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Q7SIA2

- SYEP_CRIGR

UniProt

Q7SIA2 - SYEP_CRIGR

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
  1. 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

    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

    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 – 1615
    Helixi21 – 3818
    Beta strandi40 – 456

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    YDKIAAQGEV VRKLKAEKAP KAKVTEAVEC LLSLKAEYKE KTGKEYVPG    49
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 51 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