ID   SYN_UREP2               Reviewed;         454 AA.
AC   B1AJ04;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=UPA3_0381;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000942; ACA32990.1; -; Genomic_DNA.
DR   RefSeq; WP_006688779.1; NC_010503.1.
DR   AlphaFoldDB; B1AJ04; -.
DR   SMR; B1AJ04; -.
DR   EnsemblBacteria; ACA32990; ACA32990; UPA3_0381.
DR   GeneID; 29672210; -.
DR   KEGG; upa:UPA3_0381; -.
DR   HOGENOM; CLU_004553_2_0_14; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 1138123at2; -.
DR   Proteomes; UP000002162; 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: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   Pfam; PF00152; tRNA-synt_2; 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..454
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_1000081861"
SQ   SEQUENCE   454 AA;  52314 MW;  8851BF08F7149DEE CRC64;
     MQLKIKEIFN QDYVKLEGQK IQIKAWVRSN RDSKKIGFLV LNDGSSLTNL QAVYRVDKID
     NYEEIAAARM WAAVVIEGVI KLTPTAKQPL ELEVLNAQIL KQSDEDFLLS NNDLNLETLR
     LNAHLRPRTN LFHAIMKVRA TLAFAVHEFM NQNEYSWLAA PLFTGNDAEG AGETFSIQKF
     DNEEFFGKQT HLSVTGQLQA EAYAQAFGNV YTFGPTFRAE KSHTNRHLAE FWMIEPEMAF
     VDLKGMQDIV EDLVKHVIKA VLEKNQQELE FLAQRNDENL IKKLQKVVES KFERIEYKDA
     VKILADAVKN GHQFENNEIF FGMDLGSEHE RYMCETYHQG PVFLQNYPKD IKAFYMKLND
     DQQTVASTDL LIPGVGELVG GSQREDSYEK LLKRCQELKM PIESLQWYLD LRRFGYYMSS
     GFGIGFERLV MYVTGVNNIK DTIPFPRSHG QIEF