ID   SYNC_MACFA              Reviewed;         558 AA.
AC   Q4R4Z1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22 {ECO:0000250|UniProtKB:O43776};
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
DE   AltName: Full=Asparaginyl-tRNA synthetase 1;
GN   Name=NARS1; Synonyms=NARS; ORFNames=QnpA-18508;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-
CC       step reaction: asparagine is first activated by ATP to form Asn-AMP and
CC       then transferred to the acceptor end of tRNA(Asn). In addition to its
CC       essential role in protein synthesis, acts as a signaling molecule that
CC       induced migration of CCR3-expressing cells. Has an essential role in
CC       the development of the cerebral cortex, being required for proper
CC       proliferation of radial glial cells. {ECO:0000250|UniProtKB:O43776}.
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:0000250|UniProtKB:O43776};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43776}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43776}.
CC   -!- DOMAIN: The N-terminal domain (1-77) recruits and activates specific
CC       immune cells by interacting with CCR3-expressing cells.
CC       {ECO:0000250|UniProtKB:O43776}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AB169753; BAE01834.1; -; mRNA.
DR   AlphaFoldDB; Q4R4Z1; -.
DR   SMR; Q4R4Z1; -.
DR   STRING; 9541.XP_005586658.1; -.
DR   eggNOG; KOG0555; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031728; F:CCR3 chemokine receptor binding; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS: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   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..558
FT                   /note="Asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000341690"
FT   REGION          79..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43776"
FT   MOD_RES         254
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43776"
FT   MOD_RES         500
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BP47"
SQ   SEQUENCE   558 AA;  63839 MW;  B484626B81020D17 CRC64;
     MSLEVTRATA GMVLELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK
     ENERWNVISK SQLKNIKKMW HREQMKSESR EKKEAEDSLR REKNLEEAKK ITIKNDPALP
     EPKCVKISAL EGYRGQRVKV FGWVHRLRRQ GKNLMFLVLR DGTGYLQCVL ADELCQCYNG
     VLLSTESSVA VYGMLNLTPK GKQAPGGHEL SCDFWELIGL APAGGADNLI NEESDVDVQL
     NNRHMMIRGE NMSKILKARS MITRCFRDHF FDRGYHEITP PSLVQTQVEG GATLFKLNYF
     GEEAFLTQSS QLYLETCLPA LGDVFCIAQS YRAEQSRTRR HLAEYTHVEA ECPLLTFDDL
     LNRLEDLVCD VVDRILKSPA GSIVYELNPN FQPPKRPFKR MNYSDAIIWL KEHDIKKEDG
     TFYEFGEDIP EAPERLMTDT INEPILLCRF PVEIKSFYMQ RCPEDSCLTE SVDVLMPNVG
     EIVGGSMRTS DAEEILAGYK REGIDPAPYY WYTDQRKYGT CPHGGYGLGL ERFLTWILNR
     YHIRDVCLYP RFVQRCTP