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A0RY20 (SYE_CENSY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:CENSYa_1618
OrganismCenarchaeum symbiosum (strain A) [Reference proteome] [HAMAP]
Taxonomic identifier414004 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaCenarchaealesCenarchaeaceaeCenarchaeum

Protein attributes

Sequence length562 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 – 562562Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367799

Regions

Motif101 – 11111"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A0RY20 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 8DF90221F9D20FFC

FASTA56262,086
        10         20         30         40         50         60 
MSDIAGEARK IALQNAVSHG GRAREGAVLA GLLGARPELR PKAGELMEEI SDIVAGINAM 

        70         80         90        100        110        120 
PESKQREELG DVPVERKKQE GQALPPLEGA IKGRVVTRFP PEPNGYPHIG HAKAAIINEE 

       130        140        150        160        170        180 
YVTMYGGIKI LRMDDTNPGA ERMEYYAAIK VGLDWLGIEY DVIKNTSDDM DLLLSKGREL 

       190        200        210        220        230        240 
LESGDAYVCT CKRDDMSKNR RAMAPCKCSK KAQEDHMEGW DKMHGKFKPG QAVARFRGDM 

       250        260        270        280        290        300 
ESQNTVMRDP VLFRIMEERH PLLGDRHRVW PSYDMAVAIE DSIDGVTHAF RSKEYELRNE 

       310        320        330        340        350        360 
LYGAILGKLD MRAPMVLEFS RLEFEGMPVS KRVIRPLIED GKIPWYDDPR LPTLEGMKKR 

       370        380        390        400        410        420 
GITPGAIRRF VISLGLTKAD TLAPFGALEA FNRKEIDGNS TRLFLVGDPR RIDVAGLPGT 

       430        440        450        460        470        480 
AELPNHPSGD MGSRKIETGG ALYLPGKDAE GLSEGGHIRL MGLGDVRIDS AGRDLAGTYT 

       490        500        510        520        530        540 
GDDISAGYPK MQWVPCGDAR KIKVVIPRAP IKDGEFDSSS LGILEGMVEP HYLQVGDGQS 

       550        560 
IQFVRFGYCR KESQHMAVFT HG 

« Hide

References

[1]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DP000238 Genomic DNA. Translation: ABK78237.1.
RefSeqYP_876541.1. NC_014820.1.

3D structure databases

ProteinModelPortalA0RY20.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK78237; ABK78237; CENSYa_1618.
GeneID6371798.
KEGGcsy:CENSYa_1618.

Phylogenomic databases

HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.

Family and domain databases

Gene3D1.10.1160.10. 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.
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_CENSY
AccessionPrimary (citable) accession number: A0RY20
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 45 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