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Annotation rule MF_00184
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General rule information [?]

Accession MF_00184
Dates 1-JUN-2001 (Created)
2-JAN-2019 (Last updated, Version 41)
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 [?]


Identifier, protein and gene names [?]

Identifier
SYT
Protein name
RecName: Full=Threonine--tRNA ligase;
EC=6.1.1.3;
AltName: Full=Threonyl-tRNA synthetase;
Short=ThrRS;
Gene name
thrS

Comments [?]

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 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 [?]

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 [?]

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 [?]

Pfam PF00587; tRNA-synt_2b; 1;
PF03129; HGTP_anticodon; 1;
PF08915; tRNA-Thr_ED; 0-1;
PRINTS PR01047; TRNASYNTHTHR; 1;
TIGRFAMs TIGR00418; ThrS; 1;
PROSITE PS50862; AA_TRNA_LIGASE_II; 1;
PS51880; TGS; 0-1; trigger=PRU01228;

Features [?]

From: SYT_ECOLI (P0A8M3)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     243     534       Catalytic        
METAL     334     334       Zinc; catalytic     C   1
METAL     385     385       Zinc; catalytic     H   1
METAL     511     511       Zinc; catalytic     H   1
case <OC:Escherichia> or <OC:Shigella>
MOD_RES     286     286       N6-acetyllysine   acet   K  
end case
case <OC:Archaea> and <Feature:PF08915>
From: SYT_PYRAB (Q9UZ14)
REGION     1     143       Editing domain        
end case

Additional information [?]

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.


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