uL16 family ribosomal protein such as human 60S ribosomal protein L10, bacteria 50S ribosomal protein L16, chloroplast 50S ribosomal protein L16, and mitochondrial 39S ribosomal protein L16
Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, ...
1-173
1.43e-113
Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, mitochondria, and chloroplasts. Large subunits that lack L16 are defective in peptidyl transferase activity, peptidyl-tRNA hydrolysis activity, association with the 30S subunit, binding of aminoacyl-tRNA and interaction with antibiotics. L16 is required for the function of elongation factor P (EF-P), a protein involved in peptide bond synthesis through the stimulation of peptidyl transferase activity by the ribosome. Mutations in L16 and the adjoining bases of 23S rRNA confer antibiotic resistance in bacteria, suggesting a role for L16 in the formation of the antibiotic binding site. The GTPase RbgA (YlqF) is essential for the assembly of the large subunit, and it is believed to regulate the incorporation of L16. L10e is the archaeal and eukaryotic cytosolic homolog of bacterial L16. L16 and L10e exhibit structural differences at the N-terminus.
The actual alignment was detected with superfamily member PTZ00173:
Pssm-ID: 469737 Cd Length: 213 Bit Score: 321.21 E-value: 1.43e-113
ribosomal protein uL16(L10.e), eukarotic/archaeal form; This model finds the archaeal and ...
1-139
6.59e-63
ribosomal protein uL16(L10.e), eukarotic/archaeal form; This model finds the archaeal and eukaryotic forms of ribosomal protein uL16, previously L10.e. The protein is encoded by multiple loci in some eukaryotes and has been assigned a number of extra-ribosomal functions, some of which will require re-evaluation in the context of identification as a ribosomal protein. L10.e is distantly related to eubacterial ribosomal protein L16. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 129380 Cd Length: 172 Bit Score: 191.61 E-value: 6.59e-63
Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, ...
28-129
2.94e-35
Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, mitochondria, and chloroplasts. Large subunits that lack L16 are defective in peptidyl transferase activity, peptidyl-tRNA hydrolysis activity, association with the 30S subunit, binding of aminoacyl-tRNA and interaction with antibiotics. L16 is required for the function of elongation factor P (EF-P), a protein involved in peptide bond synthesis through the stimulation of peptidyl transferase activity by the ribosome. Mutations in L16 and the adjoining bases of 23S rRNA confer antibiotic resistance in bacteria, suggesting a role for L16 in the formation of the antibiotic binding site. The GTPase RbgA (YlqF) is essential for the assembly of the large subunit, and it is believed to regulate the incorporation of L16. L10e is the archaeal and eukaryotic cytosolic homolog of bacterial L16. L16 and L10e exhibit structural differences at the N-terminus.
Pssm-ID: 238714 Cd Length: 112 Bit Score: 119.13 E-value: 2.94e-35
Ribosomal protein L16/L10AE [Translation, ribosomal structure and biogenesis]; Ribosomal ...
28-129
2.17e-18
Ribosomal protein L16/L10AE [Translation, ribosomal structure and biogenesis]; Ribosomal protein L16/L10AE is part of the Pathway/BioSystem: Ribosome 50S subunit
Pssm-ID: 439967 Cd Length: 136 Bit Score: 76.61 E-value: 2.17e-18
ribosomal protein uL16(L10.e), eukarotic/archaeal form; This model finds the archaeal and ...
1-139
6.59e-63
ribosomal protein uL16(L10.e), eukarotic/archaeal form; This model finds the archaeal and eukaryotic forms of ribosomal protein uL16, previously L10.e. The protein is encoded by multiple loci in some eukaryotes and has been assigned a number of extra-ribosomal functions, some of which will require re-evaluation in the context of identification as a ribosomal protein. L10.e is distantly related to eubacterial ribosomal protein L16. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 129380 Cd Length: 172 Bit Score: 191.61 E-value: 6.59e-63
Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, ...
28-129
2.94e-35
Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, mitochondria, and chloroplasts. Large subunits that lack L16 are defective in peptidyl transferase activity, peptidyl-tRNA hydrolysis activity, association with the 30S subunit, binding of aminoacyl-tRNA and interaction with antibiotics. L16 is required for the function of elongation factor P (EF-P), a protein involved in peptide bond synthesis through the stimulation of peptidyl transferase activity by the ribosome. Mutations in L16 and the adjoining bases of 23S rRNA confer antibiotic resistance in bacteria, suggesting a role for L16 in the formation of the antibiotic binding site. The GTPase RbgA (YlqF) is essential for the assembly of the large subunit, and it is believed to regulate the incorporation of L16. L10e is the archaeal and eukaryotic cytosolic homolog of bacterial L16. L16 and L10e exhibit structural differences at the N-terminus.
Pssm-ID: 238714 Cd Length: 112 Bit Score: 119.13 E-value: 2.94e-35
Ribosomal protein L16/L10AE [Translation, ribosomal structure and biogenesis]; Ribosomal ...
28-129
2.17e-18
Ribosomal protein L16/L10AE [Translation, ribosomal structure and biogenesis]; Ribosomal protein L16/L10AE is part of the Pathway/BioSystem: Ribosome 50S subunit
Pssm-ID: 439967 Cd Length: 136 Bit Score: 76.61 E-value: 2.17e-18
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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