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Q7UNF9 (SYE_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:RB7600
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length515 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 CAD75460.1 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 – 515515Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119634

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UNF9 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: E91E67F990E1E651

FASTA51556,844
        10         20         30         40         50         60 
MIRTRFAPSP TGYLHIGGVR TALFNWLLAK QAGGQFILRI DDTDAGRNVD AALKPILDGF 

        70         80         90        100        110        120 
RWLGMDWDEG PDVGGPHGPY FQSERGDQYR AAAEKLLADG HAYRDFAKPE ELQTLREEAQ 

       130        140        150        160        170        180 
KGGEAFVYDR RWMAEDEATA AKFEAEGRQG VVRLKMPREG QCVIQDLIRG EVVVEWASEQ 

       190        200        210        220        230        240 
DHVIARADGS PLYHLASVVD DHELKITHVV RAAEHLPNTA RQVFIAQSLG YELPIYAHLP 

       250        260        270        280        290        300 
YVAEPGGSAK LSKRKLDKYK KNRDFAVLLA HGEKIAERCN MQVDADTFNP VLVDFYREIG 

       310        320        330        340        350        360 
FLPDALLNYL LLLGWSLDGE TEKFTIAEMI EKFTLDRVNK APASFDPAKL QSFQGDAFAE 

       370        380        390        400        410        420 
LSDEKRTELV RPFAVAAGFV ADGDADETLK AVLAAAGDRL KMAGDIVDFD YCFVDDYSVD 

       430        440        450        460        470        480 
EKAYEKRLAK ADGAKELLAK LNETLKAATE FDAANVETTV KSFCESEGIK IGQIIHALRV 

       490        500        510 
ATTGAASGFG MFDTLAVLGK DKVTARIEKT IAGLS 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294146 Genomic DNA. Translation: CAD75460.1. Different initiation.
RefSeqNP_867913.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UNF9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB7600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD75460; CAD75460; RB7600.
GeneID1791060.
KEGGrba:RB7600.
PATRIC23248801. VBIRhoBal59814_3674.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.
ProtClustDBCLSK2759267.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 2 hits.
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. 2 hits.
[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_RHOBA
AccessionPrimary (citable) accession number: Q7UNF9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 70 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