ID:SYRC_HUMAN DESCRIPTION: RecName: Full=Arginine--tRNA ligase, cytoplasmic; EC=6.1.1.19; AltName: Full=Arginyl-tRNA synthetase; Short=ArgRS; FUNCTION: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1. CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius); KM=3.5 uM for arginine (arginylation at 37 degrees Celsius); KM=1183 uM for ATP (ATP-PPi exchange at 37 Celsius); KM=910 uM for ATP (arginylation at 37 Celsius); KM=0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius); KM=0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius); SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. INTERACTION: Q9P2J5:LARS; NbExp=3; IntAct=EBI-355482, EBI-356077; SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
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: PF00750 - tRNA synthetases class I (R) PF03485 - Arginyl tRNA synthetase N terminal domain PF05746 - DALR anticodon binding domain
SCOP Domains: 47323 - Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases 52374 - Nucleotidylyl transferase 64496 - DNA-binding domain of intron-encoded endonucleases 55190 - Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain
ModBase Predicted Comparative 3D Structure on P54136
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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.