Aspartate--tRNA(Asp) ligase

Details

Name

Aspartate--tRNA(Asp) ligase

Synonyms

• 6.1.1.12
• Aspartyl-tRNA synthetase
• AspRS
• D-AspRS
• Discriminating aspartyl-tRNA synthetase

Gene Name

aspS

Organism

Thermus thermophilus

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

Functions

aspartate-tRNA ligase activity / ATP binding / nucleic acid binding

Processes

tRNA aminoacylation for protein translation

Components

cytoplasm

General Function

Nucleic acid binding

Specific Function

Catalyzes the attachment of glutamate to tRNA(Asp) in a two-step reaction: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).

Pfam Domain Function

• tRNA-synt_2 (PF00152)
• tRNA_anti-codon (PF01336)
• GAD (PF02938)

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

General References

1. 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]
2. 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]
3. 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]
4. 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]
5. 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]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB01895	Aspartyl-Adenosine-5'-Monophosphate	experimental	unknown		Details