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Reviewed, UniProtKB/Swiss-Prot Q5FGB6 (SYE1_EHRRG)

Last modified February 9, 2010. Version 36. 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: ERGA_CDS_07930
OrganismEhrlichia ruminantium (strain Gardel) [Complete proteome] [HAMAP]
Taxonomic identifier302409 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length445 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 – 445445Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000119558

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022
Motif238 – 2425"KMSKS" region HAMAP MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FGB6-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: EA69015D12BC3557

FASTA44551,819
        10         20         30         40         50         60 
MIMMTRFAPS PTGYLHVGNV RTALICWLYT RSKQGRFLLR FDDTDLQRSK DDYRNEIAND 

        70         80         90        100        110        120 
LKWLQMDWDF DVRQSSRFDR YDEIFNYLLK EELIYPCYES KEELDFKRKM QLKLGLPPIY 

       130        140        150        160        170        180 
DRSALKLTQD EKNKYSEQDV YFRFKIDQSQ LISWDDEIRG KVSFNAANIS DPIVKRADGT 

       190        200        210        220        230        240 
YTYMLPSVID DIDFDITHIV RGEDHISNTA IQIQMFNALR ASVPTFSHLS LLYCDDNKIS 

       250        260        270        280        290        300 
KRVGGFSIKD MQFYELEPMA INSYFAKIGT SDPIVVHTKI QDLIYNFDIT KFNQAPTQFN 

       310        320        330        340        350        360 
IDDVIKLNPK VLHKMSFSDV KHRLSELNIT SPDLWDFVSG NVQKFSDIQE WIKICGQSTV 

       370        380        390        400        410        420 
PVINESDQDF IKMALSVFPN GEINQDTWKT WVANIKEKTD RKSKDIFIPL RLALTGISTG 

       430        440 
PELAKLLPIL GRAEIIRRLG YSSRC 

« Hide

References

[1]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed: 16547041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR925677 Genomic DNA. Translation: CAI28245.1.
RefSeqYP_196719.1.

3D structure databases

SMRQ5FGB6. Positions 3-440.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5FGB6.

Genome annotation databases

GeneID3268758.
GenomeReviewsGene locus ERGA_CDS_07930 in contig CR925677_GR.
KEGGerg:ERGA_CDS_07930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMALRLDDTD.

Enzyme and pathway databases

BioCycERUM302409:ERGA_CDS_07930-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
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:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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_EHRRG
AccessionPrimary (citable) accession number: Q5FGB6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2005
Last modified: February 9, 2010
This is version 36 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