Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB is part of a heterotrimeric complex that forms correctly charged Gln-tRNA(Gln) or Asn-tRNA(Asn) through the transamidation of misacylated Glu-tRNA(Gln) or Asp-tRNA(Asn)
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and ...
62-556
0e+00
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
:
Pssm-ID: 439834 [Multi-domain] Cd Length: 477 Bit Score: 619.35 E-value: 0e+00
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and ...
62-556
0e+00
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439834 [Multi-domain] Cd Length: 477 Bit Score: 619.35 E-value: 0e+00
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is ...
64-556
2.55e-158
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is responsible for transferring the NH2 group that converts Glu to Gln, or Asp to Asn after the Glu or Asp has been ligated to the tRNA for Gln or Asn, respectively. In Lactobacillus, GatABC is responsible only for tRNA(Gln). In the Archaea, GatABC is responsible only for tRNA(Asn), while GatDE is responsible for tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyzes both. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272926 [Multi-domain] Cd Length: 478 Bit Score: 460.34 E-value: 2.55e-158
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about ...
407-555
9.55e-48
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB which transamidates Glu-tRNA to Gln-tRNA. The function of this domain is uncertain. It does however suggest that Yqey and its relatives have a role in tRNA metabolism.
Pssm-ID: 197913 [Multi-domain] Cd Length: 147 Bit Score: 163.06 E-value: 9.55e-48
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and ...
62-556
0e+00
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439834 [Multi-domain] Cd Length: 477 Bit Score: 619.35 E-value: 0e+00
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is ...
64-556
2.55e-158
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is responsible for transferring the NH2 group that converts Glu to Gln, or Asp to Asn after the Glu or Asp has been ligated to the tRNA for Gln or Asn, respectively. In Lactobacillus, GatABC is responsible only for tRNA(Gln). In the Archaea, GatABC is responsible only for tRNA(Asn), while GatDE is responsible for tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyzes both. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272926 [Multi-domain] Cd Length: 478 Bit Score: 460.34 E-value: 2.55e-158
GatB domain; This domain is found in GatB. It is about 140 amino acid residues long. This ...
406-555
1.58e-53
GatB domain; This domain is found in GatB. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB, which transamidates Glu-tRNA to Gln-tRNA.
Pssm-ID: 396969 [Multi-domain] Cd Length: 148 Bit Score: 178.52 E-value: 1.58e-53
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about ...
407-555
9.55e-48
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB which transamidates Glu-tRNA to Gln-tRNA. The function of this domain is uncertain. It does however suggest that Yqey and its relatives have a role in tRNA metabolism.
Pssm-ID: 197913 [Multi-domain] Cd Length: 147 Bit Score: 163.06 E-value: 9.55e-48
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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