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Identification
NamePhenylalanyl-tRNA synthetase alpha chain
Synonyms
  • Phenylalanine--tRNA ligase alpha chain
  • PheRS
Gene NameFRS2
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00304L-PhenylalanineShow
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
nucleic acid binding
adenyl nucleotide binding
RNA binding
adenyl ribonucleotide binding
tRNA binding
ATP binding
phenylalanine-tRNA ligase activity
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
phenylalanyl-tRNA aminoacylation
Gene Properties
Chromosome Locationchromosome 6
LocusYFL022C
Gene Sequence>1512 bp ATGTCTGATTTCCAATTAGAAATTCTAAAAAAACTAGATGAATTGGATGAGATCAAGTCC ACACTGGCAACTTTCCCTCAGCACGGCTCTCAAGATGTTCTTTCCGCTTTGAACTCTTTG AAAGCCCACAACAAGTTAGAGTTTTCCAAGGTCGACACGGTTACGTATGACTTGACCAAA GAAGGTGCTCAAATTTTGAATGAAGGTTCGTACGAAATTAAACTAGTCAAGCTCATCCAA GAGTTGGGTCAACTTCAAATCAAAGATGTGATGTCCAAACTGGGTCCTCAAGTTGGTAAG GTCGGTCAGGCTAGAGCTTTCAAGAACGGCTGGATCGCCAAAAACGCCTCAAACGAGCTT GAACTCTCCGCAAAATTGCAAAATACCGATTTAAATGAGCTTACTGATGAAACGCAATCT ATTCTAGCGCAAATCAAGAACAACTCGCATCTGGATAGCATTGACGCCAAGATTTTGAAC GACTTGAAGAAAAGAAAGTTAATTGCTCAAGGTAAAATCACAGATTTCAACGTTACCAAA GGGCCAGAGTTCTCGACCGACCTCACCAAATTGGAAACCGATCTTACCTCCGACATGGTC TCCACCAATGCATACAAGGACTTGAAGTTCAAGCCTTACAATTTCAATTCTCAAGGTGTG CAAATATCTTCAGGTGCTCTTCACCCCTTAAACAAAGTCAGAGAGGAATTTAGACAAATT TTCTTTTCCATGGGATTCACAGAGATGCCCTCGAACCAATACGTCGAGACAGGTTTCTGG AACTTCGATGCCCTTTACGTCCCACAACAGCATCCTGCTCGTGACCTGCAAGACACTTTC TACATCAAGGACCCACTAACCGCTGACTTGCCCGATGACAAGACATACATGGACAATATC AAAGCCGTTCACGAACAGGGGAGATTCGGGTCCATCGGTTATCGTTACAACTGGAAGCCA GAAGAATGTCAAAAATTGGTCTTGAGAACTCACTCCACAGCCATCTCTGCCAGAATGCTG CACGATTTGGCCAAAGATCCAAAGCCCACCAGATTGTTTTCTATCGACCGTGTTTTCCGT AACGAAGCAGTTGACGCCACCCATTTGGCCGAATTCCACCAGGTGGAAGGTGTTCTTGCC GACTACAACATTACTCTGGGTGACCTGATCAAGTTCATGGAAGAGTTTTTCGAAAGAATG GGTGTCACCGGTTTGAGATTCAAGCCTACCTACAATCCTTACACCGAGCCATCAATGGAA ATCTTTTCTTGGCACGAAGGTTTGCAAAAATGGGTCGAAATCGGTAACTCTGGTATGTTC AGACCAGAAATGCTCGAGTCCATGGGTCTACCAAAGGATCTAAGAGTCCTTGGTTGGGGG TTATCCTTGGAAAGACCTACCATGATCAAATATAAGGTTCAAAACATCAGAGAACTGTTA GGTCATAAAGTCTCTTTGGACTTTATCGAAACCAATCCTGCTGCTAGATTGGACGAAGAC TTGTACGAATAA
Protein Properties
Pfam Domain Function
Protein Residues503
Protein Molecular Weight57511.0
Protein Theoretical pI5.53
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Phenylalanyl-tRNA synthetase alpha chain MSDFQLEILKKLDELDEIKSTLATFPQHGSQDVLSALNSLKAHNKLEFSKVDTVTYDLTK EGAQILNEGSYEIKLVKLIQELGQLQIKDVMSKLGPQVGKVGQARAFKNGWIAKNASNEL ELSAKLQNTDLNELTDETQSILAQIKNNSHLDSIDAKILNDLKKRKLIAQGKITDFNVTK GPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEFRQI FFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPDDKTYMDNI KAVHEQGRFGSIGYRYNWKPEECQKLVLRTHSTAISARMLHDLAKDPKPTRLFSIDRVFR NEAVDATHLAEFHQVEGVLADYNITLGDLIKFMEEFFERMGVTGLRFKPTYNPYTEPSME IFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTMIKYKVQNIRELL GHKVSLDFIETNPAARLDEDLYE
References
External Links
ResourceLink
Saccharomyces Genome Database FRS2
Uniprot IDP15625
Uniprot NameSYFA_YEAST
GenBank Gene IDD50617
Genebank Protein ID836732
General Reference
  • Sanni, A., Mirande, M., Ebel, J. P., Boulanger, Y., Waller, J. P., Fasiolo, F. (1988). "Structure and expression of the genes encoding the alpha and beta subunits of yeast phenylalanyl-tRNA synthetase." J Biol Chem 263:15407-15415.3049607
  • Murakami, Y., Naitou, M., Hagiwara, H., Shibata, T., Ozawa, M., Sasanuma, S., Sasanuma, M., Tsuchiya, Y., Soeda, E., Yokoyama, K., et, a. l. .. (1995). "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Nat Genet 10:261-268.7670463
  • Fasiolo, F., Sanni, A., Potier, S., Ebel, J. P., Boulanger, Y. (1989). "Identification of the major tRNA(Phe) binding domain in the tetrameric structure of cytoplasmic phenylalanyl-tRNA synthetase from baker's yeast." FEBS Lett 242:351-356.2644133
  • 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
  • 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