HAMAP annotation rule: MF_00184
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Accession MF_00184
Dates 1-JUN-2001 (Created)
21-NOV-2011 (Last updated, Version 36)
Data class Protein
Names Thr_tRNA_synth



Identifier SYT
Protein name
RecName: Full=Threonine--tRNA ligase;
EC=6.1.1.3;
AltName: Full=Threonyl-tRNA synthetase;
Short=ThrRS;
Gene name thrS
CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

case <FTGroup:1>
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
end case


case <OC:Bacteria>
SUBUNIT: Homodimer (By similarity).
end case

SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
Pfam PF00587; tRNA-synt_2b; 1;
PRINTS PR01047; TRNASYNTHTHR; 1;
TIGRFAMs TIGR00418; ThrS; 1;
PROSITE PS50862; AA_TRNA_LIGASE_II; 1;

case <FTTag:acet>
end case


case <FTGroup:1>
end case

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.
From: SYT_ECOLI (P0A8M3)
Key     From     To       Description   Condition   FTGroup
REGION     243     534       Catalytic      
 
METAL     334     334       Zinc; catalytic (By similarity)   C   1
METAL     385     385       Zinc; catalytic (By similarity)   H   1
METAL     511     511       Zinc; catalytic (By similarity)   H   1
case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
 
MOD_RES     286     286       N6-acetyllysine (By similarity)   K  
end case




Size range: 540-702 amino acids
Related UniRules: None
Template: P0A8M3 (SYT_ECOLI); P56881 (SYT_THET8): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in AERPE, BACSU
Plasmid encoded: None
Comments: There are two ThrRS in AERPE. The first one (APE_0809.1) is most similar to bacterial ThrRS but it lack the N-terminal domain. The second one (APE_0117.1) is most similar to archaeal ThrRS but lack the central domain

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