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Reviewed, UniProtKB/Swiss-Prot A9KBJ3 (SYE1_COXBN)

Last modified February 9, 2010. Version 21. 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: CBUD_0531
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length465 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 By similarity 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 – 465465Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367659

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022
Motif249 – 2535"KMSKS" region HAMAP MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KBJ3-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 393FE9F270B9F55B

FASTA46552,691
        10         20         30         40         50         60 
MMKSRFCPSP TGLMHLGNAR TALFNYLFAK SKDGIFLLRI EDTDVERSKE TFDLGLKEDL 

        70         80         90        100        110        120 
RWLNLEWQEG PGADEGNGPY HQSKRQAIYD DYYQRLEEAD QAYPCFCSEE QLRLSRKIQR 

       130        140        150        160        170        180 
SAGKPPRYAG TCRSLSAAEI EKKKAEGLQP ALRFRVPDDE VVVFADLVRG EQRFQTNDIG 

       190        200        210        220        230        240 
DFIIRRANGT SPFMFCNAID DALMGVSHVL RGEDHLTNTP RQLLILQALE LPVPTYAHIA 

       250        260        270        280        290        300 
LIVGPDGSPL SKRHGSRGIK ELRDNGYLPL ALTNYLARLG HYYASDELLS LAELAKGFNV 

       310        320        330        340        350        360 
ESLSKSPAKF NAQQLDYWQK QTVNQLPNDD FWEWAGSELQ SQIPTDKADL FLTTVKPNAS 

       370        380        390        400        410        420 
FPRDVAYWVN VCFGKTLNLE TAQSELLRAT GNRYFEEAFE AFKKFGKDLN SVVSHLKEKL 

       430        440        450        460 
NLKGKPLYQP LRIALTGAEH GPELAKLILI MDYETIQNRL QEACQ 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed: 19047403] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000733 Genomic DNA. Translation: ABS78423.1.
RefSeqYP_001423945.1.

3D structure databases

SMRA9KBJ3. Positions 1-464.
ModBaseSearch...

Genome annotation databases

GeneID5457444.
GenomeReviewsGene locus CBUD_0531 in contig CP000733_GR.
KEGGcbd:CBUD_0531.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMACNAIDDA.

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.
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.
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_COXBN
AccessionPrimary (citable) accession number: A9KBJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: February 9, 2010
This is version 21 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