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Identification
NameLysyl-tRNA synthetase, cytoplasmic
Synonyms
  • Lysine--tRNA ligase
  • LysRS
Gene NameKRS1
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
Adenosine triphosphate + tRNA(Lys) + L-LysineAdenosine monophosphate + Pyrophosphate + Lys-tRNA(Lys)
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00330L-LysineShow
GO Classification
Component
intracellular part
cytoplasm
cell part
Function
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
nucleic acid binding
adenyl ribonucleotide binding
lysine-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
binding
Process
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
lysyl-tRNA aminoacylation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
RNA metabolic process
ncRNA metabolic process
biosynthetic process
tRNA metabolic process
tRNA aminoacylation
Gene Properties
Chromosome Locationchromosome 4
LocusYDR037W
Gene Sequence>1776 bp ATGTCTCAACAAGATAATGTCAAAGCCGCCGCTGAAGGTGTTGCTAACCTACATCTCGAC GAAGCTACCGGGGAAATGGTCTCCAAGTCTGAATTGAAGAAGCGTATCAAGCAAAGACAA GTCGAAGCTAAAAAGGCCGCCAAAAAGGCTGCCGCTCAACCAAAACCGGCTTCCAAAAAA AAAACAGATTTGTTCGCTGACCTGGATCCATCGCAATATTTCGAAACAAGATCTCGCCAA ATTCAAGAATTGAGAAAGACTCACGAACCAAATCCATACCCACACAAGTTTCACGTTTCT ATATCCAATCCTGAGTTCTTGGCCAAATATGCGCATTTGAAAAAAGGTGAAACCTTACCT GAAGAGAAGGTTTCAATTGCTGGTAGAATTCATGCCAAAAGAGAATCTGGCTCCAAATTG AAATTCTATGTTCTTCACGGTGATGGTGTTGAAGTTCAATTGATGTCCCAATTGCAGGAC TACTGCGACCCAGACTCTTACGAAAAGGATCACGACCTTTTGAAAAGGGGTGATATCGTT GGTGTCGAGGGTTACGTCGGAAGAACTCAACCAAAGAAAGGTGGTGAAGGTGAAGTTTCC GTCTTCGTTAGCAGAGTGCAATTATTGACACCATGTTTGCACATGTTACCTGCCGACCAC TTTGGTTTCAAAGACCAGGAAACCAGATACAGAAAGCGTTATTTGGATTTGATCATGAAC AAAGACGCCAGAAACCGTTTTATTACCCGTTCTGAAATTATCCGTTACATCAGAAGATTT TTGGACCAAAGAAAGTTTATTGAAGTAGAAACTCCAATGATGAACGTTATTGCTGGTGGT GCTACCGCTAAGCCATTTATTACCCACCATAATGACCTTGATATGGACATGTACATGAGA ATTGCTCCAGAATTGTTCTTGAAACAATTGGTTGTCGGTGGTTTGGATCGTGTTTACGAA ATTGGTAGACAATTCAGAAATGAAGGTATCGATATGACACATAATCCAGAATTCACCACT TGTGAGTTTTATCAAGCCTACGCTGATGTTTATGATTTGATGGATATGACTGAATTGATG TTTTCAGAAATGGTCAAGGAGATCACTGGTTCTTATATTATCAAATACCATCCGGACCCT GCTGATCCAGCCAAAGAACTAGAATTGAACTTTTCTAGACCATGGAAGAGAATCAACATG ATTGAAGAATTAGAAAAGGTATTCAACGTTAAGTTCCCATCTGGTGATCAATTACATACA GCTGAGACTGGTGAATTTTTGAAAAAGATTCTTGTCGACAACAAATTAGAATGTCCACCT CCACTAACTAATGCTCGTATGTTAGATAAGCTTGTCGGTGAATTAGAAGATACATGTATC AACCCAACTTTCATTTTTGGCCACCCTCAAATGATGTCTCCATTAGCCAAGTACTCAAGA GATCAACCGGGTCTATGTGAGCGTTTCGAGGTCTTTGTAGCTACAAAGGAAATTTGTAAT GCCTACACTGAATTGAACGATCCATTTGACCAAAGGGCACGTTTCGAAGAACAAGCTAGA CAAAAGGATCAAGGTGATGACGAAGCTCAATTAGTCGATGAAACCTTCTGTAATGCTCTA GAATACGGTTTACCACCAACTGGTGGTTGGGGTTGTGGTATTGATAGACTGGCCATGTTC TTGACCGACTCCAACACCATTAGAGAAGTCTTATTGTTCCCAACTTTGAAGCCTGATGTT TTGAGAGAGGAAGTCAAAAAGGAAGAAGAAAATTAA
Protein Properties
Pfam Domain Function
Protein Residues591
Protein Molecular Weight67958.0
Protein Theoretical pI6.01
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Lysyl-tRNA synthetase, cytoplasmic MSQQDNVKAAAEGVANLHLDEATGEMVSKSELKKRIKQRQVEAKKAAKKAAAQPKPASKK KTDLFADLDPSQYFETRSRQIQELRKTHEPNPYPHKFHVSISNPEFLAKYAHLKKGETLP EEKVSIAGRIHAKRESGSKLKFYVLHGDGVEVQLMSQLQDYCDPDSYEKDHDLLKRGDIV GVEGYVGRTQPKKGGEGEVSVFVSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMN KDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMR IAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELM FSEMVKEITGSYIIKYHPDPADPAKELELNFSRPWKRINMIEELEKVFNVKFPSGDQLHT AETGEFLKKILVDNKLECPPPLTNARMLDKLVGELEDTCINPTFIFGHPQMMSPLAKYSR DQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNAL EYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKPDVLREEVKKEEEN
References
External Links
ResourceLink
Saccharomyces Genome Database KRS1
Uniprot IDP15180
Uniprot NameSYKC_YEAST
GenBank Gene IDJ04186
Genebank Protein ID171799
General Reference
  • Mirande, M., Waller, J. P. (1988). "The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid control of its expression and domain structure of the encoded protein." J Biol Chem 263:18443-18451.2903861
  • Martinez, R., Latreille, M. T., Mirande, M. (1991). "A PMR2 tandem repeat with a modified C-terminus is located downstream from the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces cerevisiae." Mol Gen Genet 227:149-154.2046655
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Lanker, S., Bushman, J. L., Hinnebusch, A. G., Trachsel, H., Mueller, P. P. (1992). "Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5/KRS1 by translational and transcriptional control mechanisms." Cell 70:647-657.1505029
  • Garrels, J. I., Futcher, B., Kobayashi, R., Latter, G. I., Schwender, B., Volpe, T., Warner, J. R., McLaughlin, C. S. (1994). "Protein identifications for a Saccharomyces cerevisiae protein database." Electrophoresis 15:1466-1486.7895733
  • 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
  • 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