ID   SYDND_CAUSK             Reviewed;         609 AA.
AC   B0SWQ6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   04-NOV-2026, entry version 91.
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE            EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044};
DE   AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE            Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE            Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
GN   Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044};
GN   OrderedLocusNames=Caul_2557;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Caulobacterales; Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC       it is able to aspartylate not only its cognate tRNA(Asp) but also
CC       tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first
CC       activated by ATP to form Asp-AMP and then transferred to the acceptor
CC       end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710, Rhea:RHEA-
CC         COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215;
CC         EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00044};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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DR   EMBL; CP000927; ABZ71684.1; -; Genomic_DNA.
DR   SMR; B0SWQ6; -.
DR   STRING; 366602.Caul_2557; -.
DR   KEGG; cak:Caul_2557; -.
DR   eggNOG; COG0173; Bacteria.
DR   HOGENOM; CLU_014330_3_2_5; -.
DR   OMA; AAADLMC; -.
DR   OrthoDB; 9802326at2; -.
DR   CDD; cd00777; AspRS_core; 1.
DR   CDD; cd04317; EcAspRS_like_N; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR   InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR047090; AspRS_core.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF55261; GAD domain-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   NCBIfam; NF001750; aspS; 1.
DR   NCBIfam; TIGR00459; aspS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   AlphaFoldDB; B0SWQ6; -.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..609
FT                   /note="Aspartate--tRNA(Asp/Asn) ligase"
FT                   /id="PRO_1000074694"
FT   REGION          199..202
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         175
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         221
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         468
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         509
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         554..557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   SITE            33
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   609 AA;  68147 MW;  82ECE8C71554B9F0 CRC64;
     MHAYRTHTCG ALRASDTGAS VRVSGWIHRK RDHGGLVFID LRDHYGLTQL VLHPETPGFD
     VVERLRAESV IKIDGEVVAR DAAAVNPNLP TGEIEIRVSA VEVLSEAAEL PLPVFGEPDY
     PEEIRLKHRY LDLRRETLHK NIVLRSRVIQ SIRSRMFAQG FNEFQTPILT ASSPEGARDF
     LVPSRLHPGK FYALPQAPQQ FKQLLMVSGF DRYFQIAPCF RDEDLRADRS LEFYQLDVEM
     SFVTQEDVFA AIEPVMHGVF EEFSAGKPVS PIDGVHTFTN DFGATLEHRG FERLTYAQSM
     AWYGSDKPDL RNPIKMQDVS EHFRDGGFGL FAKILGADPK NRVWAIPAPT GGSRAFCDRM
     NSWAQGEGQP GLGYAFFSKD QNGWGGPIAK NLGEGFQPIA DQLGLTHDDA VFFVAGDPAV
     FAKFAGLART RVGTELKLVD EEQFKFCWIV DFPMFEWNED EKKVDFSHNP FSMPQGGLEA
     LETQDPLTIR AYQYDIVCNG YELCSGAIRN HKPEIMLKAF EVAGYGAEVV EEQFGGMLNA
     FRYGAPPHGG LAPGIDRIVM LLAEQVAIRE VIAFPLNQQG QDLLMNAPAE AQDRQYKELY
     IRSAPPIKV
//