Exosome complex component RRP45 [Caenorhabditis elegans]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| RNase_PH super family | cl03114 | RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ... |
6-54 | 3.75e-14 | ||
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Evolutionarily related members can be fond in prokaryotes, archaea, and eukaryotes. Bacterial ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain and is involved in mRNA degradation in a 3'-5' direction. Archaeal exosomes contain two individually encoded RNase PH-like 3'-5' exoribonucleases and are required for 3' processing of the 5.8S rRNA. The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits, but it is not a phosphorolytic enzyme per se; it directly associates with Rrp44 and Rrp6, which are hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. All members of the RNase PH-like family form ring structures by oligomerization of six domains or subunits, except for a total of 3 subunits with tandem repeats in the case of PNPase, with a central channel through which the RNA substrate must pass to gain access to the phosphorolytic active sites. The actual alignment was detected with superfamily member cd11368: Pssm-ID: 446015 [Multi-domain] Cd Length: 259 Bit Score: 63.70 E-value: 3.75e-14
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| Name | Accession | Description | Interval | E-value | ||
| RNase_PH_RRP45 | cd11368 | RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ... |
6-54 | 3.75e-14 | ||
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts. Pssm-ID: 206773 [Multi-domain] Cd Length: 259 Bit Score: 63.70 E-value: 3.75e-14
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| PRK04282 | PRK04282 | exosome complex protein Rrp42; |
14-54 | 2.53e-05 | ||
exosome complex protein Rrp42; Pssm-ID: 235268 [Multi-domain] Cd Length: 271 Bit Score: 39.47 E-value: 2.53e-05
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| Name | Accession | Description | Interval | E-value | ||
| RNase_PH_RRP45 | cd11368 | RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ... |
6-54 | 3.75e-14 | ||
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts. Pssm-ID: 206773 [Multi-domain] Cd Length: 259 Bit Score: 63.70 E-value: 3.75e-14
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| RNase_PH_archRRP42 | cd11365 | RRP42 subunit of archaeal exosome; The RRP42 subunit of the archaeal exosome is a member of ... |
11-54 | 2.34e-06 | ||
RRP42 subunit of archaeal exosome; The RRP42 subunit of the archaeal exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp42 dimers. The central chamber within the ring contains three phosphorolytic active sites located in an Rrp41 pocket at the interface between Rrp42 and Rrp41. The ring is capped by three copies of Rrp4 and/or Csl4 which contain putative RNA interaction domains. The archaeal exosome degrades single-stranded RNA (ssRNA) in the 3'-5' direction, but also can catalyze the reverse reaction of adding nucleoside diphosphates to the 3'-end of RNA which has been shown to lead to the formation of poly-A-rich tails on RNA. It is required for 3' processing of the 5.8S rRNA. Pssm-ID: 206770 [Multi-domain] Cd Length: 256 Bit Score: 42.20 E-value: 2.34e-06
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| PRK04282 | PRK04282 | exosome complex protein Rrp42; |
14-54 | 2.53e-05 | ||
exosome complex protein Rrp42; Pssm-ID: 235268 [Multi-domain] Cd Length: 271 Bit Score: 39.47 E-value: 2.53e-05
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| PRK03983 | PRK03983 | exosome complex exonuclease Rrp41; Provisional |
21-54 | 8.05e-03 | ||
exosome complex exonuclease Rrp41; Provisional Pssm-ID: 235187 [Multi-domain] Cd Length: 244 Bit Score: 32.30 E-value: 8.05e-03
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