Aspartyl-tRNA synthetase, cytoplasmic (P04802)

Identification
NameAspartyl-tRNA synthetase, cytoplasmic
Synonyms
  • Aspartate--tRNA ligase
  • AspRS
Gene NameDPS1
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
L-Aspartic acid + Adenosine triphosphate + tRNA(Asp) → Adenosine monophosphate + Pyrophosphate + Asp-tRNA(Asp)
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00896L-Aspartic acidShow
GO Classification
Component
intracellular part
cytoplasm
cell part
Function
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
nucleic acid binding
adenyl ribonucleotide binding
aspartate-tRNA ligase activity
ATP binding
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-tRNA and related compounds
catalytic activity
aminoacyl-tRNA ligase activity
nucleotide binding
ligase activity
Process
tRNA aminoacylation
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
aspartyl-tRNA aminoacylation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
RNA metabolic process
ncRNA metabolic process
biosynthetic process
tRNA metabolic process
Gene Properties
Chromosome Locationchromosome 12
LocusYLL018C
Gene Sequence>1674 bp ATGTCTCAAGACGAAAATATTGTCAAAGCTGTTGAAGAATCCGCAGAACCTGCTCAAGTT ATTCTTGGGGAAGATGGTAAGCCATTGTCCAAGAAGGCCTTGAAGAAATTGCAGAAAGAG CAAGAGAAACAGAGAAAGAAGGAGGAAAGAGCTCTCCAGTTGGAAGCTGAAAGAGAAGCC CGTGAAAAGAAAGCCGCTGCCGAAGACACCGCAAAGGACAACTACGGTAAGTTGCCATTG ATCCAGTCTCGTGACTCTGACAGAACTGGTCAGAAGCGTGTCAAGTTTGTTGACTTGGAT GAGGCTAAGGATAGCGACAAAGAAGTCCTCTTCAGGGCAAGAGTCCACAACACCAGACAA CAAGGTGCAACATTGGCCTTTTTAACTTTAAGGCAACAAGCTTCCTTGATCCAAGGTCTA GTAAAGGCCAACAAGGAAGGTACCATCAGCAAAAACATGGTCAAATGGGCTGGTTCATTG AATTTGGAGTCCATTGTCCTTGTCAGAGGTATTGTCAAGAAGGTAGATGAGCCAATCAAG TCTGCTACTGTGCAAAACCTGGAAATTCACATTACCAAGATTTATACCATTTCCGAGACT CCAGAAGCATTGCCAATCCTTTTGGAAGATGCCTCCCGTTCCGAAGCTGAAGCTGAAGCT GCAGGTTTGCCCGTGGTCAACTTGGACACCAGATTAGACTACCGTGTCATTGACTTGAGA ACCGTCACCAACCAAGCTATTTTCAGGATTCAAGCTGGTGTTTGTGAGTTGTTCAGAGAA TATTTGGCCACAAAGAAATTTACCGAAGTACACACACCAAAACTGTTGGGTGCACCAAGT GAAGGTGGTTCCAGTGTGTTTGAGGTGACATACTTCAAAGGGAAGGCCTACCTAGCTCAA TCTCCACAATTTAACAAGCAACAATTGATTGTGGCCGACTTTGAAAGAGTTTACGAAATC GGGCCTGTGTTCAGGGCTGAAAACTCCAACACCCACCGTCACATGACCGAGTTTACTGGT TTGGACATGGAAATGGCTTTCGAAGAACATTACCACGAAGTTTTGGACACGTTGAGTGAG TTGTTTGTGTTTATTTTCAGTGAATTGCCCAAGAGATTTGCTCATGAAATTGAGTTGGTA CGTAAGCAATACCCTGTTGAAGAATTCAAGTTACCTAAAGATGGTAAGATGGTTCGTCTA ACATACAAAGAAGGTATTGAAATGCTAAGAGCTGCCGGTAAGGAAATTGGTGATTTTGAA GACTTGAGTACCGAAAATGAAAAGTTCTTGGGTAAGTTGGTTCGCGACAAATACGACACC GACTTTTACATCCTAGACAAGTTCCCCTTGGAGATCCGTCCCTTCTACACAATGCCCGAC CCAGCCAACCCTAAGTATTCTAACTCGTATGATTTCTTCATGAGGGGTGAAGAAATCTTG TCCGGTGCACAACGTATCCACGACCATGCTCTATTACAAGAAAGGATGAAAGCCCATGGT TTGTCTCCTGAGGACCCAGGTCTAAAGGACTACTGTGACGGCTTCAGCTATGGGTGTCCT CCACACGCCGGTGGTGGTATCGGTTTGGAAAGAGTTGTTATGTTCTATTTGGATTTGAAA AATATCAGAAGAGCTTCATTGTTCCCAAGAGATCCAAAGAGATTAAGACCATGA
Protein Properties
Pfam Domain Function
Protein Residues557
Protein Molecular Weight63514.89844
Protein Theoretical pI6.53
