HAMAP rule MF_00157
General rule information
[?]
| Accession | MF_00157 |
| Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 25) |
| Name | RNase_T |
| Scope(s) |
Bacteria |
| Template(s) | P30014 (RNT_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_00157 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier | RNT |
| Protein name | RecName: Full=Ribonuclease T; EC=3.1.13.-; AltName: Full=Exoribonuclease T; Short=RNase T; |
| Gene name | Name=rnt; |
Comments
[?]
| FUNCTION | Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis. |
| case <FTGroup:1> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds two Mg(2+) per subunit. The active form of the enzyme binds two Mg(2+) ions in its active site. The first Mg(2+) forms only one salt bridge with the protein.; |
| end case | |
| SUBUNIT | Homodimer. |
| SIMILARITY | Belongs to the RNase T family. |
Keywords
[?]
| Exonuclease | |
| Hydrolase | |
| Nuclease | |
| tRNA processing | |
| case <FTGroup:1> | |
| Magnesium | |
| Metal-binding | |
| end case | |
Gene Ontology
[?]
| GO:0016896; Molecular function:RNA exonuclease activity, producing 5'-phosphomonoesters | |
| case <FTGroup:1> | |
| GO:0000287; Molecular function:magnesium ion binding | |
| end case | |
| GO:0006396; Biological process:RNA processing | |
Cross-references
[?]
Features
[?]
| From: RNT_ECOLI (P30014) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 181 | 181 | /note="Proton donor/acceptor" | H | ||||||||
| BINDING | 23 | 23 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" /ligand_note="catalytic" |
D | 1 | |||||||
| BINDING | 23 | 23 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" /ligand_note="catalytic" |
D | 1 | |||||||
| BINDING | 25 | 25 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" /ligand_note="catalytic" |
E | 1 | |||||||
| BINDING | 181 | 181 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" /ligand_note="catalytic" |
H | 1 | |||||||
| BINDING | 186 | 186 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" /ligand_note="catalytic" |
D | 1 | |||||||
| SITE | 29 | 29 | /note="Important for substrate binding and specificity" | F | ||||||||
| SITE | 77 | 77 | /note="Important for substrate binding and specificity" | F | ||||||||
| SITE | 124 | 124 | /note="Important for substrate binding and specificity" | F | ||||||||
| SITE | 146 | 146 | /note="Important for substrate binding and specificity" | F | ||||||||
Additional information
[?]
| Size range | 190-275 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |