ID:SYEP_HUMAN DESCRIPTION: RecName: Full=Bifunctional glutamate/proline--tRNA ligase; AltName: Full=Bifunctional aminoacyl-tRNA synthetase; AltName: Full=Cell proliferation-inducing gene 32 protein; Includes: RecName: Full=Glutamate--tRNA ligase; EC=6.1.1.17; AltName: Full=Glutamyl-tRNA synthetase; Short=GluRS; Includes: RecName: Full=Proline--tRNA ligase; EC=6.1.1.15; AltName: Full=Prolyl-tRNA synthetase; 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 (By similarity). CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). SUBUNIT: 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. INTERACTION: P41252:IARS; NbExp=4; IntAct=EBI-355315, EBI-355303; DOMAIN: The WHEP-TRS domain is involved in RNA binding. PTM: Phosphorylated at Ser-886 by CDK5 in a IFN-gamma-dependent manner; this phosphorylation activates assembly of the GAIT (IFN- gamma-activated inhibitor of translation) complex, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells. SIMILARITY: In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family. SIMILARITY: In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family. SIMILARITY: Contains 3 WHEP-TRS domains. CAUTION: Was originally thought to be a glutaminyl-tRNA synthetase. SEQUENCE CAUTION: Sequence=AAH15494.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=AAH34797.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=AAH46156.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=AAH58921.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=AAS72877.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=CAA30354.1; Type=Miscellaneous discrepancy; Note=Sequencing errors; Sequence=CAA38224.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF00043 - Glutathione S-transferase, C-terminal domain PF00458 - WHEP-TRS domain PF00587 - tRNA synthetase class II core domain (G, H, P, S and T) PF00749 - tRNA synthetases class I (E and Q), catalytic domain PF03129 - Anticodon binding domain PF03950 - tRNA synthetases class I (E and Q), anti-codon binding domain PF09180 - Prolyl-tRNA synthetase, C-terminal
SCOP Domains: 47060 - S15/NS1 RNA-binding domain 47616 - GST C-terminal domain-like 50715 - Ribosomal protein L25-like 52374 - Nucleotidylyl transferase 52954 - Class II aaRS ABD-related 55681 - Class II aaRS and biotin synthetases 64586 - C-terminal domain of ProRS
ModBase Predicted Comparative 3D Structure on P07814
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.