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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

EPRS

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, RNA-binding
Biological processProtein biosynthesis, Translation regulation
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase
Including the following 2 domains:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Proline--tRNA ligase (EC:6.1.1.15By similarity)
Alternative name(s):
Prolyl-tRNA synthetase
Short name:
ProRS
Gene namesi
Name:EPRS
Synonyms:QPRS
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000119742‹1 – ›49Bifunctional glutamate/proline--tRNA ligaseAdd BLAST›49

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35N6-acetyllysineBy similarity1
Modified residuei46PhosphotyrosineBy similarity1

Post-translational modificationi

Phosphorylated at Ser-886 by CDK5 and at Ser-999 by an unknown kinase in a IFN-gamma-dependent manner in monocytes; these sequential phosphorylations are causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition. Phosphorylation at Ser-999 is specifically required for the interaction of GAIT complex-associated RPL13A with eIF4G.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Homodimer. Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex. Interacts with DUS2L. Component of the GAIT complex; in humans the complex assembly seems to be a two-step process in which EPRS first associates with SYNCRIP to form a pre-GAIT complex which is deficient in GAIT element binding.By similarity

Structurei

Secondary structure

149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 16Combined sources15
Helixi21 – 38Combined sources18
Beta strandi40 – 45Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D2DNMR-A1-49[»]
1R1BNMR-A1-49[»]
ProteinModelPortaliQ7SIA2.
SMRiQ7SIA2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIA2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – ›49WHEP-TRSPROSITE-ProRule annotationAdd BLAST›49

Domaini

The WHEP-TRS domain is involved in RNA binding.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
InterProiView protein in InterPro
IPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS_dom.
PfamiView protein in Pfam
PF00458. WHEP-TRS. 1 hit.
SMARTiView protein in SMART
SM00991. WHEP-TRS. 1 hit.
SUPFAMiSSF47060. SSF47060. 1 hit.
PROSITEiView protein in PROSITE
PS51185. WHEP_TRS_2. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q7SIA2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
YDKIAAQGEV VRKLKAEKAP KAKVTEAVEC LLSLKAEYKE KTGKEYVPG
Length:49
Mass (Da):5,409
Last modified:July 19, 2004 - v2
Checksum:iA8B609A53C7E695A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei491

Similar proteinsi

Entry informationi

Entry nameiSYEP_CRIGR
AccessioniPrimary (citable) accession number: Q7SIA2
Secondary accession number(s): Q7SIG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: October 25, 2017
This is version 62 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references