AC   MF_00123;
DC   Protein; auto
TR   HAMAP; MF_00123; -; 1; level=0
XX
Names: Arg_tRNA_synth
XX
ID   SYR
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19;
case <OC:Bacteria>
CC   -!- SUBUNIT: Monomer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF00750; tRNA-synt_1d; 1; trigger=no
DR   PRINTS; PR01038; TRNASYNTHARG; 1; trigger=no
DR   NCBIfam; TIGR00456; ArgS; 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:0004814; F:arginine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0006420; P:arginyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYR_BACSU (P46906)
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
FT   Condition: [AVPG]-N-[PTIVL]-x-[KGHS]-x-[LIMFV]-[HTSGNV]-[LMIV]-[GAV]-[HGRSNQ]
XX
Size: 527-671;
Related: None;
Template: P11875; P46906;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACCZ, HALH5, BACHK
Plasmid: None
Comments: Possible wrong start site in BORBU
XX
# Revision 1.36 2023/06/01
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