ID A0A218NZJ5_THECE Unreviewed; 438 AA. AC A0A218NZJ5; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 20-DEC-2017, entry version 4. 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. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=2264 {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 CC a two-step reaction: L-aspartate is first activated by ATP to form CC Asp-AMP and then transferred to the acceptor end of tRNA(Asp). CC {ECO:0000256|HAMAP-Rule:MF_02075}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP + CC diphosphate + L-aspartyl-tRNA(Asp). {ECO:0000256|HAMAP- CC Rule:MF_02075}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02075}; CC Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium CC site (Mg1) is bound to the beta- and gamma-phosphates of ATP and CC four water molecules complete its coordination sphere. CC {ECO:0000256|HAMAP-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 CC family. Type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02075}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 KEGG; tce:A3L02_00150; -. DR KO; K01876; -. 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:0016874; F:ligase activity; IEA:UniProtKB-KW. 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 HAMAP; MF_02075; Asp_tRNA_synth_type2; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR006195; aa-tRNA-synth_II. 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; PTHR43450; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 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|HAMAP-Rule:MF_02075}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02075}; KW Complete proteome {ECO:0000313|Proteomes:UP000197156}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02075, ECO:0000313|EMBL:ASI98091.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02075}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02075}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02075}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075}; KW Reference proteome {ECO:0000313|Proteomes:UP000197156}. FT DOMAIN 137 438 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. FT NP_BIND 214 216 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}. FT NP_BIND 222 224 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}. FT NP_BIND 409 412 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}. FT REGION 192 195 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT METAL 361 361 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT METAL 361 361 Magnesium 3. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT METAL 364 364 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT BINDING 170 170 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT BINDING 214 214 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT BINDING 361 361 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}. FT BINDING 364 364 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT BINDING 368 368 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_02075}. FT SITE 85 85 Important for tRNA discrimination. FT {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 //