ID   SYN_THEAC               Reviewed;         429 AA.
AC   Q9HKS7;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 111.
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}; OrderedLocusNames=Ta0519;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); 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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR   EMBL; AL445064; CAC11659.1; -; Genomic_DNA.
DR   RefSeq; WP_010900944.1; NC_002578.1.
DR   AlphaFoldDB; Q9HKS7; -.
DR   SMR; Q9HKS7; -.
DR   STRING; 273075.Ta0519; -.
DR   PRIDE; Q9HKS7; -.
DR   EnsemblBacteria; CAC11659; CAC11659; CAC11659.
DR   GeneID; 1456117; -.
DR   KEGG; tac:Ta0519; -.
DR   eggNOG; arCOG00407; Archaea.
DR   HOGENOM; CLU_004553_2_0_2; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 24864at2157; -.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 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   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00457; asnS; 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..429
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176489"
SQ   SEQUENCE   429 AA;  49948 MW;  266B477FCC0C32B6 CRC64;
     MLSIAEVSTK AYVGSKVSIR GWVYRIRSSG GVTFVVVRDS SGIIQCTARK NELPEDVYDT
     ISSLGIESSV EFHGTLKEDR RSPSGYEIAV DSFRVYQKND VFPITKDQGE EFLLDNRHLW
     LRSREFTSVL KIRSTIFRSF ADFFYENGYY QVQTPFMVST AVEGGSTLFK VDFFGEPIYL
     NQSAQFYLET MIYSLEKVFT IAPSFRAEKS RTRRHLTEYW HAEAEVAWID NNEMMDIEER
     MIYYIVSRVT EDNEDELKML NRDPEVLKAM KPPFPRIRYS EIIKVANSIG LPLKYGDDLG
     ADEERQITMK YDRPIFVTNY PKDLKPFYMP VDPENPGEVL NHDMLAPEGY GEIIGGSQRI
     WNYDELMQRI REANLDESAY YWYVDLRKYG SVPHSGFGLG LDRLAMWIMH LDNIREAIPY
     PRTIRRTKP