AC   MF_00140;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00140_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00140_A; -; 1; level=0
XX
Names: Trp_tRNA_synth
XX
ID   SYW
DE   RecName: Full=Tryptophan--tRNA ligase;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
GN   Name=trpS;
XX
CC   -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
case <OC:Bacteria>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF00579; tRNA-synt_1b; 1; trigger=no
DR   PRINTS; PR01039; TRNASYNTHTRP; 1; trigger=no
DR   NCBIfam; TIGR00233; TrpS; 1; trigger=no
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004830; F:tryptophan-tRNA ligase activity
GO   GO:0006436; P:tryptophanyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYW_GEOSE (P00953)
case <OC:Bacteria>
FT   BINDING         9..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [QTRK]-[PATS]-x(0,1)-[ST]
FT   BINDING         17..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[NH]
FT   BINDING         144..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x-D
FT   BINDING         192..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K-M-[SG]-K-S
FT   MOTIF           10..18
FT                   /note="'HIGH' region"
FT   Condition: [PATS]-x(0,1)-[STA]-[GDN]-x-[ILVFYQP]-[HST]-[ILW]-G-[NH]
FT   MOTIF           192..196
FT                   /note="'KMSKS' region"
FT   Condition: K-M-[SG]-K-S
FT   BINDING         132
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT   Condition: D
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [VIL]
end case
FT   From: SYW_METJA (Q58810)
case <OC:Archaea>
FT   MOTIF           75..83
FT                   /note="'HIGH' region"
FT   Condition: P-[ST]-x(2)-[MVFP]-H-[LIF]-G-[HN]
FT   MOTIF           255..259
FT                   /note="'KMSKS' region"
FT   Condition: K-M-S-[SA]-[SN]
end case
XX
case <OC:Bacteria>
Size: 319-451;
end case
case <OC:Archaea>
Size: 364-437;
end case
Related: None;
Template: P00953; P21656; P00954; Q9RVD6; Q58810;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in HALSA, STRCO
Plasmid: None
Comments: Weird insertions in AQUAE, RALN1 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.
XX
# Revision 1.42 2023/11/28
//