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A1RYD7 (SYE_THEPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Tpen_0816
OrganismThermofilum pendens (strain Hrk 5) [Reference proteome] [HAMAP]
Taxonomic identifier368408 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum

Protein attributes

Sequence length569 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
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 – 569569Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001982

Regions

Motif108 – 11811"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A1RYD7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: BCA13B7C3A20DCB9

FASTA56964,322
        10         20         30         40         50         60 
MEVDIRRVAL KHALANAVKF GGKARVDSVV SKVFAEVPEA RKAAKEVVEL VKEVVEEVNS 

        70         80         90        100        110        120 
MSPESQASLL SELWPEALSG ERKVEVKRLP PLPGAEEVGG KVVTRFAPNP DFVLHLGSAR 

       130        140        150        160        170        180 
PAILNYYYAK KMYNGKFILR FEDTDPRTKR PMPEAYDLIR EDLRWLGTPW DEEYIQSQRM 

       190        200        210        220        230        240 
EVYYEVAEAL IKSGNAYVCT HSQDEIKAFR DAGKPDPCSF LPPEEHMERW EKMLSGEYPE 

       250        260        270        280        290        300 
GAAVLRIKTD PAHPNPSVRD WIAFRVLDTE KTPHPLTGDK YRVWPTYNFA CAVDDHMLGV 

       310        320        330        340        350        360 
THVLRGEEHA VNTLKQEYVY RHMGWKPPVS IHFGRMNLEG MVLSKSVIRR GIEKGLFSSI 

       370        380        390        400        410        420 
DDIRLGTLRA LRRRGILPEA IWDLVLEVGI KPSTARVSVD KLHAFNRKYL EPRANRYMFV 

       430        440        450        460        470        480 
PEPAKVASIE GLEAPITAEV IVHPSFPERG RRRITFSKPE VYLPSDVASS MVRLMGLGNF 

       490        500        510        520        530        540 
EVVDGGSKLR YLNNDVSFAK KHELPIVQWA PVESSVRGRV LKAAGTKIEE ISGYGEPSLA 

       550        560 
ELPPGEQVQF VRLGFVRVEG PETYIFTHD 

« Hide

References

[1]"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction."
Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. expand/collapse author list , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.
J. Bacteriol. 190:2957-2965(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hrk 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000505 Genomic DNA. Translation: ABL78217.1.
RefSeqYP_920220.1. NC_008698.1.

3D structure databases

ProteinModelPortalA1RYD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368408.Tpen_0816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL78217; ABL78217; Tpen_0816.
GeneID4601986.
KEGGtpe:Tpen_0816.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAAFRIIDT.

Enzyme and pathway databases

BioCycTPEN368408:GHSG-866-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_THEPD
AccessionPrimary (citable) accession number: A1RYD7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 50 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