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InterPro: IPR004524 Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type
Protein matches
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UniProtKB Matches: 1712 proteins |
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Accession
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IPR004524 Asp-tRNA-synth_IIb_bac/mt |
Type
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Family |
Signatures
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InterPro Relationships
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Children
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IPR020564 Aspartyl-tRNA synthetase, class IIb, bacterial-type
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Contains
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IPR002312 Aspartyl-tRNA synthetase, class IIb
IPR004115 GAD domain
IPR004364 Aminoacyl-tRNA synthetase, class II (D/K/N)
IPR004365 Nucleic acid binding, OB-fold, tRNA/helicase-type
IPR006195 Aminoacyl-tRNA synthetase, class II, conserved region
IPR012340 Nucleic acid-binding, OB-fold
IPR016027 Nucleic acid-binding, OB-fold-like
IPR018150 Aminoacyl-tRNA synthetase, class II (D/K/N)-like
IPR018153 Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type, C-terminal
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GO Term annotation
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Process
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GO:0006412 translation
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Function
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GO:0005524 ATP binding
GO:0016874 ligase activity
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Component
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GO:0005737 cytoplasm
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The aminoacyl-tRNA synthetases (EC:6.1.1.) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology [1]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [2]. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [3], and are mostly dimeric or multimeric, containing at least three conserved regions [4, 5, 6]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases; these synthetases are further divided into three subclasses, a, b and c, according to sequence homology. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases [7]. Aspartyl tRNA synthetase EC:6.1.1.12 is an alpha2 dimer that belongs to class IIb. Structural analysis combined with mutagenesis and enzymology data on the yeast enzyme point to a tRNA binding process that starts by a recognition event between the tRNA anticodon loop and the synthetase anticodon binding module [8].
This family represents aspartyl-tRNA synthetases from the bacteria, plants, metazoa and fungi, including mitochondrial forms of the enzyme. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn).
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Structural links
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Database links
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Example proteins
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P15179 Aspartyl-tRNA synthetase, mitochondrial
P21889 Aspartyl-tRNA synthetase
P73851 Aspartyl-tRNA synthetase
Q6PI48 Aspartyl-tRNA synthetase, mitochondrial
Q8BIP0 Aspartyl-tRNA synthetase, mitochondrial
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR020564 |
Aspartyl-tRNA synthetase, class IIb, bacterial-type |
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| IPR004115 |
GAD domain |
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| IPR016027 |
Nucleic acid-binding, OB-fold-like |
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| IPR012340 |
Nucleic acid-binding, OB-fold |
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| IPR002312 |
Aspartyl-tRNA synthetase, class IIb |
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| IPR004524 |
Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type |
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| IPR018153 |
Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type, C-terminal |
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| IPR018150 |
Aminoacyl-tRNA synthetase, class II (D/K/N)-like |
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| IPR004365 |
Nucleic acid binding, OB-fold, tRNA/helicase-type |
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| IPR006195 |
Aminoacyl-tRNA synthetase, class II, conserved region |
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| IPR004364 |
Aminoacyl-tRNA synthetase, class II (D/K/N) |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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Publications
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1.
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Eriani G, Delarue M, Poch O, Gangloff J, Moras D.
Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs.
Nature 347 203-6 1990
[PubMed: 2203971]
http://dx.doi.org/10.1038/347203a0
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2.
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Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A, Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M.
The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.
Structure 8 197-208 2000
[PubMed: 10673435]
http://dx.doi.org/10.1016/S0969-2126(00)00095-2
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3.
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Perona JJ, Rould MA, Steitz TA.
Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.
Biochemistry 32 8758-71 1993
[PubMed: 8364025]
http://dx.doi.org/10.1021/bi00085a006
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4.
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Delarue M, Moras D.
The aminoacyl-tRNA synthetase family: modules at work.
Bioessays 15 675-87 1993
[PubMed: 8274143]
http://dx.doi.org/10.1002/bies.950151007
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5.
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Schimmel P.
Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code.
Trends Biochem. Sci. 16 1-3 1991
[PubMed: 2053131]
http://dx.doi.org/10.1016/0968-0004(91)90002-D
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6.
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Cusack S, Hartlein M, Leberman R.
Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.
Nucleic Acids Res. 19 3489-98 1991
[PubMed: 1852601]
http://dx.doi.org/10.1093/nar/19.13.3489
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7.
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Bairoch A.
List of aminoacyl-tRNA synthetases.
2004
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8.
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Sauter C, Lorber B, Cavarelli J, Moras D, Giege R.
The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain.
J. Mol. Biol. 299 1313-24 2000
[PubMed: 10873455]
http://dx.doi.org/10.1006/jmbi.2000.3791
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Additional Reading
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Eiler S, Dock-Bregeon A, Moulinier L, Thierry JC, Moras D.
Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.
EMBO J. 18 1999 6532-41
[PubMed: 10562565]
http://dx.doi.org/10.1093/emboj/18.22.6532
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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. 299 2000 1051-60
[PubMed: 10843857]
http://dx.doi.org/10.1006/jmbi.2000.3819
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Rees B, Webster G, Delarue M, Boeglin M, Moras D.
Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates.
J. Mol. Biol. 299 2000 1157-64
[PubMed: 10873442]
http://dx.doi.org/10.1006/jmbi.2000.3792
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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. 58 2002 645-52
[PubMed: 11914489]
http://dx.doi.org/10.1107/S0907444902003177
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Moulinier L, Eiler S, Eriani G, Gangloff J, Thierry JC, Gabriel K, McClain WH, Moras D.
The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.
EMBO J. 20 2001 5290-301
[PubMed: 11566892]
http://dx.doi.org/10.1093/emboj/20.18.5290
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