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Reviewed, UniProtKB/Swiss-Prot A7H295 (SYE1_CAMJD)

Last modified November 3, 2009. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: JJD26997_0434
OrganismCampylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP]
Taxonomic identifier360109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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). HAMAP MF_00022

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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367638

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022
Motif240 – 2445"KMSKS" region HAMAP MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7H295-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 39847C75E3061C9B

FASTA46353,086
        10         20         30         40         50         60 
MHEKLTTRFA PSPTGYLHIG GLRTALYNYL YARKNGGNFL LRIEDTDLKR NSKEATKAII 

        70         80         90        100        110        120 
EAFKWCGLEH DGEVTYQSER FDLYKEYVKK LLDEGKAYYC YMSKEELEEL RAKQEAAKER 

       130        140        150        160        170        180 
PRYDGRYREF TGTPPQGIEP VVRIKAPQSG EIVFKDGVKG EVRFKAEDIM DDFIIARSDG 

       190        200        210        220        230        240 
TPTYNFTVVI DDALMGVSDV IRGDDHLSNT PKQIVLYEAL GFKIPQFFHV AMIHGEDGKK 

       250        260        270        280        290        300 
LSKRHGATDV MEYKEMGILP QALLNFLVRL GWSHGDDEVF SLEDLKKLFD PYHINKSASC 

       310        320        330        340        350        360 
YNAKKLEWLN THYIKTLPFE EIKRQLKDLG FDLSVYEKAG FLLDLLRERA KTLHDIINGA 

       370        380        390        400        410        420 
KSIVNAPQNY DENAVQKFVN ENNLELLQAF ANTLKDPKTG KDFEDFTNDF LEKKEAKLKD 

       430        440        450        460 
LAQPIRIALT GSAVSPSIFE VLEFLGVDEC KKRIENFLKV RGK 

« Hide

References

[1]"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000768 Genomic DNA. Translation: ABS43292.1.
RefSeqYP_001397625.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7H295.

Genome annotation databases

GeneID5389780.
GenomeReviewsGene locus JJD26997_0434 in contig CP000768_GR.
KEGGcjd:JJD26997_0434.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIEWFNLD.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_CAMJD
AccessionPrimary (citable) accession number: A7H295
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents