ID   SYNC_BOVIN              Reviewed;         559 AA.
AC   Q2KJG3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 3.
DT   03-AUG-2022, entry version 98.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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; BC105358; AAI05359.1; -; mRNA.
DR   RefSeq; NP_001040037.1; NM_001046572.2.
DR   AlphaFoldDB; Q2KJG3; -.
DR   SMR; Q2KJG3; -.
DR   STRING; 9913.ENSBTAP00000025659; -.
DR   PaxDb; Q2KJG3; -.
DR   PeptideAtlas; Q2KJG3; -.
DR   PRIDE; Q2KJG3; -.
DR   GeneID; 616033; -.
DR   KEGG; bta:616033; -.
DR   CTD; 4677; -.
DR   eggNOG; KOG0555; Eukaryota.
DR   InParanoid; Q2KJG3; -.
DR   OrthoDB; 1056670at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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   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   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..559
FT                   /note="Asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000284071"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43776"
FT   MOD_RES         255
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43776"
FT   MOD_RES         501
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BP47"
SQ   SEQUENCE   559 AA;  64399 MW;  95E21B2DCF629C31 CRC64;
     MSLEVVRAAA GMVLAELYVS DREGNDVTGD GTKEKPFKTG LKALMTVGKE PFPTIYVDSQ
     KENERWDVIS KSQMKNIRKL WHREQMKSES REKKEAEDNL RREKNLEEAK KITIKNDPSL
     PEPKCVKIRE LKGYRGQRIK VFGWVHRLRR QGKNLMFLVL RDGTGFLQCV LSDDLCQCYN
     GVVLSTESSV AVYGVLNLTP KGKQAPGGHE LSCDFWELIG LAPAGGADNL INEESDVDVQ
     LNNRHMMIRG ENMSKILKAR SVITRCFRDH FFDRGYHEIT PPTLVQTQVE GGATLFKLDY
     FGEEAYLTQS SQLYLETCIP ALGDVFCIAQ SYRAEQSRTR RHLAEYTHVE AECPFLTFEE
     LLNRLEDLVC DVVDRVLKSP AGNIVRDLNP NFKPPKRPFK RMNYSDAIVW LKEHNIKKED
     GTFYEFGEDI PEAPERLMTD TINEPILLCR FPVEIKSFYM QRCPEDPRLT ESVDVLMPNV
     GEIVGGSMRI WDNEEILAGY KREGIDPTPY YWYTDQRKYG TCPHGGYGLG LERFLTWILD
     RYHIRDVCLY PRFVQRCKP