ID   SYNC_CAEEL              Reviewed;         545 AA.
AC   Q19722;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
GN   Name=nars-1 {ECO:0000312|WormBase:F22D6.3a};
GN   Synonyms=nrs-1 {ECO:0000312|WormBase:F22D6.3a};
GN   ORFNames=F22D6.3 {ECO:0000312|WormBase:F22D6.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23076791; DOI=10.1152/ajpcell.00294.2012;
RA   Lee E.C., Strange K.;
RT   "GCN-2 dependent inhibition of protein synthesis activates osmosensitive
RT   gene transcription via WNK and Ste20 kinase signaling.";
RL   Am. J. Physiol. 303:C1269-1277(2012).
CC   -!- FUNCTION: Involved in protein synthesis (PubMed:23076791). Catalyzes
CC       the specific attachment of an amino acid to its cognate tRNA in a 2
CC       step reaction: the amino acid (AA) is first activated by ATP to form
CC       AA-AMP and then transferred to the acceptor end of the tRNA.
CC       {ECO:0000269|PubMed:23076791, ECO:0000305}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an increase in
CC       the expression of gpdh-1 independent of hypertonic stress.
CC       {ECO:0000269|PubMed:23076791}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; Z71262; CAA95808.1; -; Genomic_DNA.
DR   PIR; T21253; T21253.
DR   RefSeq; NP_001021405.1; NM_001026234.4.
DR   AlphaFoldDB; Q19722; -.
DR   SMR; Q19722; -.
DR   BioGRID; 37887; 2.
DR   STRING; 6239.F22D6.3a; -.
DR   EPD; Q19722; -.
DR   PaxDb; Q19722; -.
DR   PeptideAtlas; Q19722; -.
DR   PRIDE; Q19722; -.
DR   EnsemblMetazoa; F22D6.3a.1; F22D6.3a.1; WBGene00003815.
DR   GeneID; 172442; -.
DR   KEGG; cel:CELE_F22D6.3; -.
DR   UCSC; F22D6.3a.1; c. elegans.
DR   CTD; 172442; -.
DR   WormBase; F22D6.3a; CE05684; WBGene00003815; nars-1.
DR   eggNOG; KOG0555; Eukaryota.
DR   GeneTree; ENSGT01030000234618; -.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   InParanoid; Q19722; -.
DR   OMA; CKQHTVR; -.
DR   OrthoDB; 1056670at2759; -.
DR   PhylomeDB; Q19722; -.
DR   PRO; PR:Q19722; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003815; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IMP:UniProtKB.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 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..545
FT                   /note="Asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000176495"
SQ   SEQUENCE   545 AA;  61186 MW;  53FADA68ECB81BAC CRC64;
     MSKLYIDTDA GSDQHPGTEA QPLATLVQAM LISKNSGEFL MKKKSEEGES WEPAAKAAIK
     KAVKKYEAEV KKLEKAGCRE KEAEEAQHAA LEEAKKITFS LDKSLPEAKV IKIGESVQHR
     DQRVSIKAWV HRLRRQGKSL MFLVLRDGYG FLQCVLNDKL CQSYDAVTLS TETSVQVYGI
     IKALPDGKSA PDGHELTVDY WEVIGKAPAG GIDNVLNESA GVDVMLDNRH LVIRGENASR
     ILRIRAAATR AMRDHFFAAG YTEVAPPTLV QTQVEGGSTL FGLDYYGEPA YLTQSSQLYL
     ETCNAALGDV YCISQSYRAE KSRTRRHLSE YQHVEAECAF ITFDQLMDRI EALVCDTVDR
     LLADPVTKSL IEFVNPGYKA PARPFKRMPY KEAIEWLQKN DVRNEMGEKF VYGEDIAEAA
     ERRMTDTIGV PILLNRFPHG IKAFYMPRCA DDNELTESVD LLMPGVGEIV GGSMRIWKED
     QLLAAFEKGG LDSKNYYWYM DQRKYGSVPH GGYGLGLERF ICWLTDTNHI RDVCLYPRFV
     GRCAP