ID   SYN_PARD8               Reviewed;         468 AA.
AC   A6LIA1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=BDI_3727;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR45415.1; -; Genomic_DNA.
DR   RefSeq; WP_012056148.1; NC_009615.1.
DR   AlphaFoldDB; A6LIA1; -.
DR   SMR; A6LIA1; -.
DR   STRING; 435591.BDI_3727; -.
DR   PRIDE; A6LIA1; -.
DR   EnsemblBacteria; ABR45415; ABR45415; BDI_3727.
DR   KEGG; pdi:BDI_3727; -.
DR   PATRIC; fig|435591.13.peg.3683; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_10; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 1138123at2; -.
DR   BioCyc; PDIS435591:G1G5A-3822-MON; -.
DR   Proteomes; UP000000566; 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..468
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_1000051412"
SQ   SEQUENCE   468 AA;  53353 MW;  5FABEE7694285350 CRC64;
     METIKRTKIV DVLKSDAFGT TVNVKGWVRT RRGSKQVNFI ALNDGSTINN VQIVVDVDKL
     GDEFLKPITT GASISVNGIL TQSQGKGQSV EIQATEIEIF GTADPATYPL QKKGHSMEFL
     REIAHLRPRT NTFGAVFRIR HNMAYAIHKF FHDRGFFYFH TPIITASDCE GAGQMFQVTT
     KNLYDLKKDE NGSIIYEDDF FGKQASLTVS GQLEGELAAT ALGQIYTFGP TFRAENSNTP
     RHLAEFWMIE PEVAFNDITD NMELAEEFIK YCVQWALDNC MEDIKFLNDM FDKELIARLE
     GVLKDSFVRL PYTEGIKILE EAVAKGHKFE FPVYWGVDLA SEHERFLVED HFKRPVILTD
     YPKEIKAFYM KQNEDGKTVR AMDVLFPKIG EIIGGSEREA DYDKLMTRID ELGIPMKDMW
     WYLDTRRFGT VPHSGFGLGF ERLLLFVTGM ANIRDVIPFP RTPNNAEF