Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; ...
48-334
8.62e-52
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Ts is part of the Pathway/BioSystem: Translation factors
The actual alignment was detected with superfamily member COG0264:
Pssm-ID: 440034 [Multi-domain] Cd Length: 290 Bit Score: 173.34 E-value: 8.62e-52
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; ...
48-334
8.62e-52
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Ts is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440034 [Multi-domain] Cd Length: 290 Bit Score: 173.34 E-value: 8.62e-52
translation elongation factor Ts; Translational elongation factor Ts (EF-Ts) catalyzes the exchange of GTP for the GDP of the EF-Tu.GDP complex as part of the cycle of translation elongation. This protein is found in Bacteria, mitochondria, and chloroplasts. [Protein synthesis, Translation factors]
Pssm-ID: 272914 [Multi-domain] Cd Length: 291 Bit Score: 129.90 E-value: 3.77e-35
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria ...
48-84
2.60e-14
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria of eukaryotes; EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains.
Pssm-ID: 270461 [Multi-domain] Cd Length: 37 Bit Score: 65.88 E-value: 2.60e-14
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; ...
48-334
8.62e-52
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Ts is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440034 [Multi-domain] Cd Length: 290 Bit Score: 173.34 E-value: 8.62e-52
translation elongation factor Ts; Translational elongation factor Ts (EF-Ts) catalyzes the exchange of GTP for the GDP of the EF-Tu.GDP complex as part of the cycle of translation elongation. This protein is found in Bacteria, mitochondria, and chloroplasts. [Protein synthesis, Translation factors]
Pssm-ID: 272914 [Multi-domain] Cd Length: 291 Bit Score: 129.90 E-value: 3.77e-35
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria ...
48-84
2.60e-14
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria of eukaryotes; EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains.
Pssm-ID: 270461 [Multi-domain] Cd Length: 37 Bit Score: 65.88 E-value: 2.60e-14
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
53-79
6.81e-05
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.
Pssm-ID: 270455 Cd Length: 28 Bit Score: 39.32 E-value: 6.81e-05
UBA-like domain found in uncharacterized bacteria proteins similar to eukaryotic nascent ...
48-84
1.04e-03
UBA-like domain found in uncharacterized bacteria proteins similar to eukaryotic nascent polypeptide-associated complex proteins (NAC); This subfamily contains a group of uncharacterized proteins found in bacteria. They all contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes.
Pssm-ID: 270543 [Multi-domain] Cd Length: 38 Bit Score: 36.10 E-value: 1.04e-03
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
58-82
8.07e-03
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.
Pssm-ID: 270491 Cd Length: 36 Bit Score: 33.57 E-value: 8.07e-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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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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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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