AC MF_00127; DC Protein; auto c? or or TR HAMAP; MF_00127; -; 1; level=0 XX Names: His_tRNA_synth XX ID SYH case or DE RecName: Full=Histidine--tRNA ligase; DE EC=6.1.1.21; DE AltName: Full=Histidyl-tRNA synthetase; DE Short=HisRS; else case DE RecName: Full=Histidine--tRNA ligase, chloroplastic; DE EC=6.1.1.21; DE AltName: Full=Histidyl-tRNA synthetase; DE Short=HisRS; end case GN Name=hisS; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L- CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21; case CC -!- SUBUNIT: Homodimer. end case case not CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. XX DR Pfam; PF00587; tRNA-synt_2b; 1; trigger=no DR Pfam; PF03129; HGTP_anticodon; 1; trigger=no DR NCBIfam; TIGR00442; HisS; 1; trigger=no DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no XX case not KW Cytoplasm end case KW Aminoacyl-tRNA synthetase KW Protein biosynthesis KW Ligase KW ATP-binding KW Nucleotide-binding XX GO GO:0005524; F:ATP binding GO GO:0004821; F:histidine-tRNA ligase activity GO GO:0006427; P:histidyl-tRNA aminoacylation case not GO GO:0005737; C:cytoplasm end case case GO GO:0009507; C:chloroplast end case XX FT None XX Size: 403-523; Related: MF_00125; Template: P60906; P60911; P56194; Scope: Bacteria Archaea Plastid Fusion: Nter: None Cter: None Duplicate: in BACAN, BACC1, BACCR, BACCZ, BACHK, SHOC1 Plasmid: None Comments: Divergent TROW8 and TROWT; not shown in alignment. It is difficult to distinguish between hisS and hisZ families. XX # Revision 1.45 2023/11/28 //