ID   SYN_ALIF1               Reviewed;         466 AA.
AC   Q5E5P2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=VF_1159;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85654.1; -; Genomic_DNA.
DR   RefSeq; WP_011261782.1; NC_006840.2.
DR   RefSeq; YP_204542.1; NC_006840.2.
DR   AlphaFoldDB; Q5E5P2; -.
DR   SMR; Q5E5P2; -.
DR   STRING; 312309.VF_1159; -.
DR   EnsemblBacteria; AAW85654; AAW85654; VF_1159.
DR   KEGG; vfi:VF_1159; -.
DR   PATRIC; fig|312309.11.peg.1166; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_6; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 1138123at2; -.
DR   Proteomes; UP000000537; Chromosome I.
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_1000051454"
SQ   SEQUENCE   466 AA;  52444 MW;  DF1F975EEF182F2D CRC64;
     MTYAPVTDVL SGKLAVDSEV TVRGWIRSRR DSKAGISFLA VYDGSCFDPI QAVVPNDLNN
     YNDEVLKLTT GCSVEVTGTI VASPAKGQDF ELAATEVKVV GWVEDAETYP MAKTRHSIEY
     LREVAHLRPR TNVIGAVARV RNCLSQAIHR FYHEQGYFWM SAPLITASDA EGAGEMFRVS
     TLDHANLPLD DKGNVDYDKD FFGKETFLTV SGQLNAETYA CALSKVYTFG PTFRAENSHT
     SRHLAEFWMV EPEVAFATLD DVAKLAEDML KYVFEAVLAE RRDDLEFFAS RIDKQAITRL
     EQFVSSDFAQ VDYTDAIQIL KDSGRDFEFD VEWGIDMSSE HERYLAEEHF KAPVIVKNYP
     KDIKAFYMRQ NDDGKTVAAM DVLAPGIGEI IGGSQREERL DILDARMIEM GIDPEHMSWY
     RDLRRYGTVP HAGFGLGFER LVSYVTGMGN VRDVIPFPRT PRSANF