AC MF_00534; DC Protein; auto TR HAMAP; MF_00534; -; 1; level=0 XX Names: Asn_tRNA_synth XX ID SYN DE RecName: Full=Asparagine--tRNA ligase; DE EC=6.1.1.22; DE AltName: Full=Asparaginyl-tRNA synthetase; DE Short=AsnRS; GN Name=asnS; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L- CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; case CC -!- SUBUNIT: Homodimer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. XX DR Pfam; PF01336; tRNA_anti; 1; trigger=no DR Pfam; PF00152; tRNA-synt_2; 1; trigger=no DR PRINTS; PR01042; TRNASYNTHASP; 1; trigger=no DR NCBIfam; TIGR00457; AsnS; 1; trigger=no DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no XX KW Cytoplasm KW Aminoacyl-tRNA synthetase KW Protein biosynthesis KW Ligase KW ATP-binding KW Nucleotide-binding XX GO GO:0004816; F:asparagine-tRNA ligase activity GO GO:0005524; F:ATP binding GO GO:0006421; P:asparaginyl-tRNA aminoacylation GO GO:0005737; C:cytoplasm XX FT None XX Size: 429-523; Related: MF_00044; Template: P0A8M0; P54263; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in LACPL Plasmid: None Comments: None XX # Revision 1.27 2023/06/01 //