| Identification |
|---|
| Name | Seryl-tRNA synthetase, cytoplasmic |
|---|
| Synonyms | - Serine--tRNA ligase
- SerRS
- Seryl-tRNA(Ser/Sec) synthetase
|
|---|
| Gene Name | SES1 |
|---|
| Enzyme Class | |
|---|
| Biological Properties |
|---|
| General Function | Involved in nucleotide binding |
|---|
| Specific Function | Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) |
|---|
| Cellular Location | Cytoplasm |
|---|
| SMPDB Pathways | Not Available |
|---|
| KEGG Pathways | Not Available |
|---|
| SMPDB Reactions | Not Available |
|---|
| KEGG Reactions | |
|---|
| Metabolites | | YMDB ID | Name | View |
|---|
| YMDB00097 | Adenosine monophosphate | Show | | YMDB00109 | Adenosine triphosphate | Show | | YMDB00112 | L-Serine | Show | | YMDB00219 | Pyrophosphate | Show |
|
|---|
| 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 | | adenyl nucleotide binding | | serine-tRNA ligase activity | | Process |
|---|
| seryl-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 Location | chromosome 4 |
|---|
| Locus | YDR023W |
|---|
| Gene Sequence | >1389 bp
ATGTTGGACATCAACCAATTTATCGAAGATAAGGGTGGTAACCCAGAGCTAATCAGACAA
TCTCAGAAAGCAAGAAATGCCAGTGTTGAAATCGTCGATGAAATTATTTCCGACTACAAA
GATTGGGTCAAAACAAGATTCGAATTAGATGAATTGAACAAGAAATTCAACAAGCTTCAA
AAGGATATTGGTTTGAAGTTTAAAAACAAGGAAGACGCTTCCGGATTATTAGCCGAAAAA
GAGAAGTTAACCCAACAAAAGAAGGAATTGACTGAAAAGGAGCAACAGGAAGATAAGGAC
TTGAAGAAAAAAGTTTTTCAAGTAGGAAATATCGTTCATCCATCTGTTGTTGTTTCCAAC
GATGAAGAAAACAATGAATTGGTCCGTACTTGGAAACCAGAGGATTTAGAAGCGGTTGGC
CCCATTGCTTCTGTGACTGGTAAACCAGCTAGTTTATCCCATCATGAAATCTTGCTAAGA
TTAGATGGATATGATCCAGACCGTGGTGTAAAGATTTGTGGTCATAGAGGTTATTTCTTC
AGAAATTATGGTGTTTTCTTGAACCAAGCTTTGATTAACTATGGTTTACAGTTCTTAGCT
GCCAAGGGTTATATTCCTTTACAAGCTCCAGTCATGATGAATAAAGAACTTATGTCAAAA
ACTGCTCAACCATCTGAATTCGATGAAGAGTTATACAAAGTTATCGATGGTGAAGATGAA
AAATACCTAATTGCTACCTCAGAACAACCTATCTCCGCTTACCACAGCGGTGAATGGTTT
GAAAAGCCACAAGAGCAATTGCCAATTCACTATGTCGGTTACTCCTCTTGTTTCCGTAGA
GAAGCCGGTTCTCACGGTAAGGATGCTTGGGGTGTCTTCAGAGTTCATGCTTTCGAAAAA
ATTGAACAATTCGTCATCACTGAACCTGAAAAATCTTGGGAGGAGTTTGAAAAGATGATC
TCTTACTCTGAGGAATTTTATAAGTCTTTGAAATTACCATACCGTATCGTTGGTATCGTT
TCCGGTGAATTAAACAATGCTGCCGCTAAAAAGTACGATTTAGAAGCCTGGTTCCCATAC
CAAAAGGAGTACAAAGAACTCGTCTCTTGCTCCAATTGTACTGATTATCAGTCAAGAAAC
TTAGAAATTAGATGCGGTATAAAGAAAATGGGCGACAGAGAAAAGAAATACGTACACTGT
TTGAATTCCACTTTGGCTGCTACCCAAAGAGCTTTGTGCTGTATCTTGGAGAACTACCAA
ACGGAAGATGGTTTGGTTGTACCAGAAGTTTTGAGGAAATACATTCCAGGTGAACCAGAA
TTTTTACCATTCGTTAATGAATTACCAAAGAATTCCACCTCTAGTAAAGACAAGAAAAAG
AAGAATTAA |
|---|
| Protein Properties |
|---|
| Pfam Domain Function | |
|---|
| Protein Residues | 462 |
|---|
| Protein Molecular Weight | 53309.19922 |
|---|
| Protein Theoretical pI | 5.94 |
|---|
| Signalling Regions | |
|---|
| Transmembrane Regions | |
|---|
| Protein Sequence | >Seryl-tRNA synthetase, cytoplasmic
MLDINQFIEDKGGNPELIRQSQKARNASVEIVDEIISDYKDWVKTRFELDELNKKFNKLQ
KDIGLKFKNKEDASGLLAEKEKLTQQKKELTEKEQQEDKDLKKKVFQVGNIVHPSVVVSN
DEENNELVRTWKPEDLEAVGPIASVTGKPASLSHHEILLRLDGYDPDRGVKICGHRGYFF
RNYGVFLNQALINYGLQFLAAKGYIPLQAPVMMNKELMSKTAQLSEFDEELYKVIDGEDE
KYLIATSEQPISAYHSGEWFEKPQEQLPIHYVGYSSCFRREAGSHGKDAWGVFRVHAFEK
IEQFVITEPEKSWEEFEKMISYSEEFYKSLKLPYRIVGIVSGELNNAAAKKYDLEAWFPY
QKEYKELVSCSNCTDYQSRNLEIRCGIKKMGDREKKYVHCLNSTLAATQRALCCILENYQ
TEDGLVVPEVLRKYIPGEPEFLPFVNELPKNSTSSKDKKKKN |
|---|
| References |
|---|
| External Links | |
|---|
| General Reference | - Weygand-Durasevic, I., Johnson-Burke, D., Soll, D. (1987). "Cloning and characterization of the gene coding for cytoplasmic seryl-tRNA synthetase from Saccharomyces cerevisiae." Nucleic Acids Res 15:1887-1904.3031581
- Eide, L. G., Sander, C., Prydz, H. (1996). "Sequencing and analysis of a 35.4 kb region on the right [corrected] arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames." Yeast 12:1085-1090.8896275
- 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
- Folley, L. S., Fox, T. D. (1994). "Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae." Genetics 137:369-379.8070651
- 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
|
|---|