ribonuclease P protein subunit p29 isoform X2 [Macaca thibetana thibetana]
ribonuclease P component 1 family protein( domain architecture ID 10486930)
ribonuclease (RNase) P component 1 family protein is a component of RNase MRP and/or RNase P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends; such as mammalian ribonuclease P protein subunit p29 (Rpp29/POP4)
List of domain hits
Name | Accession | Description | Interval | E-value | |||
RNase_P-MRP_p29 | pfam01868 | Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ... |
87-169 | 1.68e-40 | |||
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic proteins. The archaeal proteins are found to be expressed within ribosomal operons and several of the sequences are described as ribonuclease P protein subunit p29 proteins. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured beta-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex. Rpp29 catalyzes the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits. : Pssm-ID: 460367 Cd Length: 84 Bit Score: 131.78 E-value: 1.68e-40
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Name | Accession | Description | Interval | E-value | |||
RNase_P-MRP_p29 | pfam01868 | Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ... |
87-169 | 1.68e-40 | |||
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic proteins. The archaeal proteins are found to be expressed within ribosomal operons and several of the sequences are described as ribonuclease P protein subunit p29 proteins. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured beta-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex. Rpp29 catalyzes the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits. Pssm-ID: 460367 Cd Length: 84 Bit Score: 131.78 E-value: 1.68e-40
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POP4 | smart00538 | A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ... |
84-174 | 1.97e-36 | |||
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes and archaeal proteins; Pssm-ID: 197780 Cd Length: 92 Bit Score: 121.61 E-value: 1.97e-36
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POP4 | COG1588 | RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis]; |
99-175 | 4.01e-09 | |||
RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441196 Cd Length: 94 Bit Score: 51.37 E-value: 4.01e-09
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PRK03879 | PRK03879 | ribonuclease P protein component 1; Validated |
82-149 | 3.57e-05 | |||
ribonuclease P protein component 1; Validated Pssm-ID: 235169 Cd Length: 96 Bit Score: 40.69 E-value: 3.57e-05
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Name | Accession | Description | Interval | E-value | |||
RNase_P-MRP_p29 | pfam01868 | Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ... |
87-169 | 1.68e-40 | |||
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic proteins. The archaeal proteins are found to be expressed within ribosomal operons and several of the sequences are described as ribonuclease P protein subunit p29 proteins. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured beta-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex. Rpp29 catalyzes the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits. Pssm-ID: 460367 Cd Length: 84 Bit Score: 131.78 E-value: 1.68e-40
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POP4 | smart00538 | A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ... |
84-174 | 1.97e-36 | |||
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes and archaeal proteins; Pssm-ID: 197780 Cd Length: 92 Bit Score: 121.61 E-value: 1.97e-36
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POP4 | COG1588 | RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis]; |
99-175 | 4.01e-09 | |||
RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441196 Cd Length: 94 Bit Score: 51.37 E-value: 4.01e-09
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PRK03879 | PRK03879 | ribonuclease P protein component 1; Validated |
82-149 | 3.57e-05 | |||
ribonuclease P protein component 1; Validated Pssm-ID: 235169 Cd Length: 96 Bit Score: 40.69 E-value: 3.57e-05
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Blast search parameters | ||||
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