ferredoxin-fold anticodon-binding domain-containing protein 1 contains a DUF2431 domain that belongs to the class I SAM-dependent methyltransferase superfamily
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
7-171
1.38e-58
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.
:
Pssm-ID: 463056 Cd Length: 162 Bit Score: 193.52 E-value: 1.38e-58
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
7-171
1.38e-58
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.
Pssm-ID: 463056 Cd Length: 162 Bit Score: 193.52 E-value: 1.38e-58
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
482-614
4.02e-23
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 129561 [Multi-domain] Cd Length: 460 Bit Score: 102.85 E-value: 4.02e-23
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
523-617
1.02e-20
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).
Pssm-ID: 214893 [Multi-domain] Cd Length: 93 Bit Score: 87.10 E-value: 1.02e-20
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
523-617
1.50e-16
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold.
Pssm-ID: 460826 [Multi-domain] Cd Length: 94 Bit Score: 75.21 E-value: 1.50e-16
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
512-617
2.22e-03
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439842 [Multi-domain] Cd Length: 793 Bit Score: 40.92 E-value: 2.22e-03
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
7-171
1.38e-58
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.
Pssm-ID: 463056 Cd Length: 162 Bit Score: 193.52 E-value: 1.38e-58
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
482-614
4.02e-23
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 129561 [Multi-domain] Cd Length: 460 Bit Score: 102.85 E-value: 4.02e-23
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
523-617
1.02e-20
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).
Pssm-ID: 214893 [Multi-domain] Cd Length: 93 Bit Score: 87.10 E-value: 1.02e-20
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
523-617
1.50e-16
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold.
Pssm-ID: 460826 [Multi-domain] Cd Length: 94 Bit Score: 75.21 E-value: 1.50e-16
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
512-617
2.22e-03
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439842 [Multi-domain] Cd Length: 793 Bit Score: 40.92 E-value: 2.22e-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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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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the domain superfamily to which the specific and non-specific hits belong
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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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