ID SYH1_BACCR Reviewed; 426 AA. AC Q81B71; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Histidine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00127}; DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127}; DE AltName: Full=Histidyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00127}; DE Short=HisRS 1 {ECO:0000255|HAMAP-Rule:MF_00127}; GN Name=hisS-1 {ECO:0000255|HAMAP-Rule:MF_00127}; GN OrderedLocusNames=BC_3317; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). 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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00127}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00127}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016877; AAP10257.1; -; Genomic_DNA. DR RefSeq; NP_833056.1; NC_004722.1. DR AlphaFoldDB; Q81B71; -. DR SMR; Q81B71; -. DR STRING; 226900.BC_3317; -. DR KEGG; bce:BC3317; -. DR PATRIC; fig|226900.8.peg.3402; -. DR HOGENOM; CLU_025113_3_0_9; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProt. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00773; HisRS-like_core; 1. DR CDD; cd00859; HisRS_anticodon; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR HAMAP; MF_00127; His_tRNA_synth; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR036621; Anticodon-bd_dom_sf. DR InterPro; IPR015807; His-tRNA-ligase. DR InterPro; IPR041715; HisRS-like_core. DR InterPro; IPR004516; HisRS/HisZ. DR InterPro; IPR033656; HisRS_anticodon. DR NCBIfam; TIGR00442; hisS; 1. DR PANTHER; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1. DR PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF13393; tRNA-synt_His; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..426 FT /note="Histidine--tRNA ligase 1" FT /id="PRO_0000136097" SQ SEQUENCE 426 AA; 48144 MW; 4DB7E3D889D43C30 CRC64; MMEMRNVKGT KDYLPEEQVL RNKIKRACED TFERYGCKPL ETPTLNMYEL MSYKYGGGDE ILKEIYTLQD QGKRELALRY DLTIPFAKVV AMNPNLRLPF KRYEIGKVFR DGPIKQGRFR EFIQCDVDIV GVESVMAEAE LMAMAFELFR TLNLEITIQY NNRKLLNGIL ESINIPTELT SDVILSLDKI EKIGIDGVRK DVLERGISEE MADTICNTVL SCLKLTIADF KEAFNNPLVA DGVNELQQLQ QYLIALGINE NTIFNPFLAR GLTMYTGTVY EIFLKDRSIT SSIGSGGRYD NIIGAFRGDN MNYPTVGISF GLDVIYTALS QKETISSTAD VFIIPLGTEL QCLQIAQQLR STTSLKVELE LAGRKLKRAL NYANKENIPY VLIIGEDELS TNTVVLRNMK EGSEVKVPIS SLSRYL //