Tryptophanyl-tRNA synthetase, mitochondrial (P04803)

Identification
NameTryptophanyl-tRNA synthetase, mitochondrial
Synonyms
  • Tryptophan--tRNA ligase
  • TrpRS
Gene NameMSW1
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Cellular LocationMitochondrion matrix
SMPDB Pathways
Tryptophan metabolismPW002442 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Tryptophan metabolismec00380 Map00380
SMPDB ReactionsNot Available
KEGG Reactions
Adenosine triphosphate + tRNA(Trp) + L-Tryptophan → Adenosine monophosphate + Pyrophosphate + Trp-tRNA(Trp)
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00126L-TryptophanShow
YMDB00219PyrophosphateShow
GO Classification
Component
cell part
intracellular part
cytoplasm
Function
adenyl ribonucleotide binding
ATP binding
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-tRNA and related compounds
aminoacyl-tRNA ligase activity
catalytic activity
nucleotide binding
ligase activity
binding
nucleoside binding
purine nucleoside binding
tryptophan-tRNA ligase activity
adenyl nucleotide binding
Process
tryptophanyl-tRNA aminoacylation
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
Gene Properties
Chromosome Locationchromosome 4
LocusYDR268W
Gene Sequence>1140 bp ATGTCGAATAAGCAGGCGGTTCTGAAGTTAATCAGTAAAAGGTGGATAAGCACAGTGCAA CGTGCCGATTTTAAGCTGAATTCCGAAGCGCTTCATAGTAATGCTACGGTATTTAGTATG ATTCAGCCAACTGGGTGTTTCCACCTTGGTAATTATCTAGGTGCTACACGTGTTTGGACA GACTTATGTGAATTAAAACAACCTGGCCAGGAATTGATATTTGGAGTTGCTGATTTACAC GCTATCACTGTTCCAAAGCCAGATGGAGAAATGTTTAGAAAATTTCGCCATGAGGCAGTA GCAAGTATACTGGCTGTCGGTGTAGATCCAGAAAAGGCTTCGGTGATCTACCAATCCGCC ATCCCTCAACACAGTGAATTACACTGGTTGCTTTCTACTCTTGCCTCGATGGGATTACTT AACCGCATGACGCAATGGAAATCAAAATCGAATATCAAACAATCAACTAATGGGGATTAT CTGGTTAACGATTCTGACGTGGGAAAAGTTAGACTGGGCTTATTTTCGTATCCTGTTTTA CAGGCAGCGGATATTCTACTTTATAAATCTACACACGTTCCTGTTGGCGATGATCAATCG CAGCATTTGGAACTAACAAGACACCTTGCTGAAAAGTTTAACAAAATGTACAAGAAAAAT TTTTTTCCTAAACCTGTAACTATGTTGGCACAAACGAAAAAAGTTTTGAGCTTAAGCACG CCTGAAAAGAAAATGTCCAAGAGTGATCCGAATCACGACTCTGTAATTTTTTTGAATGAT GAGCCTAAGGCAATTCAGAAAAAGATTAGAAAAGCTTTAACAGATTCCATTTCTGATAGG TTCTACTACGACCCTGTAGAAAGACCAGGCGTATCGAATTTAATTAACATTGTCAGTGGC ATTCAAAGAAAATCGATTGAAGATGTCGTAGAAGATGTATCTCGTTTCAATAACTATAGG GATTTCAAAGATTATGTTTCAGAAGTGATAATTGAGGAATTGAAAGGCCCAAGAACAGAA TTTGAGAAATATATCAACGAACCGACCTATTTGCATAGTGTCGTTGAATCTGGCATGCGC AAAGCGAGAGAAAAAGCAGCAAAAAACCTGGCCGACATTCATAAAATAATGGGCTTCTGA
Protein Properties
Pfam Domain Function
Protein Residues379
Protein Molecular Weight43015.10156
Protein Theoretical pI9.63
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Tryptophanyl-tRNA synthetase, mitochondrial MSNKQAVLKLISKRWISTVQRADFKLNSEALHSNATVFSMIQPTGCFHLGNYLGATRVWT DLCELKQPGQELIFGVADLHAITVPKPDGEMFRKFRHEAVASILAVGVDPEKASVIYQSA IPQHSELHWLLSTLASMGLLNRMTQWKSKSNIKQSTNGDYLVNDSDVGKVRLGLFSYPVL QAADILLYKSTHVPVGDDQSQHLELTRHLAEKFNKMYKKNFFPKPVTMLAQTKKVLSLST PEKKMSKSDPNHDSVIFLNDEPKAIQKKIRKALTDSISDRFYYDPVERPGVSNLINIVSG IQRKSIEDVVEDVSRFNNYRDFKDYVSEVIIEELKGPRTEFEKYINEPTYLHSVVESGMR KAREKAAKNLADIHKIMGF
References
External Links
ResourceLink
Saccharomyces Genome Database MSW1
Uniprot IDP04803
Uniprot NameSYWM_YEAST
GenBank Gene IDU51030
Genebank Protein ID1230641
General Reference
  • Myers, A. M., Tzagoloff, A. (1985). "MSW, a yeast gene coding for mitochondrial tryptophanyl-tRNA synthetase." J Biol Chem 260:15371-15377.2999114
  • Entrup, R., Langgut, W., Lisowsky, T., Schweizer, E. (1992). "An yeast nuclear mutation conferring temperature-sensitivity to the mitochondrial tryptophanyl-tRNA synthetase." Curr Genet 21:281-283.1525855
  • 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
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278
  • Reinders, J., Zahedi, R. P., Pfanner, N., Meisinger, C., Sickmann, A. (2006). "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics." J Proteome Res 5:1543-1554.16823961