hypothetical protein DMUE_1636 [Dictyocoela muelleri]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| RNase_P-MRP_p29 super family | cl46579 | Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ... |
87-144 | 3.23e-08 | ||
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. The actual alignment was detected with superfamily member pfam01868: Pssm-ID: 480919 Cd Length: 84 Bit Score: 48.19 E-value: 3.23e-08
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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 ... |
87-144 | 3.23e-08 | ||
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: 48.19 E-value: 3.23e-08
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| POP4 | smart00538 | A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ... |
87-144 | 5.72e-04 | ||
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: 37.25 E-value: 5.72e-04
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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 ... |
87-144 | 3.23e-08 | ||
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: 48.19 E-value: 3.23e-08
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| POP4 | smart00538 | A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ... |
87-144 | 5.72e-04 | ||
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: 37.25 E-value: 5.72e-04
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