HAMAP annotation rule: MF_00140
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Accession MF_00140
Dates 1-JUN-2001 (Created)
21-NOV-2011 (Last updated, Version 33)
Data class Protein

case <OC:Bacteria>
end case


case <OC:Archaea>
end case

Names Trp_tRNA_synth



Identifier SYW
Protein name
RecName: Full=Tryptophan--tRNA ligase;
EC=6.1.1.2;
AltName: Full=Tryptophanyl-tRNA synthetase;
Short=TrpRS;
Gene name trpS
CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

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

SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
Pfam PF00579; tRNA-synt_1b; 1;
PRINTS PR01039; TRNASYNTHTRP; 1;
TIGRFAMs TIGR00233; TrpS; 1;
PROSITE PS00178; AA_TRNA_LIGASE_I; 1;
GO:0005524; Molecular function: ATP binding.
GO:0004830; Molecular function: tryptophan-tRNA ligase activity.
GO:0006436; Biological process: tryptophanyl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.

case <OC:Bacteria>
From: SYW_ECOLI (P00954)
Key     From     To       Description   Condition   FTGroup
MOTIF     12     20       "HIGH" region   [PATS]-x(0,1)-[STA]-[GDN]-x-[ILVFYQP]-[HST]-[ILW]-G-[NH]  
MOTIF     195     199       "KMSKS" region   K-M-[SG]-K-S  
BINDING     198     198       ATP (By similarity)   K  
end case

case <OC:Archaea>
From: SYW_METJA (Q58810)
Key     From     To       Description   Condition   FTGroup
MOTIF     75     83       "HIGH" region   P-[ST]-x(2)-[MVFP]-H-[LIF]-G-[HN]  
MOTIF     255     259       "KMSKS" region   K-M-S-[SA]-[SN]  
end case





case <OC:Bacteria>
Size range: 319-451 amino acids
end case


case <OC:Archaea>
Size range: 364-437 amino acids
end case

Related UniRules: None
Template: P00953 (SYW_GEOSE); P21656 (SYW_BACSU); P00954 (SYW_ECOLI); Q9RVD6 (SYW2_DEIRA); Q58810 (SYW_METJA): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in HALSA, STRCO
Plasmid encoded: None
Comments: Weird insertions in AQUAE, RALSO and METMA; not shown in alignment. DEIRA has a second tryptophanyl-tRNA synthetase (DR1093), which shows a weaker activity and whose role in protein biosynthesis has not been proven. It is probably involved in other processes.

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