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| Identification |
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| Name | Threonyl-tRNA synthetase, cytoplasmic |
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| Synonyms | - Threonine--tRNA ligase
- ThrRS
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| Gene Name | THS1 |
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| Enzyme Class | |
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| Biological Properties |
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| General Function | Involved in nucleotide binding |
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| Specific Function | ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) |
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| Cellular Location | Cytoplasm |
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| SMPDB Pathways | Not Available |
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| KEGG Pathways | Not Available |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00097 | Adenosine monophosphate | Show | | YMDB00109 | Adenosine triphosphate | Show | | YMDB00214 | L-Threonine | Show | | YMDB00219 | Pyrophosphate | Show |
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| GO Classification | | Component |
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| cell part | | intracellular part | | cytoplasm | | Function |
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| nucleoside binding | | purine nucleoside binding | | adenyl nucleotide binding | | threonine-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 | | Process |
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| cellular macromolecule biosynthetic process | | translation | | threonyl-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 |
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| Gene Properties |
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| Chromosome Location | chromosome 9 |
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| Locus | YIL078W |
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| Gene Sequence | >2205 bp
ATGAGTGCTAGTGAAGCAGGTGTCGCTGAGCAAGTCAAAAAGCTGTCTGTCAACGATAGT
AGTAATGATGCCGTAAAACCAAATAAGAAAGAAAACAAAAAATCCAAGCAACAGTCCTTG
TACTTGGATCCTGAACCAACTTTCATCGAGGAAAGAATTGAAATGTTTGACAGATTACAA
AAGGAATACAATGATAAAGTTGCTTCTATGCCACGTGTTCCATTGAAGATTGTCTTGAAG
GATGGAGCCGTTAAGGAAGCCACTTCTTGGGAAACCACTCCGATGGATATTGCCAAAGGA
ATTTCTAAATCTTTAGCAGACAGGTTATGTATTTCTAAGGTTAATGGTCAATTATGGGAC
TTAGATAGACCATTTGAAGGCGAAGCCAACGAAGAAATCAAATTAGAACTGCTAGATTTC
GAATCTGACGAAGGTAAGAAGGTCTTTTGGCATTCGTCTGCCCACGTCTTGGGTGAATCT
TGTGAGTGCCACCTAGGTGCCCATATTTGTTTAGGTCCTCCAACTGATGATGGGTTCTTT
TATGAAATGGCTGTTAGAGATAGTATGAAAGATATATCTGAATCTCCAGAAAGAACCGTC
TCCCAAGCTGATTTCCCAGGATTAGAAGGCGTTGCCAAGAATGTTATCAAGCAAAAGCAA
AAATTTGAAAGATTGGTCATGTCCAAAGAAGATCTTTTGAAAATGTTTCATTATTCGAAG
TATAAGACTTACTTGGTACAGACAAAGGTTCCAGATGGAGGTGCTACTACCGTCTACCGT
TGCGGTAAATTGATTGATCTTTGTGTCGGCCCTCATATCCCACATACTGGGCGTATCAAA
GCTTTCAAACTATTAAAGAACTCTTCTTGTTATTTCTTAGGTGATGCGACAAACGACTCT
TTACAAAGAGTTTACGGTATCTCTTTTCCAGACAAAAAATTAATGGATGCTCATTTGAAG
TTCTTGGCGGAAGCCTCTATGAGAGATCACAGAAAGATTGGTAAAGAACAAGAATTATTC
TTATTCAATGAAATGTCCCCAGGTTCTTGCTTTTGGTTACCTCATGGTACTAGAATTTAC
AACACTTTGGTTGACTTGTTGAGAACTGAATACCGTAAGAGAGGTTACGAAGAAGTCATC
