ID   SYDND_CHLCH             Reviewed;         605 AA.
AC   Q3AS30;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   18-JUN-2025, entry version 117.
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=Cag_0932;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
OC   Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) 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}.
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; CP000108; ABB28195.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AS30; -.
DR   SMR; Q3AS30; -.
DR   STRING; 340177.Cag_0932; -.
DR   KEGG; cch:Cag_0932; -.
DR   eggNOG; COG0173; Bacteria.
DR   HOGENOM; CLU_014330_3_2_10; -.
DR   OrthoDB; 9802326at2; -.
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   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   NCBIfam; TIGR00459; aspS_bact; 1.
DR   NCBIfam; NF001750; PRK00476.1; 1.
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   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.
FT   CHAIN           1..605
FT                   /note="Aspartate--tRNA(Asp/Asn) ligase"
FT                   /id="PRO_0000235519"
FT   REGION          210..213
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         186
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         232..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         232
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         460
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         501
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         546..549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   SITE            43
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   605 AA;  68899 MW;  A5A128C0A2EC8FC4 CRC64;
     MSNPVEQQVV CNRFRSHSCG LLNATFEQQH VRLAGWVHRK RDHGGLIFID LRDHTGICQL
     VIQPEQQALF AEAEHLHNES VISVEGTVIL RAENAINPRL SSGEIEVVIS CMSIESNAHP
     LPFSVADELP TSEELRLKYR FLDLRREKLH ENIIFRSRLT AAVRRYLEEK NFTEIQTPIL
     TSSSPEGARD FLVPSRLHPG KFYALPQAPQ QFKQLLMVAG FPRYFQIAPC FRDEDARADR
     SPGEFYQLDM EMAFIEQENL FEILEGMLEH ITSTMSKKRI TQVPFPRISY RDVMNRFGTD
     KPDLRIPLEI QDVTSLFVDS GFKVFAKNTV PGCCVKALVV KGRGNESRLF YDKAEKRAKE
     LGSAGLAYIQ FKDEGAKGPL VKFLSEDDMN ALKQHLNLEQ GDVVFFGAGK WEVTCKIMGG
     MRNYFADLFT LDKDELSFCW IVDFPMYEYN EEAKKIDFSH NPFSMPQGEM EALETKDALD
     ILAYQYDIVC NGIELSSGAI RNHKPEIMYK AFAIAGYSRE EVDQRFGHMI EAFKLGAPPH
     GGIAPGLDRL VMILCDEQNI REVIAFPMNQ QAQDLMMSAP SEVTLAQLRE LHLKVELPKK
     EEKKG
//