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Q2GDP4 (SYE1_NEOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:NSE_0518
OrganismNeorickettsia sennetsu (strain Miyayama) [Complete proteome] [HAMAP]
Taxonomic identifier222891 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeNeorickettsia

Protein attributes

Sequence length433 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 – 433433Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367718

Regions

Motif7 – 1711"HIGH" region HAMAP-Rule MF_00022
Motif230 – 2345"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2331ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2GDP4 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 862FFB1C69E5A119

FASTA43349,866
        10         20         30         40         50         60 
MITRFAPSPT GLIHLGNART ALIAYFAARS SGGEFILRID DTDVTRIKSE YVNKIFTDLS 

        70         80         90        100        110        120 
WLGIKEDLCI KQSERCELYA NAVVKLKESG RIYPCYETPE ELEIERRSLL ARALPPVYRR 

       130        140        150        160        170        180 
KNRPQHSTRL PYYRFELDPD RVVIWEDKLR GKIVIDLHST SDPIVIRENG TYTYMLPSVV 

       190        200        210        220        230        240 
DDIECRISTI IRGEDHISNT AVQIQMFEAL GCTEIPKFAH MPLLKLQTGK MSKRAGGNEI 

       250        260        270        280        290        300 
QTFRENYIEP EVICLYLLNL GSKSRSTFKN YKDYSNFNLE NYSSSSSVTV LEDEIYSLNA 

       310        320        330        340        350        360 
DFLRLSNYED LARRLGGVSK TFWDAVKNNV KSIPEVNYWW EICTTEAKLY PGIGCNAQLV 

       370        380        390        400        410        420 
RDAISVLPQE EVSRETYRRW VELIVENYRY DKREVHINLR LALTGKVGGP EMAAILPFIS 

       430 
RERILIRLND SLS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000237 Genomic DNA. Translation: ABD46392.1.
RefSeqYP_506402.1. NC_007798.1.

3D structure databases

ProteinModelPortalQ2GDP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222891.NSE_0518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD46392; ABD46392; NSE_0518.
GeneID3931642.
KEGGnse:NSE_0518.
PATRIC22681085. VBINeoSen119815_0469.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAICTTEAK.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycNSEN222891:GHFU-520-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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_NEOSM
AccessionPrimary (citable) accession number: Q2GDP4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 21, 2006
Last modified: May 14, 2014
This is version 64 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