Lysyl-tRNA synthetase, cytoplasmic (P15180)

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-Lysine → Adenosine monophosphate + Pyrophosphate + Lys-tRNA(Lys)
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00330L-LysineShow
GO Classification
Component
cell part
intracellular part
cytoplasm
Function
nucleic acid binding
adenyl nucleotide binding
lysine-tRNA ligase activity
adenyl ribonucleotide binding
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
nucleoside binding
purine nucleoside binding
Process
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
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
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