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Q7SIA2

- SYEP_CRIGR

UniProt

Q7SIA2 - SYEP_CRIGR

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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

EPRS

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 3 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).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

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-tRNA ligase activity Source: UniProtKB-EC
  3. proline-tRNA ligase activity Source: UniProtKB-EC
  4. RNA stem-loop binding Source: UniProtKB

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. tRNA aminoacylation for protein translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-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:6.1.1.15)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

GO - Cellular componenti

  1. GAIT complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›49›49Bifunctional glutamate/proline--tRNA ligasePRO_0000119742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N6-acetyllysineBy similarity
Modified residuei46 – 461PhosphotyrosineBy similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

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).By similarity

Structurei

Secondary structure

1
49
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1615Combined sources
Helixi21 – 3818Combined sources
Beta strandi40 – 456Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7SIA2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini‹1 – ›49›49WHEP-TRSPROSITE-ProRule annotationAdd
BLAST

Domaini

The WHEP-TRS domain is involved in RNA binding.

Sequence similaritiesi

Contains at least 1 WHEP-TRS domain.Curated

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
InterProiIPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view]
PfamiPF00458. WHEP-TRS. 1 hit.
[Graphical view]
SMARTiSM00991. WHEP-TRS. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
PROSITEiPS51185. WHEP_TRS_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei49 – 491

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D2D NMR - A 1-49 [» ]
1R1B NMR - A 1-49 [» ]
ProteinModelPortali Q7SIA2.
SMRi Q7SIA2. Positions 1-49.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q7SIA2.

Family and domain databases

Gene3Di 1.10.287.10. 1 hit.
InterProi IPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view ]
Pfami PF00458. WHEP-TRS. 1 hit.
[Graphical view ]
SMARTi SM00991. WHEP-TRS. 1 hit.
[Graphical view ]
SUPFAMi SSF47060. SSF47060. 1 hit.
PROSITEi PS51185. WHEP_TRS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSYEP_CRIGR
AccessioniPrimary (citable) accession number: Q7SIA2
Secondary accession number(s): Q7SIG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: November 26, 2014
This is version 52 of the entry and version 2 of the sequence. [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
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3