ACTCCAAACATGTACAACTCCAAATTGTGGGAAACCTCAGGTCACTGGGCCAATTACAAG
GAAAACATGTTTACTTTCGAAGTAGAGAAGGAAACTTTCGGTCTAAAACCAATGAACTGT
CCAGGTCATTGTTTGATGTTCAAGTCTAGAGAACGTTCTTATAGAGAATTGCCATGGAGA
GTTGCAGACTTCGGTGTTATCCACAGAAATGAATTTTCTGGTGCCTTGTCTGGTTTGACT
CGTGTCAGAAGATTCCAACAAGATGATGCTCATATCTTCTGTACCCATGACCAAATTGAA
TCTGAAATTGAAAACATTTTCAACTTTTTGCAATACATTTACGGCGTTTTTGGATTTGAA
TTTGAAATGGAATTGTCCACTAGACCAGAAAAGTACGTTGGAAAGATCGAAACCTGGGAT
GCCGCTGAATCAAAATTAGAATCTGCCTTAAAGAAATGGGGTGGTAACTGGGAGATCAAT
GCTGGTGATGGTGCTTTCTACGGTCCAAAGATTGACATTATGATTTCTGACGCTTTAAGA
AGATGGCATCAATGTGCCACCATCCAATTAGATTTCCAATTGCCAAACAGGTTCGAATTG
GAATTTAAATCTAAAGATCAAGATAGCGAGAGTTACGAAAGACCGGTCATGATCCATCGT
GCCATTTTAGGGTCTGTTGAAAGAATGACTGCCATTTTGACCGAGCATTTTGCTGGTAAA
TGGCCATTTTGGTTATCACCACGTCAAGTTTTGGTTGTACCAGTTGGTGTCAAGTACCAA
GGGTATGCTGAAGACGTCCGTAACAAATTGCACGATGCTGGCTTCTATGCCGATGTCGAT
TTGACTGGTAACACTCTGCAAAAGAAGGTCAGAAACGGGCAAATGCTAAAATATAACTTC
ATTTTTATTGTTGGTGAACAAGAAATGAATGAAAAATCTGTTAACATTAGAAACAGAGAC
GTTATGGAACAACAGGGTAAAAATGCTACTGTTTCTGTTGAAGAGGTTTTGAAACAGTTG
CGTAACTTGAAAGATGAAAAGAGAGGTGACAACGTCTTAGCTTAA |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 734 |
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| Protein Molecular Weight | 84519.79688 |
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| Protein Theoretical pI | 7.03 |
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| Signalling Regions | |
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| Transmembrane Regions | |
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| Protein Sequence | >Threonyl-tRNA synthetase, cytoplasmic
MSASEAGVTEQVKKLSVKDSSNDAVKPNKKENKKSKQQSLYLDPEPTFIEERIEMFDRLQ
KEYNDKVASMPRVPLKIVLKDGAVKEATSWETTPMDIAKGISKSLADRLCISKVNGQLWD
LDRPFEGEANEEIKLELLDFESDEGKKVFWHSSAHVLGESCECHLGAHICLGPPTDDGFF
YEMAVRDSMKDISESPERTVSQADFPGLEGVAKNVIKQKQKFERLVMSKEDLLKMFHYSK
YKTYLVQTKVPDGGATTVYRCGKLIDLCVGPHIPHTGRIKAFKLLKNSSCYFLGDATNDS
LQRVYGISFPDKKLMDAHLKFLAEASMRDHRKIGKEQELFLFNEMSPGSCFWLPHGTRIY
NTLVDLLRTEYRKRGYEEVITPNMYNSKLWETSGHWANYKENMFTFEVEKETFGLKPMNC
PGHCLMFKSRERSYRELPWRVADFGVIHRNEFSGALSGLTRVRRFQQDDAHIFCTHDQIE
SEIENIFNFLQYIYGVFGFEFKMELSTRPEKYVGKIETWDAAESKLESALKKWGGNWEIN
AGDGAFYGPKIDIMISDALRRWHQCATIQLDFQLPNRFELEFKSKDQDSESYERPVMIHR
AILGSVERMTAILTEHFAGKWPFWLSPRQVLVVPVGVKYQGYAEDVRNKLHDAGFYADVD
LTGNTLQKKVRNGQMLKYNFIFIVGEQEMNEKSVNIRNRDVMEQQGKNATVSVEEVLKQL
RNLKDEKRGDNVLA |
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| References |
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| External Links | |
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| General Reference | - Pape, L. K., Tzagoloff, A. (1985). "Cloning and characterization of the gene for the yeast cytoplasmic threonyl-tRNA synthetase." Nucleic Acids Res 13:6171-6183.2995918
- Churcher, C., Bowman, S., Badcock, K., Bankier, A., Brown, D., Chillingworth, T., Connor, R., Devlin, K., Gentles, S., Hamlin, N., Harris, D., Horsnell, T., Hunt, S., Jagels, K., Jones, M., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Rowley, N., Skelton, J., Smith, V., Barrell, B., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
- 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
- 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
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