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Q9PP78 (SYE1_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Synonyms:gltX2
Ordered Locus Names:Cj0845c
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [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-Rule MF_00022

Catalytic activity

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

Subunit structure

Monomer By similarity. 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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000119532

Regions

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

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PP78 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34973.1.
PIRE81357.
RefSeqYP_002344252.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PP78.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9PP78. 1 interaction.
STRING192222.Cj0845c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL34973; CAL34973; Cj0845c.
GeneID905144.
KEGGcje:Cj0845c.
PATRIC20058638. VBICamJej33762_0833.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAYCSKEFL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-819-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
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: May 14, 2014
This is version 81 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