HAMAP rule MF_00564
General rule information
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Accession | MF_00564 |
Dates | 27-JUN-2002 (Created) 1-JUN-2023 (Last updated, Version 29) |
Name | RNase_PH |
Scope | Bacteria |
Templates | P28619 (RNPH_BACSU); P0CG18 (RNPH_ECOBW); P0CG19 (RNPH_ECOLI): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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Function | Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. |
Catalytic activity | RHEA:10628: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
EC 2.7.7.56 |
Subunit | Homohexameric ring arranged as a trimer of dimers. |
Similarity | Belongs to the RNase PH family. |
Keywords
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Gene Ontology
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GO:0000049; Molecular function: tRNA binding.
GO:0009022; Molecular function: phosphate-dependent exonuclease activity.
GO:0008033; Biological process: tRNA processing.
GO:0000175; Molecular function: 3'-5'-RNA exonuclease activity.
GO:0016075; Biological process: rRNA catabolic process.
GO:0009022; Molecular function: phosphate-dependent exonuclease activity.
GO:0008033; Biological process: tRNA processing.
GO:0000175; Molecular function: 3'-5'-RNA exonuclease activity.
GO:0016075; Biological process: rRNA catabolic process.
Cross-references
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Pfam | PF01138; RNase_PH; 1; |
PF03725; RNase_PH_C; 1; | |
PROSITE | PS01277; RIBONUCLEASE_PH; 1; |
NCBIfam | TIGR01966; RNasePH; 1; |
Features
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From: RNPH_PSEAE (P50597) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 125 | 127 | /ligand="phosphate" /ligand_id="ChEBI:CHEBI:43474" /ligand_note="substrate | [GS]-T-R | ||||||||
BINDING | 87 | 87 | /ligand="phosphate" /ligand_id="ChEBI:CHEBI:43474" /ligand_note="substrate | R |
Additional information
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