AC   MF_02004;
DC   Protein; auto
TR   HAMAP; MF_02004; -; 1; level=0
XX
Names: Val_tRNA_synth_type1
XX
ID   SYV
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   Name=valS;
XX
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily.
XX
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no
DR   Pfam; PF00133; tRNA-synt_1; 1; trigger=no
DR   Pfam; PF08264; Anticodon_1; 1; trigger=no
DR   PRINTS; PR00986; TRNASYNTHVAL; 1; trigger=no
DR   NCBIfam; TIGR00422; ValS; 1; trigger=no
DR   General; Coiled_coil; -; 1-unlimited; trigger=yes
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Coiled coil
KW   Ligase
KW   Nucleotide-binding
KW   Protein biosynthesis
XX
GO   GO:0004832; F:valine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0006438; P:valyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYV_ECOLI (P07118)
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   Condition: P-N-[VIL]-T-G-x-[LI]-H-[MLIV]-G-H
FT   MOTIF           554..558
FT                   /note="'KMSKS' region"
FT   Condition: K-[MLF]-[ST]-K-[ST]
FT   BINDING         557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
XX
Size: 822-1020;
Related: MF_02005;
Template: P07118; P96142; P11931;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.16 2023/06/01
//