Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
1-331
0e+00
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
The actual alignment was detected with superfamily member TIGR00669:
Pssm-ID: 444800 Cd Length: 330 Bit Score: 513.30 E-value: 0e+00
aspartate--ammonia ligase, AsnA-type; This model represents one of two non-homologous forms of ...
1-331
0e+00
aspartate--ammonia ligase, AsnA-type; This model represents one of two non-homologous forms of aspartate--ammonia ligase (asparagine synthetase) found in E. coli. This type is also found in Haemophilus influenzae, Treponema pallidum and Lactobacillus delbrueckii, but appears to have a very limited distribution. The fact that the protein from the H. influenzae is more than 70 % identical to that from the spirochete Treponema pallidum, but less than 65 % identical to that from the closely related E. coli, strongly suggests lateral transfer. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129752 Cd Length: 330 Bit Score: 513.30 E-value: 0e+00
Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of ...
9-321
2.78e-178
Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. AsnA is a homodimeric enzyme which is structurally similiar to the catalytic core domain of class II aminoacyl-tRNA synthetases. Ammonia-dependent AsnA is not homologous to the glutamine-dependent asparagine synthetase AsnB.
Pssm-ID: 238350 Cd Length: 309 Bit Score: 495.32 E-value: 2.78e-178
aspartate--ammonia ligase, AsnA-type; This model represents one of two non-homologous forms of ...
1-331
0e+00
aspartate--ammonia ligase, AsnA-type; This model represents one of two non-homologous forms of aspartate--ammonia ligase (asparagine synthetase) found in E. coli. This type is also found in Haemophilus influenzae, Treponema pallidum and Lactobacillus delbrueckii, but appears to have a very limited distribution. The fact that the protein from the H. influenzae is more than 70 % identical to that from the spirochete Treponema pallidum, but less than 65 % identical to that from the closely related E. coli, strongly suggests lateral transfer. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129752 Cd Length: 330 Bit Score: 513.30 E-value: 0e+00
Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of ...
9-321
2.78e-178
Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. AsnA is a homodimeric enzyme which is structurally similiar to the catalytic core domain of class II aminoacyl-tRNA synthetases. Ammonia-dependent AsnA is not homologous to the glutamine-dependent asparagine synthetase AsnB.
Pssm-ID: 238350 Cd Length: 309 Bit Score: 495.32 E-value: 2.78e-178
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
11-301
9.91e-27
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 104.89 E-value: 9.91e-27
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
241-314
3.65e-03
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 38.61 E-value: 3.65e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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