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B1YAX4 (SYE_PYRNV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Tneu_1756
OrganismPyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus) [Complete proteome] [HAMAP]
Taxonomic identifier444157 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length570 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 – 570570Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090116

Regions

Motif107 – 11711"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
B1YAX4 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: A8CEDDCB043E24C2

FASTA57065,052
        10         20         30         40         50         60 
MNIEDVVLKY ALANAVKYGG RADVKAVMAK IMAEVPDLRP RAREVRQLVE AVVAKVNSMQ 

        70         80         90        100        110        120 
PEEQLRLLRE RWPEALEERR VEQRRPGIES LPELPNVRGG VVVRFAPNPD FVLHLGSARP 

       130        140        150        160        170        180 
AILNYAYRMR YGGRFILRFE DTDPRTKRPL VSDEVNAYEA IREDLRWLGV RWDEEHIQSR 

       190        200        210        220        230        240 
RMEIYYDHAR MLLSMGAAYV DLCRPEEWRR LRNAGRACPH RGQSPEEALE LWDRMLRGDF 

       250        260        270        280        290        300 
GEGEAVVRIK TDLSHPDPSV RDWVAFRVID TSKTPHPLTG DRYVVWPTYN FAVSIDDHLM 

       310        320        330        340        350        360 
GVTHVLRAQE HSVNTVKQSY VFKHFGWEQP VTIHFGRLRI EGASLSKSKL KALRVRYDDV 

       370        380        390        400        410        420 
SLPTLAGLRS RGILPEAIWE LILTVGIKPS DTTVALSNLF ALNRKRVEPA ANRYMFVTEP 

       430        440        450        460        470        480 
VKLVFESDRE LVAKIPLHPS YRERGERVYK LGPGRVEVYV SSRDVRPGAV VRLMELANVE 

       490        500        510        520        530        540 
VLEVGGGAAR GRLHSLELEA ARRVGAPIVQ WVADPVEVRV VKPVAVGKKV EEVGLGERAL 

       550        560        570 
EAVEEGAYLQ FFRYGFVKKV GRLDFVYVHD 

« Hide

References

[1]"Complete sequence of Thermoproteus neutrophilus V24Sta."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2338 / JCM 9278 / V24Sta.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001014 Genomic DNA. Translation: ACB40674.1.
RefSeqYP_001795120.1. NC_010525.1.

3D structure databases

ProteinModelPortalB1YAX4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444157.Tneu_1756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB40674; ACB40674; Tneu_1756.
GeneID6165414.
KEGGtne:Tneu_1756.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAAFRIIDT.

Enzyme and pathway databases

BioCycTNEU444157:GHL2-1801-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_PYRNV
AccessionPrimary (citable) accession number: B1YAX4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 40 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