ID   SYN_LACLA               Reviewed;         447 AA.
AC   Q9CEK9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=LL1828;
GN   ORFNames=L0345;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05926.1; -; Genomic_DNA.
DR   PIR; D86853; D86853.
DR   RefSeq; NP_267985.1; NC_002662.1.
DR   RefSeq; WP_010906156.1; NC_002662.1.
DR   AlphaFoldDB; Q9CEK9; -.
DR   SMR; Q9CEK9; -.
DR   STRING; 272623.L0345; -.
DR   PaxDb; Q9CEK9; -.
DR   EnsemblBacteria; AAK05926; AAK05926; L0345.
DR   KEGG; lla:L0345; -.
DR   PATRIC; fig|272623.7.peg.1958; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_9; -.
DR   OMA; DNMDLAE; -.
DR   Proteomes; UP000002196; 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..447
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176417"
SQ   SEQUENCE   447 AA;  50840 MW;  617D327DD4AC64F4 CRC64;
     MKDLISIIDV KDHVGETVKI GAWVADKSGK GKLQFLQLRD GTAFFQAVVF KPNMIENFGE
     EEGTAKFDEI KHLSQETSVY VTGVVKEDSR SKFGYELDVT DLEVIGQSHD YPITPKEHGV
     EFLLDNRHLW LRSKRQMAMM QVRNAIIYAS YDFFAKNGFI KFDSPILSGN AAENTTELFE
     TDYFGNSAFL SQSGQLYLEA GAMALGRVFD FGPVFRAEKS KTRRHLTEFW MMDAEYPFVT
     HDESLDIQEA YVKALIQGVL DNAAYALETL ERDTSMLQKY IDTPFKRVSY DAAIDLLQAH
     ENDEDTDYEH VEHGDDFGSP HETWISNYYG VPTFIVNYPA SFKAFYMKPV PGNPERVLCA
     DLLAPEGYGE IIGGSERETD YDLLLKKIAD FGLDPKDYDW YLELRKFGSV PHAGFGLGLE
     RMVTFVAGTE HIREAIPFPR MINRIQP