ID   SYDC_CAEEL              Reviewed;         531 AA.
AC   Q03577;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Aspartate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
GN   Name=dars-1 {ECO:0000312|WormBase:B0464.1};
GN   Synonyms=drs-1 {ECO:0000312|WormBase:B0464.1};
GN   ORFNames=B0464.1 {ECO:0000312|WormBase:B0464.1};
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=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC         Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.12;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 2 subfamily. {ECO:0000305}.
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DR   EMBL; Z19152; CAA79536.1; -; Genomic_DNA.
DR   PIR; S28278; S28278.
DR   RefSeq; NP_499089.1; NM_066688.3.
DR   AlphaFoldDB; Q03577; -.
DR   SMR; Q03577; -.
DR   BioGRID; 41531; 15.
DR   DIP; DIP-59879N; -.
DR   IntAct; Q03577; 1.
DR   STRING; 6239.B0464.1.1; -.
DR   iPTMnet; Q03577; -.
DR   EPD; Q03577; -.
DR   PaxDb; Q03577; -.
DR   PeptideAtlas; Q03577; -.
DR   PRIDE; Q03577; -.
DR   EnsemblMetazoa; B0464.1.1; B0464.1.1; WBGene00001094.
DR   GeneID; 176334; -.
DR   KEGG; cel:CELE_B0464.1; -.
DR   UCSC; B0464.1.1; c. elegans.
DR   CTD; 176334; -.
DR   WormBase; B0464.1; CE00015; WBGene00001094; dars-1.
DR   eggNOG; KOG0556; Eukaryota.
DR   GeneTree; ENSGT01030000234618; -.
DR   HOGENOM; CLU_004553_2_1_1; -.
DR   InParanoid; Q03577; -.
DR   OMA; WVHEIRD; -.
DR   OrthoDB; 677307at2759; -.
DR   PhylomeDB; Q03577; -.
DR   PRO; PR:Q03577; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00001094; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR43450; PTHR43450; 1.
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; TIGR00458; aspS_nondisc; 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..531
FT                   /note="Aspartate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000111013"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..284
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        8..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         259
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         303..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         502..505
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   531 AA;  59939 MW;  094E3207DC102733 CRC64;
     MADAAEGEQP KLSKKELNKL ARKAKKDEKA GEKGGNQQQA AAMDQEDASK DFYGSYGLVN
     SKEKKVLNFL KVKEINVSNA TKDVWVRGRI HTTRSKGKNC FLVLRQGVYT VQVAMFMNEK
     ISKQMLKFVS SISKESIVDV YATINKVDNP IESCTQKDVE LLAQQVFVVS TSAPKLPLQI
     EDASRRAPTD EEKASEQENQ LAVVNLDTRL DNRVIDLRTP TSHAIFRIQA GICNQFRNIL
     DVRGFVEIMA PKIISAPSEG GANVFEVSYF KGSAYLAQSP QLYKQMAIAG DFEKVYTIGP
     VFRAEDSNTH RHMTEFVGLD LEMAFNFHYH EVMETIAEVL TQMFKGLQQN YQDEIAAVGN
     QYPAEPFQFC EPPLILKYPD AITLLRENGI EIGDEDDLST PVEKFLGKLV KEKYSTDFYV
     LDKFPLSVRP FYTMPDAHDE RYSNSYDMFM RGEEILSGAQ RIHDADMLVE RAKHHQVDLA
     KIQSYIDSFK YGCPPHAGGG IGLERVTMLF LGLHNIRLAS LFPRDPKRLT P