ID SYN_THET8 Reviewed; 438 AA. AC P54263; Q5SKD5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 2. DT 10-JUN-2026, entry version 151. DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534}; DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534}; DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534}; DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534}; GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; GN OrderedLocusNames=TTHA0708; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION. RX PubMed=8706760; DOI=10.1111/j.1432-1033.1996.0501u.x; RA Seignovert L., Haertlein M., Leberman R.; RT "Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence of the RT gene and crystallization of the enzyme expressed in Escherichia coli."; RL Eur. J. Biochem. 239:501-508(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=9582288; DOI=10.1093/emboj/17.10.2947; RA Berthet-Colominas C., Seignovert L., Haertlein M., Grotli M., Cusack S., RA Leberman R.; RT "The crystal structure of asparaginyl-tRNA synthetase from Thermus RT thermophilus and its complexes with ATP and asparaginyl-adenylate: the RT mechanism of discrimination between asparagine and aspartic acid."; RL EMBO J. 17:2947-2960(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Asn) + L-asparagine + ATP = L-asparaginyl-tRNA(Asn) + AMP CC + diphosphate + H(+); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00534}; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00534}. 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; X91009; CAA62491.1; -; Genomic_DNA. DR EMBL; AP008226; BAD70531.1; -; Genomic_DNA. DR RefSeq; WP_011228137.1; NC_006461.1. DR PDB; 5ZG8; X-ray; 2.40 A; A=1-438. DR PDB; 9SH8; X-ray; 2.62 A; A=1-438. DR PDB; 9SH9; X-ray; 2.95 A; A/B=1-438. DR AlphaFoldDB; P54263; -. DR SMR; P54263; -. DR EnsemblBacteria; BAD70531; BAD70531; BAD70531. DR GeneID; 3168522; -. DR KEGG; ttj:TTHA0708; -. DR PATRIC; fig|300852.9.peg.702; -. DR eggNOG; COG0017; Bacteria. DR HOGENOM; CLU_004553_2_0_0; -. DR PhylomeDB; P54263; -. DR BRENDA; 6.1.1.22; 2305. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IDA:UniProtKB. DR CDD; cd04323; AsnRS_cyto_like_N; 1. DR CDD; cd00776; AsxRS_core; 1. DR FunFam; 3.30.930.10:FF:000016; Asparagine--tRNA ligase; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00534; Asn_tRNA_synth; 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; IPR004522; Asn-tRNA-ligase. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR NCBIfam; TIGR00457; asnS; 1. DR NCBIfam; NF003037; PRK03932.1; 1. DR PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1. DR PANTHER; PTHR22594; ASPARTYL/LYSYL-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 PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR PDBsum; 5ZG8; -. DR PDBsum; 9SH8; -. DR PDBsum; 9SH9; -. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..438 FT /note="Asparagine--tRNA ligase" FT /id="PRO_0000176470" FT CONFLICT 355 FT /note="A -> R (in Ref. 1; CAA62491)" FT /evidence="ECO:0000305" FT HELIX 5..11 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 14..28 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 31..37 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 54..61 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 68..77 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 84..96 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 111..116 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 118..121 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 125..147 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 179..182 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 218..229 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 233..254 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 256..262 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 270..274 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 282..295 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 310..317 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 344..355 FT /evidence="ECO:0007829|PDB:5ZG8" FT TURN 356..359 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 360..368 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 372..381 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 390..397 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 403..409 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 410..418 FT /evidence="ECO:0007829|PDB:5ZG8" FT HELIX 423..426 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:5ZG8" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:5ZG8" SQ SEQUENCE 438 AA; 50785 MW; B6A22A7D08F3D496 CRC64; MRVFIDEIAR HVDQEVELRG WLYQRRSKGK IHFLILRDGT GFLQATVVQG EVPEAVFREA DHLPQETALR VWGRVREDRR APGGFELAVR DLQVVSRPQG EYPIGPKEHG IDFLMDHRHL WLRHRRPFAV MRIRDELERA IHEFFGERGF LRFDAPILTP SAVEGTTELF EVELFDGEKA YLSQSGQLYA EAGALAFAKV YTFGPTFRAE RSKTRRHLLE FWMVEPEVAF MTHEENMALQ EELVSFLVAR VLERRSRELE MLGRDPKALE PAAEGHYPRL TYKEAVALVN RIAQEDPEVP PLPYGEDFGA PHEAALSRRF DRPVFVERYP ARIKAFYMEP DPEDPELVLN DDLLAPEGYG EIIGGSQRIH DLELLRRKIQ EFGLPEEVYD WYLDLRRFGS VPHSGFGLGL ERTVAWICGL AHVREAIPFP RMYTRMRP //