ID   SYN_BACFR               Reviewed;         467 AA.
AC   Q64P24;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=BF4016;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD50758.1; -; Genomic_DNA.
DR   RefSeq; WP_011203550.1; NC_006347.1.
DR   RefSeq; YP_101292.1; NC_006347.1.
DR   AlphaFoldDB; Q64P24; -.
DR   SMR; Q64P24; -.
DR   STRING; 295405.BF4016; -.
DR   EnsemblBacteria; BAD50758; BAD50758; BF4016.
DR   KEGG; bfr:BF4016; -.
DR   PATRIC; fig|295405.11.peg.3864; -.
DR   HOGENOM; CLU_004553_2_0_10; -.
DR   OMA; DNMDLAE; -.
DR   Proteomes; UP000002197; 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.
FT   CHAIN           1..467
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176389"
SQ   SEQUENCE   467 AA;  53518 MW;  91F4162F29FB76EC CRC64;
     MEKISRTKIV DLMKREDFGA MVNVKGWVRT RRGSKQVNFI ALNDGSTINN VQVVVDLANF
     DEEMLKQITT GACLSVNGVL TESVGAGQKA EVQAREIEVL GTCDNTYPLQ KKGHSMEFLR
     EIAHLRPRTN TFGAVFRIRH NMAIAIHKFF HEKGFFYFHT PIITASDCEG AGQMFQVTTM
     NLYDLKKDEN GSIVYDDDFF GKQASLTVSG QLEGELAATA LGAIYTFGPT FRAENSNTPR
     HLAEFWMIEP EVAFNEIQEN MDLAEEFIKY CVRWALDNCA DDVKFLNDMF DKGLIERLEG
     VLKEDFVRLP YTEGIKILEE AVAKGHKFEF PVYWGVDLAS EHERYLVEDH FKRPVILTDY
     PKEIKAFYMK QNEDGKTVRA MDVLFPKIGE IIGGSERESD YNKLMMRIEE MHIPMKDMWW
     YLDTRKFGTC PHSGFGLGFE RLLLFVTGMS NIRDVIPFPR TPRNADF