HAMAP rule MF_00184
General rule information
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| Accession | MF_00184 |
| Dates | 1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 45) |
| Name | Thr_tRNA_synth |
| Scope | Bacteria
Archaea |
| Templates | P0A8M3 (SYT_ECOLI); P56881 (SYT_THET8); Q9UZ14 (SYT_PYRAB); Q58597 (SYT_METJA): [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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case <OC:Archaea> and not <Feature:PF08915>
| Function | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). |
else
| Function | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). |
end case
| Catalytic activity | RHEA:24624: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC 6.1.1.3 |
case <FTGroup:1>
| Cofactor | Zn(2+) Note: Binds 1 zinc ion per subunit. |
end case
| Subunit | Homodimer. |
| Subcellular location | Cytoplasm. |
case <OC:Archaea> and <Feature:PF08915>
| Domain | The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself. |
end case
| Similarity | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Keywords
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case <FTTag:acet>
end case
Aminoacyl-tRNA synthetase
ATP-binding
Cytoplasm
Ligase
Nucleotide-binding
Protein biosynthesis
RNA-binding
tRNA-binding
ATP-binding
Cytoplasm
Ligase
Nucleotide-binding
Protein biosynthesis
RNA-binding
tRNA-binding
case <FTGroup:1>
end case
Gene Ontology
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GO:0005524; Molecular function: ATP binding.
GO:0004829; Molecular function: threonine-tRNA ligase activity.
GO:0006435; Biological process: threonyl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.
GO:0004829; Molecular function: threonine-tRNA ligase activity.
GO:0006435; Biological process: threonyl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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| Pfam | PF00587; tRNA-synt_2b; 1; |
| PF03129; HGTP_anticodon; 1; | |
| PF08915; tRNA-Thr_ED; 0-1; | |
| PRINTS | PR01047; TRNASYNTHTHR; 1; |
| NCBIfam | TIGR00418; ThrS; 1; |
| PROSITE | PS50862; AA_TRNA_LIGASE_II; 1; |
| PS51880; TGS; 0-1; trigger=PRU01228; |
Features
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| From: SYT_ECOLI (P0A8M3) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | 243 | 534 | Catalytic | |||||||||
| BINDING | 334 | 334 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic | C | 1 | |||||||
| BINDING | 385 | 385 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic | H | 1 | |||||||
| BINDING | 511 | 511 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic | H | 1 | |||||||
case <OC:Escherichia> or <OC:Shigella>
end case
case <OC:Archaea> and <Feature:PF08915>
| From: SYT_PYRAB (Q9UZ14) | ||||||||||||
| REGION | 1 | 143 | Editing domain | |||||||||
end case
Additional information
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| Size range | 540-702 amino acids |
| Related rules | None |
| Fusion | None |
| Comments | In some Archaea (AERPE, METS5, Sulfolobus among others) the editing domain is found in a separate protein. |