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HAMAP annotation rule: MF_00184

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General rule information

Accession MF_00184
Dates 1-JUN-2001 (Created)
25-NOV-2009 (Last updated, Version 33)
Data class Protein

case <OC:Bacteria>
Predictors HAMAP; MF_00184_B; [distribution of match scores in UniProtKB];[seed alignment for MF_00184_B]
end case


case <OC:Archaea>
Predictors HAMAP; MF_00184_A; [distribution of match scores in UniProtKB];[seed alignment for MF_00184_A]
end case

Names Thr_tRNA_synth


Propagated annotation

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

case <FT:2> and <FT:3> and <FT:4> or <FT:7> and <FT:8> and <FT:9>
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.
Cross-references
Pfam PF00587; tRNA-synt_2b; 1;
PRINTS PR01047; TRNASYNTHTHR; 1;
TIGRFAMs TIGR00418; thrS; 1;
PROSITE PS50862; AA_TRNA_LIGASE_II; 1;
Keywords

case <FT:5>
Acetylation.
end case

Aminoacyl-tRNA synthetase, ATP-binding, Cytoplasm, Ligase, Nucleotide-binding, Protein biosynthesis.

case <FT:2> and <FT:3> and <FT:4> or <FT:7> and <FT:8> and <FT:9>
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.
Features

case <OC:Bacteria>
From: SYT_ECOLI (P0A8M3)
Key     From     To       Description   Condition   FTGroup
REGION     243     534       Catalytic      
METAL     334     334       Zinc; catalytic (By similarity)   C  
METAL     385     385       Zinc; catalytic (By similarity)   H  
METAL     511     511       Zinc; catalytic (By similarity)   H  
end case

case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
MOD_RES     286     286       N6-acetyllysine (By similarity)   K  
end case

case <OC:Archaea>
From: SYT_ARCFU (O29703)
Key     From     To       Description   Condition   FTGroup
REGION     196     495       Catalytic      
METAL     288     288       Zinc; catalytic (By similarity)   C  
METAL     340     340       Zinc; catalytic (By similarity)   H  
METAL     464     464       Zinc; catalytic (By similarity)   H  
end case



Additional information


case <OC:Bacteria>
Size range: 564-702 amino acids
end case


case <OC:Archaea>
Size range: 540-660 amino acids
end case

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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UniProtKB rule member sequences