Identification
NameTyrosyl-tRNA synthetase, mitochondrial
Synonyms
  • Tyrosine--tRNA ligase
  • TyrRS
Gene NameMSY1
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionCatalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr)
Cellular LocationMitochondrion matrix
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
L-Tyrosine + Adenosine triphosphate + tRNA(Tyr) → Adenosine monophosphate + Pyrophosphate + Tyr-tRNA(Tyr)
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00364L-TyrosineShow
GO Classification
Component
intracellular part
cytoplasm
cell part
Function
binding
nucleoside binding
purine nucleoside binding
tyrosine-tRNA ligase activity
adenyl nucleotide binding
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
Process
biosynthetic process
tRNA metabolic process
tRNA aminoacylation
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
tyrosyl-tRNA aminoacylation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
RNA metabolic process
ncRNA metabolic process
Gene Properties
Chromosome Locationchromosome 16
LocusYPL097W
Gene Sequence>1479 bp ATGCTCGAATTACGAAGTTGTAGTAATTTGGTCAATAGTAGTAGGAGACTTGTGCCTCTG GTGACTTATTCCGGACTAAGTGCAATAACATTGCCTAAATCTCGATTTTATTCACAGCCT AGTGCTTTAGAAGTACAGGGCACATCGGATTCTCGAAGCGATAATATTTTAGACGAACTC AAACAAAGGGGTCTAGTGTCCCAGGTCTCACAGCCAGAGAGTTTCCTTCGGACGAAGTTG AACGGTAACGATAAGATCAAATTATACTGCGGGGTGGATCCCACAGCTCAGTCACTTCAT TTGGGAAATCTAGTTCCACTAATGGTTTTATTACACTTTTACGTAAAAGGTCACGACATT GTCACTGTGATAGGTGGAGCTACAGGGAAAGTTGGGGACCCAAGTGGTAGGAAAACAGAA AGAGACGTTATGGAGAACGATATTAGGCAAAGCAATGTGGCATCCATCTCGCAGCAATTA CAAAGGTTTTTCAAAAATGGCCTAGAATATTACAGAAACCGATGTGCTCTCACTGAAGAT GTACCTTCCGGAAAATATACACCAAGGAATAATTTCAACTGGTGGAAAGACATCAAAATG TTGGATTTCTTAGCTGATTTTGGTAGGCACATTCGGGTACAATCTATGTTGGCGAGGGAT TCAATTTCTTCGAGGCTTCAAACCAAAAATGGTCTGGGATTTAACGAATTTACTTACCAA GTTTTACAAGCGTACGATTTTTACCATTTGTATAAGGAAGAGAATGTGACTATACAAGTA GGTGGTAACGACCAATGGGGAAATATAACAGCCGGTATCGATCTCATCAATAGGATACAG CCTATAAAGAATAAGGGTTTGCCATTTGGTATCACTGTGCCCTTGTTGACGACGGCTACA GGAGAGAAATTTGGGAAAAGTGCAGGCAATGCTGTTTTTATTGACCCCTCAATCAATACG GCGTATGATGTTTACCAGTTCTTTTATAATACTTTGGATGCTGATGTACCCAAGTTCTTG AAGATCTTTACGTTTTTAAACTCAAGTGAAATCAAAAAAATTGTGGAAACGCATATCAAA TCACCCAGTCTACGTTATGGCCAAACTTTATTGGCTAAAGAAGTCACAGATATGTTATAT GGAGTTGGCTCCGGATCGGATTCAGAAGCGCTTTCTAATATTATTTTTGGACGTTATGAC GGAACTTTATCTGCTGCGAAGTTAGTTGATCTATGTAAAAAAGCCAGAATTTTGCAGTAT GCTGATAGAGAGATTGACTTAATAAAGTTAATTTGTAAACTAGTAAATTGTTCAGTATCA GAAGCCAGAAGAAAACTTTCCCAGGGAAGCGTGTATCTGCATCATTCAAAATCTAAAGTA AACGAAAATATTTCTAACTTGGCTCCTTTCCTGATAGATGATCGAGTACTGATCTTGAGG ATAGGAAAGCAGAAGTGTTTTATAATAGAAATGCGTTAA
Protein Properties
Pfam Domain Function
Protein Residues492
Protein Molecular Weight55286.89844
Protein Theoretical pI9.52
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Tyrosyl-tRNA synthetase, mitochondrial MLELRSCSNLVNSSRRLVPLVTYSGLSAITLPKSRFYSQPSALEVQGTSDSRSDNILDEL KQRGLVSQVSQPESFLRTKLNGNDKIKLYCGVDPTAQSLHLGNLVPLMVLLHFYVKGHDI VTVIGGATGKVGDPSGRKTERDVMENDIRQSNVASISQQLQRFFKNGLEYYRNRCALTED VPSGKYTPRNNFNWWKDIKMLDFLADFGRHIRVQSMLARDSISSRLQTKNGLGFNEFTYQ VLQAYDFYHLYKEENVTIQVGGNDQWGNITAGIDLINRIQPIKNKGLPFGITVPLLTTAT GEKFGKSAGNAVFIDPSINTAYDVYQFFYNTLDADVPKFLKIFTFLNSSEIKKIVETHIK SPSLRYGQTLLAKEVTDMLYGVGSGSDSEALSNIIFGRYDGTLSAAKLVDLCKKARILQY ADREIDLIKLICKLVNCSVSEARRKLSQGSVYLHHSKSKVNENISNLAPFLIDDRVLILR IGKQKCFIIEMR
References
External Links
ResourceLink
Saccharomyces Genome Database MSY1
Uniprot IDP48527
Uniprot NameSYYM_YEAST
GenBank Gene IDL42333
Genebank Protein ID825503
General Reference
  • Bussey, H., Storms, R. K., Ahmed, A., Albermann, K., Allen, E., Ansorge, W., Araujo, R., Aparicio, A., Barrell, B., Badcock, K., Benes, V., Botstein, D., Bowman, S., Bruckner, M., Carpenter, J., Cherry, J. M., Chung, E., Churcher, C., Coster, F., Davis, K., Davis, R. W., Dietrich, F. S., Delius, H., DiPaolo, T., Hani, J., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Nature 387:103-105.9169875
  • 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