAYRFSFVKD PVPVRIEGMP 

       430        440        450        460        470        480 
NISAKLPLHP THPEYGFREY EVKGSVYIAS RDFAAISEGE RIRLKDLCYI RKKGNGIIYD 

       490        500        510        520        530        540 
GVEMTEKTKI INWCPEGSRD FSVLKPDGSK DSGLIEPKSS GYRGIAQLER YGYVNFADGD 


DLAYFTHP 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445066 Genomic DNA. Translation: CAC12071.1. Different initiation.
RefSeqNP_394401.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HJM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12071; CAC12071; CAC12071.
GeneID1456475.
KEGGtac:Ta0942.

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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. 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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_THEAC
AccessionPrimary (citable) accession number: Q9HJM5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 30, 2003
Last modified: February 19, 2014
This is version 76 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