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
cell part
intracellular part
cytoplasm
Function
aminoacyl-tRNA ligase activity
catalytic activity
nucleotide binding
ligase activity
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
Process
metabolic process
cellular macromolecule metabolic process
macromolecule metabolic process
RNA metabolic process
ncRNA metabolic process
tRNA metabolic process
biosynthetic process
tRNA aminoacylation
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
aspartyl-tRNA aminoacylation
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