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Reviewed, UniProtKB/Swiss-Prot A8GN11 (SYE1_RICAH)

Last modified February 9, 2010. Version 18. 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: A1C_02435
OrganismRickettsia akari (strain Hartford) [Complete proteome] [HAMAP]
Taxonomic identifier293614 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length447 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 – 447447Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367752

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022
Motif240 – 2445"KMSKS" region HAMAP MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8GN11-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: F765E80513E53AC9

FASTA44751,873
        10         20         30         40         50         60 
MTKVITRFAP SPTGMLHVGN IRVALLNWLY AKKHNGQFIL RFDDTDLERS KQEYKDAIKD 

        70         80         90        100        110        120 
DLKFLNLHWD QTFNQLSRLS RYDEIKNLLL DKKRLYACYE TPDELELKRK FQLSKGLPPM 

       130        140        150        160        170        180 
YDRASLNLTE EQTEKYIEQG RNPHYRFLVN HEPISWHDMI KGEIQYDGKA LSDPIVIRAD 

       190        200        210        220        230        240 
GSMTYMLCSV IDDIDYDITH IIRGEDHVSN TAIQIQMFEA LNNTPTTFGH LSLIINKDEK 

       250        260        270        280        290        300 
ISKRVGGFEI TTLRKEIGIE AMAIASFFSL LGSSAQILPY KSMEKLINQF EISSFSKSPT 

       310        320        330        340        350        360 
IYQPKDLERL NHKLLISLDF DEVKDHLKEI DAEYIDENFW LSIRPNLQKL RDVKDWWEIC 

       370        380        390        400        410        420 
HHTPNVESLN LDQEYLKQAA ELLPQGAITK DSWSIWTKEI TNITGRKGKE LFLPLRLALT 

       430        440 
GRESGPEIAD VLPLISREEI VKRLTSA 

« Hide

References

[1]"Complete genome sequence of Rickettsia akari."
Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Dasch G., Eremeeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000847 Genomic DNA. Translation: ABV74786.1.
RefSeqYP_001493294.1.

3D structure databases

SMRA8GN11. Positions 3-447.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8GN11.

Genome annotation databases

GeneID5645148.
GenomeReviewsGene locus A1C_02435 in contig CP000847_GR.
KEGGrak:A1C_02435.
NMPDRfig|293614.3.peg.452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMALRLDDTD.

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_RICAH
AccessionPrimary (citable) accession number: A8GN11
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: February 9, 2010
This is version 18 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