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Q7SIA2 (SYEP_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase

Including the following 2 domains:

  1. Glutamate--tRNA ligase
    EC=6.1.1.17
    Alternative name(s):
    Glutamyl-tRNA synthetase
    Short name=GluRS
  2. Proline--tRNA ligase
    EC=6.1.1.15
    Alternative name(s):
    Prolyl-tRNA synthetase
    Short name=ProRS
Gene names
Name:EPRS
Synonyms:QPRS
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length49 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation By similarity.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

Subunit structure

Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L. Component of the GAIT complex By similarity.

Domain

The WHEP-TRS domain is involved in RNA binding.

Post-translational modification

Phosphorylated in a IFN-gamma-dependent manner; the phosphorylation is causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition.

Sequence similarities

Contains at least 1 WHEP-TRS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›49›49Bifunctional glutamate/proline--tRNA ligase
PRO_0000119742

Regions

Domain‹1 – ›49›49WHEP-TRS

Amino acid modifications

Modified residue351N6-acetyllysine By similarity
Modified residue461Phosphotyrosine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue491

Secondary structure

....... 49
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7SIA2 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: A8B609A53C7E695A

FASTA495,409
        10         20         30         40 
YDKIAAQGEV VRKLKAEKAP KAKVTEAVEC LLSLKAEYKE KTGKEYVPG 

« Hide

References

[1]"A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases."
Cahuzac B., Berthonneau E., Birlirakis N., Guittet E., Mirande M.
EMBO J. 19:445-452(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-49, RNA-BINDING SITE.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2DNMR-A1-49[»]
1R1BNMR-A1-49[»]
ProteinModelPortalQ7SIA2.
SMRQ7SIA2. Positions 1-49.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.287.10. 1 hit.
InterProIPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view]
PfamPF00458. WHEP-TRS. 1 hit.
[Graphical view]
SMARTSM00991. WHEP-TRS. 1 hit.
[Graphical view]
SUPFAMSSF47060. SSF47060. 1 hit.
PROSITEPS51185. WHEP_TRS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7SIA2.

Entry information

Entry nameSYEP_CRIGR
AccessionPrimary (citable) accession number: Q7SIA2
Secondary accession number(s): Q7SIG9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: March 19, 2014
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries