ID A0A218NZJ5_THECE Unreviewed; 438 AA. AC A0A218NZJ5; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 14-DEC-2022, entry version 28. DE RecName: Full=Aspartate--tRNA(Asp) ligase {ECO:0000256|HAMAP-Rule:MF_02075}; DE EC=6.1.1.12 {ECO:0000256|HAMAP-Rule:MF_02075}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075}; DE Short=AspRS {ECO:0000256|HAMAP-Rule:MF_02075}; DE AltName: Full=Discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075}; DE Short=D-AspRS {ECO:0000256|HAMAP-Rule:MF_02075}; GN Name=aspC {ECO:0000313|EMBL:ASI98091.1}; GN Synonyms=aspS {ECO:0000256|HAMAP-Rule:MF_02075}; GN ORFNames=A3L02_00150 {ECO:0000313|EMBL:ASI98091.1}; OS Thermococcus celer Vu 13 = JCM 8558. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=1293037 {ECO:0000313|EMBL:ASI98091.1, ECO:0000313|Proteomes:UP000197156}; RN [1] {ECO:0000313|EMBL:ASI98091.1, ECO:0000313|Proteomes:UP000197156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vu 13 {ECO:0000313|EMBL:ASI98091.1, RC ECO:0000313|Proteomes:UP000197156}; RA Oger P.M.; RT "Complete genome sequence of Thermococcus celer."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a CC two-step reaction: L-aspartate is first activated by ATP to form Asp- CC AMP and then transferred to the acceptor end of tRNA(Asp). CC {ECO:0000256|HAMAP-Rule:MF_02075}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L- CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, CC ChEBI:CHEBI:456215; EC=6.1.1.12; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02075}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02075}; CC Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium site CC (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water CC molecules complete its coordination sphere. {ECO:0000256|HAMAP- CC Rule:MF_02075}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02075}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312, ECO:0000256|HAMAP- CC Rule:MF_02075}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02075}. 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; CP014854; ASI98091.1; -; Genomic_DNA. DR AlphaFoldDB; A0A218NZJ5; -. DR EnsemblBacteria; ASI98091; ASI98091; A3L02_00150. DR KEGG; tce:A3L02_00150; -. DR Proteomes; UP000197156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.930.10; -; 1. DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 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; SSF50249; Nucleic acid-binding proteins; 1. DR TIGRFAMs; TIGR00458; aspS_nondisc; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_02075}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02075}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02075}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02075}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02075}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02075}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075}. FT DOMAIN 137..438 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" FT REGION 192..195 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 170 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 214..216 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 214 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 222..224 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 361 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 361 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 361 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 364 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 364 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 368 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT BINDING 409..412 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" FT SITE 85 FT /note="Important for tRNA discrimination" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075" SQ SEQUENCE 438 AA; 50790 MW; A27787A4FE8CF9FD CRC64; MYRTHYSSQI TQELNGQRVK VAGWVWEIKD LGGIKFLWIR DREGIVQITA PKKKVTPEIF KLIPKLKAED VVAVEGVVNF TPKAKLGFEV LPEKLEVLSK AESPLPLDPT GKVKAELDTR LDNRFMDVRR PEVMAIFKIR SSVFKAVRDF FYGEGFIEVH TPKIIATATE GGTELFPMRY FERDAFLAQS PQLYKQIMMA TGLDRVYEIA PIFRAEEHNT TRHLNEAWSI DAEMAFIENE EEVMNLLERL VAHAIDHVRE NNGKELETLG FELEEPKLPF PRLSYDRALE ILSDLGKTIE WGEDIDTEGE KLLGEYMMEN ENAPLYFLYR YPSEAKPFYI MKYDDNPEIS RAFDLEYRGV EITSGGQREH RVDVLVEQIR EKGLNPDSFE FYLRAFRYGM PPHGGFGLGA ERLIKQMLDL NNIREVILFP RDRRRLTP //