ID   SYN_PHOLL               Reviewed;         466 AA.
AC   Q7N622;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=plu1753;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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:0000255|HAMAP-Rule:MF_00534};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR   EMBL; BX571865; CAE14046.1; -; Genomic_DNA.
DR   RefSeq; WP_011146032.1; NC_005126.1.
DR   AlphaFoldDB; Q7N622; -.
DR   SMR; Q7N622; -.
DR   STRING; 243265.plu1753; -.
DR   PRIDE; Q7N622; -.
DR   EnsemblBacteria; CAE14046; CAE14046; plu1753.
DR   GeneID; 24166876; -.
DR   KEGG; plu:plu1753; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_6; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 1138123at2; -.
DR   BioCyc; PLUM243265:PLU_RS08805-MON; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..466
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176439"
SQ   SEQUENCE   466 AA;  52451 MW;  9D34CE24AFF3B93E CRC64;
     MSVAPVVDVL QGRVAVDSEV TVRGWIRTRR DSKAGISFLA VYDGSCFNPL QAVVNNNLPN
     YQDEVLHLTT GCSVEVTGTV VASLGQGQNF ELQATKIVVI GLVEDPDTYP MAAKRHSIEY
     LREVAHLRPR TNLIGAVARM RHTLAQALHR FFHENGYFWV STPLITAADT EGAGEMFRVS
     TLDLQNLPLT DKGEVDFNQD FFGREAFLTV SGQLNGEAYA CALSKVYTFG PTFRAENSNT
     SRHLAEFWML EPEIAFANLN DAATLAENML KYVFKAALAE RADDLQFFAE RVDKDVITRL
     EKFINSDFAQ IDYTSAIEIL QNCGQKFENP VFWGVDLSSE HERYLAEKHF QAPVVVKNYP
     KDIKAFYMRM NDDGKTVAAL DVLAPGIGEI IGGSQREERL DMLDKRLEEM GLNKEDYWWY
     RDLRRYGTVP HSGFGLGFER LVAYVTGVPN VRDVIPFPRT PRSANF