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InterPro: IPR004524 Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type

Protein matchesHelp
UniProtKB
Matches:
1712 proteins
AccessionHelp IPR004524 Asp-tRNA-synth_IIb_bac/mt
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR020564 Aspartyl-tRNA synthetase, class IIb, bacterial-type
Contains 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
GO Term annotationHelp
Process GO:0006412 translation
Function GO:0005524 ATP binding
GO:0016874 ligase activity
Component GO:0005737 cytoplasm
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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).

Structural linksHelp
Database linksHelp
Enzyme: EC:6.1.1.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004524 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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
IPR004115 GAD domain
IPR016027 Nucleic acid-binding, OB-fold-like
IPR012340 Nucleic acid-binding, OB-fold
IPR002312 Aspartyl-tRNA synthetase, class IIb
IPR004524 Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type
IPR018153 Aspartyl-tRNA synthetase, class IIb, bacterial/mitochondrial type, C-terminal
IPR018150 Aminoacyl-tRNA synthetase, class II (D/K/N)-like
IPR004365 Nucleic acid binding, OB-fold, tRNA/helicase-type
IPR006195 Aminoacyl-tRNA synthetase, class II, conserved region
IPR004364 Aminoacyl-tRNA synthetase, class II (D/K/N)
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. 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
2. 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
3. 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
4. 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
5. 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
6. 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
7. Bairoch A.
List of aminoacyl-tRNA synthetases.
2004
8. 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

Additional ReadingHelp
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
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
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
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
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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InterPro 23.1