ID SYDND_BACC4 Reviewed; 591 AA. AC B7HE37; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 04-NOV-2026, entry version 91. DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; GN OrderedLocusNames=BCB4264_A4522; OS Bacillus cereus (strain B4264). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=405532; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4264; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus B4264."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since CC it is able to aspartylate not only its cognate tRNA(Asp) but also CC tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first CC activated by ATP to form Asp-AMP and then transferred to the acceptor CC end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP + CC diphosphate; Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710, Rhea:RHEA- CC COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; CC EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00044}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}. 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; CP001176; ACK62033.1; -; Genomic_DNA. DR RefSeq; WP_000840898.1; NC_011725.1. DR SMR; B7HE37; -. DR KEGG; bcb:BCB4264_A4522; -. DR HOGENOM; CLU_014330_3_2_9; -. DR OMA; AAADLMC; -. DR CDD; cd00777; AspRS_core; 1. DR CDD; cd04317; EcAspRS_like_N; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 3.30.1360.30; GAD-like domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1. DR InterPro; IPR004364; Aa-tRNA-synt_II. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004524; Asp-tRNA-ligase_1. DR InterPro; IPR047089; Asp-tRNA-ligase_1_N. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR047090; AspRS_core. DR InterPro; IPR004115; GAD-like_sf. DR InterPro; IPR029351; GAD_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1. DR Pfam; PF02938; GAD; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF55261; GAD domain-like; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR NCBIfam; NF001750; aspS; 1. DR NCBIfam; TIGR00459; aspS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProtKB-ARBA. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR AlphaFoldDB; B7HE37; -. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..591 FT /note="Aspartate--tRNA(Asp/Asn) ligase" FT /id="PRO_1000198959" FT REGION 200..203 FT /note="Aspartate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 176 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 222..224 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 222 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 231 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 450 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 484 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 491 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 536..539 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT SITE 84 FT /note="Important for tRNA non-discrimination" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" SQ SEQUENCE 591 AA; 66308 MW; 54AFCCC7C5C82B55 CRC64; MAERTHACGK VTVEAVGQTV QLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FNPETSKEAL EVAETIRSEY VLHVEGTVVE RGEGAINDNM ATGRIEVQAT KVNVLNAAKT TPIIIADDTD ASEDVRLKYR YLDLRRPVMF NTFKMRHDVT KTIRNFLDTE EFLEVETPIL TKSTPEGARD YLVPSRVHDG EFYALPQSPQ LFKQLLMVGG FERYYQVARC FRDEDLRADR QPEFTQIDIE ASFLTQDEIL DMMERMMTKV MKDAKGVEVS APFPRMKYAD AMARYGSDKP DTRFEMELTD LSEFAAGCGF KVFTSAVESG GQVKAINAKG AASKYSRKDI DALTEFVKVY GAKGLAWLKV EEDGLKGPIA KFFGEEDANV LMSTLEATAG DLLLFVADKK SVVADSLGAL RLRLGKELEL IDESKFNFLW VTDWPLLEYD EDADRYFAAH HPFTMPFRED VELLETAPEK ARAQAYDLVL NGYELGGGSL RIYERDVQEK MFKALGFSQE EAQEQFGFLL EAFEYGTPPH GGIALGLDRL VMLLAGRTNL RDTIAFPKTA SASCLLTEAP SPVAEAQLEE LNLKLSLKEE K //