Aspartate--tRNA(Asp) ligase
Details
- Name
- Aspartate--tRNA(Asp) ligase
- Kind
- protein
- Synonyms
- 6.1.1.12
- Aspartyl-tRNA synthetase
- AspRS
- D-AspRS
- Discriminating aspartyl-tRNA synthetase
- Gene Name
- aspS
- UniProtKB Entry
- P36419Swiss-Prot
- Organism
- Thermus thermophilus
- NCBI Taxonomy ID
- 274
- Amino acid sequence
>lcl|BSEQ0019098|Aspartate--tRNA(Asp) ligase MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPASPAYATA ERVRPEWVVRAKGLVRLRPEPNPRLATGRVEVELSALEVLAEAKTPPFPVDAGWRGEEEK EASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWDFLDREGFVQVETPFLTKSTPEGAR DFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDL EMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELK EVGPLFRQSGFRVFQEAESVKALALPKALSRKEVAELEEVAKRHKAQGLAWARVEEGGFS GGVAKFLEPVREALLQATEARPGDTLLFVAGPRKVAATALGAVRLRAADLLGLKREGFRF LWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLPLLEKDPGRVRALAYDLVLNGVEVGGG SIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSP SIREVIAFPKNKEGKDPLTGAPSPVPEEQLRELGLMVVRP
- Number of residues
- 580
- Molecular Weight
- 66029.175
- Theoretical pI
- 5.89
- GO Classification
- Functionsaspartate-tRNA ligase activity / ATP binding / nucleic acid bindingProcessestRNA aminoacylation for protein translationComponentscytoplasm
- General Function
- Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
- Specific Function
- aspartate-tRNA ligase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0002631|1743 bp ATGCGTCGCACCCACTACGCCGGAAGCCTGAGGGAAACCCACGTGGGCGAGGAGGTGGTC CTCGAGGGCTGGGTCAACCGCCGCCGCGACCTCGGCGGCCTCATCTTCCTGGACCTCAGG GACCGGGAGGGCCTGGTCCAGCTCGTGGCCCACCCCGCTAGCCCCGCCTACGCCACCGCC GAACGGGTGCGCCCCGAGTGGGTGGTGCGGGCCAAAGGCCTCGTGCGCCTCCGCCCCGAG CCCAACCCCCGCCTCGCCACGGGGCGGGTGGAGGTGGAGCTCTCTGCCCTCGAGGTCCTC GCCGAGGCCAAGACGCCCCCCTTCCCCGTGGACGCGGGCTGGCGGGGGGAGGAGGAGAAG GAGGCAAGTGAGGAGCTCCGCCTCAAGTACCGCTACCTGGACCTAAGAAGGCGGCGCATG CAGGAGAACCTGCGCCTGCGCCACCGGGTCATCAAGGCCATCTGGGACTTCCTGGACCGG GAGGGCTTCGTCCAGGTGGAAACCCCCTTTCTCACCAAAAGCACCCCGGAAGGGGCCCGG GACTTCCTGGTGCCCTACCGCCACGAGCCCGGCCTCTTCTACGCCCTGCCCCAGTCCCCC CAGCTCTTCAAGCAGATGCTGATGGTGGCGGGGCTGGACCGCTACTTCCAGATCGCCCGC TGCTTCCGGGACGAGGACCTCCGCGCCGACCGCCAGCCCGACTTCACCCAGCTGGACCTG GAGATGAGCTTCGTGGAGGTGGAGGACGTCCTGGAACTCAACGAGCGCCTCATGGCCCAC GTCTTCCGCGAGGCGTTGGGGGTGGAGCTTCCCCTCCCCTTCCCCCGGCTTTCCTACGAG GAGGCCATGGAGCGCTACGGCTCCGACAAGCCCGACCTCCGCTTCGGCCTGGAGCTCAAG GAGGTGGGCCCCCTCTTCCGCCAAAGCGGCTTCAGGGTCTTCCAGGAGGCGGAAAGCGTG AAGGCCCTTGCCCTCCCCAAGGCCCTCTCCCGCAAGGAGGTCGCCGAGCTGGAGGAGGTG GCCAAGCGCCACAAGGCCCAGGGCCTCGCCTGGGCCCGGGTGGAGGAGGGGGGGTTTTCC GGGGGTGTGGCCAAGTTTTTAGAACCCGTGCGGGAAGCTCTGCTCCAAGCCACGGAGGCC AGGCCCGGGGACACCCTCCTCTTCGTGGCGGGGCCCCGCAAGGTGGCGGCCACGGCCCTG GGGGCGGTGCGGCTTAGGGCGGCGGACCTTTTGGGCCTCAAGCGGGAGGGCTTCCGCTTC CTCTGGGTGGTGGACTTTCCCCTTTTGGAGTGGGACGAGGAGGAGGAGGCCTGGACCTAC ATGCACCACCCCTTCACGAGCCCCCACCCCGAGGACCTGCCCCTCCTGGAAAAGGACCCG GGGAGGGTGCGGGCCTTGGCCTACGACCTCGTCCTCAACGGGGTGGAGGTGGGCGGGGGG TCCATCCGCATCCACGACCCCAGGCTCCAGGCCCGGGTCTTCCGGCTTCTCGGCATCGGC GAGGAGGAGCAAAGGGAGAAGTTCGGGTTCTTCCTCGAGGCCCTGGAGTACGGGGCCCCG CCCCACGGGGGGATCGCCTGGGGGCTGGACCGCCTCCTCGCCCTCATGACGGGAAGCCCC TCCATCCGCGAGGTCATCGCCTTCCCCAAGAACAAGGAAGGCAAGGACCCCCTGACCGGC GCCCCGAGCCCCGTGCCCGAGGAGCAGCTTAGGGAGCTCGGCCTCATGGTGGTCCGGCCA TGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P36419 UniProtKB Entry Name SYD_THETH GenBank Protein ID 396501 GenBank Gene ID X70943 PDB ID(s) 1EFW, 1G51, 1L0W - General References
- Poterszman A, Plateau P, Moras D, Blanquet S, Mazauric MH, Kreutzer R, Kern D: Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases. FEBS Lett. 1993 Jul 5;325(3):183-6. [Article]
- Delarue M, Poterszman A, Nikonov S, Garber M, Moras D, Thierry JC: Crystal structure of a prokaryotic aspartyl tRNA-synthetase. EMBO J. 1994 Jul 15;13(14):3219-29. [Article]
- Poterszman A, Delarue M, Thierry JC, Moras D: Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase. J Mol Biol. 1994 Nov 25;244(2):158-67. [Article]
- Briand C, Poterszman A, Eiler S, Webster G, Thierry J, Moras D: An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase. J Mol Biol. 2000 Jun 16;299(4):1051-60. [Article]
- Ng JD, Sauter C, Lorber B, Kirkland N, Arnez J, Giege R: Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):645-52. Epub 2002 Mar 22. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Aspartyl-Adenosine-5'-Monophosphate experimental unknown target Details