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A8EY39 (SYE1_RICCK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:A1E_01635
OrganismRickettsia canadensis (strain McKiel) [Complete proteome] [HAMAP]
Taxonomic identifier293613 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length463 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 – 463463Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367756

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8EY39 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 345DB7B2127C606C

FASTA46352,518
        10         20         30         40         50         60 
MTNVITRFAP SPTGFLHIGS ARTALFNYLF ARHHNGKFLL RIEDTDKERS TNEAVEAIFS 

        70         80         90        100        110        120 
GLKWLGLDWD GEVIFQSKRN DLYKETALKL LQAGKAYYCF TSQEEIEKQR QKALENKQYF 

       130        140        150        160        170        180 
IFNSDWRDKD PAAYPTDIKP VIRLKTPREG SITIRDTLQG DVVIENSHID DMVLLRSDGT 

       190        200        210        220        230        240 
ATYMLAVVVD DHDMGITHII RGDDHLTNAA RQIAIYQACG YAVPSMTHIP LIHGADGAKL 

       250        260        270        280        290        300 
SKRHGALGVA AYKDMGYLPE SVCNYLLRLG WSHGDDEIIS MDQAIKWFNL DSLGKSPAKL 

       310        320        330        340        350        360 
DFANMNSLNA HYLRLLDNDS ATSKTVERLR QNYNVSKQEV IYINQAIRSL LVRSETLLDL 

       370        380        390        400        410        420 
VQLAQIYLVD SPIIYKQDAK EIIENCDKDL IKQVIENLNK LKQFDKESVQ NKFKEIATHN 

       430        440        450        460 
GLKLNELMKP VRALITGMTA SPSVFEIAEI LGKENILKRL KII 

« Hide

References

[1]"Complete genome sequence of Rickettsia canadensis."
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: McKiel.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000409 Genomic DNA. Translation: ABV73272.1.
RefSeqYP_001492057.1. NC_009879.1.

3D structure databases

ProteinModelPortalA8EY39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293613.A1E_01635.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV73272; ABV73272; A1E_01635.
GeneID5626862.
KEGGrcm:A1E_01635.
PATRIC17885273. VBIRicCan89738_0358.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRCAN293613:GHI3-329-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE1_RICCK
AccessionPrimary (citable) accession number: A8EY39
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 45 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