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Reviewed, UniProtKB/Swiss-Prot Q9PP78 (SYE1_CAMJE)

Last modified February 9, 2010. Version 56. 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
Synonyms: gltX2
Ordered Locus Names: Cj0845c
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length431 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 MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity. HAMAP MF_00022

Subcellular location

Cytoplasm HAMAP 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: 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 – 431431Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000119532

Regions

Motif6 – 1611"HIGH" region HAMAP MF_00022
Motif235 – 2395"KMSKS" region HAMAP MF_00022

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PP78-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 480A5720D24F4509

FASTA43150,191
        10         20         30         40         50         60 
MYRFAPSPTG DMHIGNLRAA IFNYICARQK NMDFILRIED TDKARNIAGK EEEIKEILNL 

        70         80         90        100        110        120 
FSISWQHYYI QSENLKFHRQ MALKLVSEKK AFACFCTEEE LEAKKELAKK QGKAYRYDGT 

       130        140        150        160        170        180 
CEKLADIDVL ECEKPFVIRL KKPTHTMKFT DFIKGELSFE PENIDSFVIM RTDKTPTYNF 

       190        200        210        220        230        240 
ACAVDDMLEN VTCIIRGEDH VSNTPKQEHI RASLGYNKAM TYAHLPIILN EEGVKMSKRE 

       250        260        270        280        290        300 
AHSSVKWLLE SGILPSAIAN YLIMLGNKTP CEIFTLEEAI KWFDISKVSK APARFDLKKL 

       310        320        330        340        350        360 
LQINREHIKM IKDDELNKIL DLNKDLAQLA KFYTQETSTI KELKEKMQAI FNAKDFGEFE 

       370        380        390        400        410        420 
TEYKILKELL KDIELFENYE DFKNELLNKS NLKGKKFFMP LRIILTGNIH GPELSDLYPY 

       430 
IKNFIHELAR I 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34973.1.
PIRE81357.
RefSeqYP_002344252.1.

3D structure databases

SMRQ9PP78. Positions 2-421.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PP78. 1 interaction.

Genome annotation databases

GeneID905144.
GenomeReviewsGene locus Cj0845c in contig AL111168_GR.
KEGGcje:Cj0845c.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMARYDGTCE.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0845C-MONOMER.
BRENDA6.1.1.17. 255835.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[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. 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_CAMJE
AccessionPrimary (citable) accession number: Q9PP78
Secondary accession number(s): Q0PA45
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 56 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