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UniProt functional annotation for P30014 | ||
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| UniProt code: P30014. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| 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, especially in strains lacking other exoribonucleases. {ECO:0000255|HAMAP-Rule:MF_00157, ECO:0000269|PubMed:12364334, ECO:0000269|PubMed:17437714, ECO:0000269|PubMed:21317904}. |
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| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00157, ECO:0000269|PubMed:12364334, ECO:0000269|PubMed:17437714, ECO:0000269|PubMed:21317904, ECO:0000269|PubMed:22718982}; 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. {ECO:0000255|HAMAP-Rule:MF_00157, ECO:0000269|PubMed:12364334, ECO:0000269|PubMed:17437714, ECO:0000269|PubMed:21317904, ECO:0000269|PubMed:22718982}; |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_00157, ECO:0000269|PubMed:17437714, ECO:0000269|PubMed:21317904}. |
| Disruption phenotype: | |
Required for optimal growth. {ECO:0000269|PubMed:21317904}. |
| Miscellaneous: | |
Member of the DEDD group of RNAses that are characterized by the presence of four acidic residues in the active site. These residues are conserved even when the proteins have highly divergent sequences. |
| Similarity: | |
Belongs to the RNase T family. {ECO:0000255|HAMAP- Rule:MF_00157}. |
Annotations taken from UniProtKB at the EBI.