ID   SYN_BACTN               Reviewed;         467 AA.
AC   Q8A0Z8;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=BT_3873;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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; AE015928; AAO78978.1; -; Genomic_DNA.
DR   RefSeq; NP_812784.1; NC_004663.1.
DR   RefSeq; WP_008760798.1; NC_004663.1.
DR   AlphaFoldDB; Q8A0Z8; -.
DR   SMR; Q8A0Z8; -.
DR   STRING; 226186.BT_3873; -.
DR   PaxDb; Q8A0Z8; -.
DR   PRIDE; Q8A0Z8; -.
DR   EnsemblBacteria; AAO78978; AAO78978; BT_3873.
DR   GeneID; 60925048; -.
DR   KEGG; bth:BT_3873; -.
DR   PATRIC; fig|226186.12.peg.3937; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_10; -.
DR   InParanoid; Q8A0Z8; -.
DR   OMA; DNMDLAE; -.
DR   Proteomes; UP000001414; 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; IBA:GO_Central.
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..467
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176394"
SQ   SEQUENCE   467 AA;  53295 MW;  4D3F1E9594A5F2EC CRC64;
     MEKIGRTKIV DLLKREDIGA MVNVKGWVRT RRGSKQVNFI ALNDGSTINN VQIVVDLANF
     DEEMLKLITT GACISVNGVM VESVGSGQKV EVQAKEIEVL GTCDNTYPLQ KKGHSMEFLR
     EIAHLRPRTN TFGAVFRIRH NMAIAIHKFF HEKGFFYFHT PIITGSDCEG AGQMFQVTTM
     NLYDLKKDER GSISYDDDFF GKQASLTVSG QLEGELAATA LGAIYTFGPT FRAENSNTPR
     HLAEFWMIEP EVAFNDIADN MDLAEEFIKY CVKWALDNCA DDVKFLNDMF DKGLIERLQG
     VLKDDFVRLP YTDGIKILED AVAKGHKFEF PVYWGVDLAS EHERYLVEEH FKRPVILTDY
     PKEIKAFYMK QNEDGKTVRA MDVLFPKIGE IIGGSEREAD YNKLMTRIEE MHIPMKDMWW
     YLDTRKFGTC PHSGFGLGFE RLLLFVTGMS NIRDVIPFPR TPRNADF