AC MF_00184; DC Protein; auto TR HAMAP; MF_00184; -; 1; level=0 XX Names: Thr_tRNA_synth XX ID SYT DE RecName: Full=Threonine--tRNA ligase; DE EC=6.1.1.3; DE AltName: Full=Threonyl-tRNA synthetase; DE Short=ThrRS; GN Name=thrS; XX case and not CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- CC step reaction: L-threonine is first activated by ATP to form Thr-AMP CC and then transferred to the acceptor end of tRNA(Thr). else CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- CC step reaction: L-threonine is first activated by ATP to form Thr-AMP CC and then transferred to the acceptor end of tRNA(Thr). Also edits CC incorrectly charged L-seryl-tRNA(Thr). end case CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L- CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. case and CC -!- DOMAIN: The N-terminal domain is an archaea-specific tRNA-editing CC domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis CC of tRNA editing is performed by the charged tRNA itself. end case CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. XX DR Pfam; PF00587; tRNA-synt_2b; 1; trigger=no DR Pfam; PF03129; HGTP_anticodon; 1; trigger=no DR Pfam; PF08915; tRNA-Thr_ED; 0-1; trigger=no DR PRINTS; PR01047; TRNASYNTHTHR; 1; trigger=no DR NCBIfam; TIGR00418; ThrS; 1; trigger=no DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no DR PROSITE; PS51880; TGS; 0-1; trigger=yes XX case KW Acetylation end case KW Aminoacyl-tRNA synthetase KW ATP-binding KW Cytoplasm KW Ligase KW Nucleotide-binding KW Protein biosynthesis KW RNA-binding KW tRNA-binding case KW Metal-binding KW Zinc end case XX GO GO:0005524; F:ATP binding GO GO:0004829; F:threonine-tRNA ligase activity GO GO:0006435; P:threonyl-tRNA aminoacylation GO GO:0005737; C:cytoplasm XX FT From: SYT_ECOLI (P0A8M3) FT REGION 243..534 FT /note="Catalytic" FT BINDING 334 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: C FT BINDING 385 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 511 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H case or FT MOD_RES 286 FT /note="N6-acetyllysine" FT Tag: acet; Condition: K end case FT From: SYT_PYRAB (Q9UZ14) case and FT REGION 1..143 FT /note="Editing domain" end case XX Size: 540-702; Related: None; Template: P0A8M3; P56881; Q9UZ14; Q58597; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in BACSU Plasmid: None Comments: In some Archaea (AERPE, METS5, Sulfolobus among others) the editing domain is found in a separate protein. XX # Revision 1.45 2023/06/01 //