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A8GN11 (SYE1_RICAH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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
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-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
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 – 447447Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367752

Regions

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

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8GN11 [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].
Strain: Hartford.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000847 Genomic DNA. Translation: ABV74786.1.
RefSeqYP_001493294.1. NC_009881.1.

3D structure databases

ProteinModelPortalA8GN11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293614.A1C_02435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV74786; ABV74786; A1C_02435.
GeneID5645148.
KEGGrak:A1C_02435.
PATRIC17875892. VBIRicAka50705_0497.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAAGRLYPC.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycRAKA293614:GI4A-459-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_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 19, 2014
This is version 44 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