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Aspartyl-tRNA synthetase, cytoplasmic MSQDENIVKAVEESAEPAQVILGEDGKPLSKKALKKLQKEQEKQRKKEERALQLEAEREA REKKAAAEDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQ QGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIK SATVQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLR TVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQ SPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSE LFVFIFSELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFE DLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEIL SGAQRIHDHALLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLK NIRRASLFPRDPKRLRP
References
External Links
ResourceLink
Saccharomyces Genome Database DPS1
Uniprot IDP04802
Uniprot NameSYDC_YEAST
GenBank Gene IDX03606
Genebank Protein ID3370
PDB ID
1ASZ
General Reference
  • Reid, G. A. (1988). "Sequence polymorphisms in the yeast gene encoding aspartyl tRNA synthase." Nucleic Acids Res 16:1212.3278298
  • Sellami, M., Fasiolo, F., Dirheimer, G., Ebel, J. P., Gangloff, J. (1986). "Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5' and 3' termini of AspRS mRNA." Nucleic Acids Res 14:1657-1666.3513127
  • Purnelle, B., Goffeau, A. (1997). "The sequence of 32b on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABS transporter homologous to the human multidrug resistance protein." Yeast 13:183-188.9046100
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Amiri, I., Mejdoub, H., Hounwanou, N., Boulanger, Y., Reinbolt, J. (1985). "The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae." Biochimie 67:607-613.3902099
  • Miosga, T., Zimmermann, F. K. (1996). "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a 43.7 kb fragment of chromosome XII including an open reading frame homologous to the human cystic fibrosis transmembrane conductance regulator protein CFTR." Yeast 12:693-708.8810043
  • Gasparini, S., Vincendon, P., Eriani, G., Gangloff, J., Boulanger, Y., Reinbolt, J., Kern, D. (1991). "Identification of structurally and functionally important histidine residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae." Biochemistry 30:4284-4289.2021621
  • Eriani, G., Cavarelli, J., Martin, F., Dirheimer, G., Moras, D., Gangloff, J. (1993). "Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline." Proc Natl Acad Sci U S A 90:10816-10820.8248175
  • Garrels, J. I., McLaughlin, C. S., Warner, J. R., Futcher, B., Latter, G. I., Kobayashi, R., Schwender, B., Volpe, T., Anderson, D. S., Mesquita-Fuentes, R., Payne, W. E. (1997). "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Electrophoresis 18:1347-1360.9298649
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Ruff, M., Krishnaswamy, S., Boeglin, M., Poterszman, A., Mitschler, A., Podjarny, A., Rees, B., Thierry, J. C., Moras, D. (1991). "Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)." Science 252:1682-1689.2047877
  • Cavarelli, J., Eriani, G., Rees, B., Ruff, M., Boeglin, M., Mitschler, A., Martin, F., Gangloff, J., Thierry, J. C., Moras, D. (1994). "The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction." EMBO J 13:327-337.8313877