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P77984 (SYE_STAXY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. 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
OrganismStaphylococcus xylosus
Taxonomic identifier1288 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length120 AA.
Sequence statusFragment.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 120›120Glutamate--tRNA ligase
PRO_0000119659

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P77984 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 6A2CE7FC1332C763

FASTA12013,698
        10         20         30         40         50         60 
KLVALYQKEM SYAGEIVPLS ELFFRDEQIL GDDEQEVING EQVPELMNHL YGKLEVLEPF 

        70         80         90        100        110        120 
EAAEIKKTIK EVQKETGIKG KQLFMPIRVA VTGQMHGPEL PNTIEVLGRE KVLSRLKKYV 

« Hide

References

[1]"Identification of the serine acetyltransferase gene of Staphylococcus xylosus."
Fiegler H., Brueckner R.
FEMS Microbiol. Lett. 148:181-187(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 20267 / Isolate C2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07614 Genomic DNA. Translation: CAA68886.1.

3D structure databases

ProteinModelPortalP77984.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.350. 1 hit.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
[Graphical view]
SUPFAMSSF48163. SSF48163. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYE_STAXY
AccessionPrimary (citable) accession number: P77984
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: June 11, 2014
This is version 75 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