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(s) |
Bacteria Archaea |
| Template(s) | P0A8M3 (SYT_ECOLI); P56881 (SYT_THET8); Q9UZ14 (SYT_PYRAB); Q58597 (SYT_METJA); [ Recover all ] |
| Triggered by |
HAMAP; MF_00184 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | SYT |
| Protein name | RecName: Full=Threonine--tRNA ligase; EC=6.1.1.3; AltName: Full=Threonyl-tRNA synthetase; Short=ThrRS; |
| Gene name | Name=thrS; |
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 | Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L- threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; |
| case <FTGroup:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; 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> | |
| Acetylation | |
| end case | |
| Aminoacyl-tRNA synthetase | |
| ATP-binding | |
| Cytoplasm | |
| Ligase | |
| Nucleotide-binding | |
| Protein biosynthesis | |
| RNA-binding | |
| tRNA-binding | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| 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 |
Cross-references
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| Pfam | PF00587; tRNA-synt_2b; 1; |
| Pfam | PF03129; HGTP_anticodon; 1; |
| Pfam | PF08915; tRNA-Thr_ED; 0-1; |
| PRINTS | PR01047; TRNASYNTHTHR; 1; |
| NCBIfam | TIGR00418; ThrS; 1; |
| PROSITE | PS50862; AA_TRNA_LIGASE_II; 1; |
| PROSITE | PS51880; TGS; 0-1; |
Features
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| From: SYT_ECOLI (P0A8M3) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | 243 | 534 | /note="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> | ||||||||||||
| MOD_RES | 286 | 286 | /note="N6-acetyllysine" | acet | K | |||||||
| end case | ||||||||||||
| From: SYT_PYRAB (Q9UZ14) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Archaea> and <Feature:PF08915> | ||||||||||||
| REGION | 1 | 143 | /note="Editing domain" | |||||||||
| end case | ||||||||||||
Additional information
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| Size range | 540-702 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | In some Archaea (AERPE, METS5, Sulfolobus among others) the editing domain is found in a separate protein. |