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Q2S1L8 (SYE_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:SRU_1796
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length488 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.

Sequence caution

The sequence ABC45991.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 488488Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237398

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S1L8 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 08A6D9EF6C11EDA8

FASTA48854,926
        10         20         30         40         50         60 
MASDAPVRVR FAPSPTGRLH IGGLRTALYN YLFARKHDGD FVLRIEDTDQ ARYEPGAEDD 

        70         80         90        100        110        120 
IREALAWTGL EHDEGPEQGG DYAPYRQSER SEHYHEYAQK LVEAGRAYYA FDTEEELEEL 

       130        140        150        160        170        180 
REEHGAYDGS TRRQMRNSLT LSDEKVEQRI DEGDDYVIRL KVPRQESVQV EDEIRGTVSF 

       190        200        210        220        230        240 
DTSEIDDQVL VKSDGMPTYH LANIVDDHLM NISHVIRGEE WLSSTPKHVL MYDALGWEPP 

       250        260        270        280        290        300 
AFAHLPLILS PNGGKLSKRD ANELGIPVYV MDYREAGYEP EALLNFLALL GWSPGTEEEL 

       310        320        330        340        350        360 
FALDEMVETF SLDRVGASGV QFDLDKLRWV NEHYVRALSV DALAEKARPH VEAAGYDVSD 

       370        380        390        400        410        420 
DRLQTICGLV QDRIQVVPEV VTDNRYFFED PEAYEEAGVE KRWNEESADL LLAYADRLEG 

       430        440        450        460        470        480 
VDAFDTDTVE TELRDLADEK DVGAGAIIHP SRLAVSGRSY GPGVFGLLAA VGKEACIRRM 


HRAVEALG 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC45991.1. Different initiation.
RefSeqYP_445913.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S1L8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_1796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC45991; ABC45991; SRU_1796.
GeneID3852853.
KEGGsru:SRU_1796.
PATRIC23426067. VBISalRub86502_1866.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OrthoDBEOG6DRPF7.
PhylomeDBQ2S1L8.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-1794-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 nameSYE_SALRD
AccessionPrimary (citable) accession number: Q2S1L8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 63 of the entry and version 2 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