ID   SYN_CLOBA               Reviewed;         464 AA.
AC   B2UXS0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=CLH_0134;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP001078; ACD51460.1; -; Genomic_DNA.
DR   RefSeq; WP_012449817.1; NC_010723.1.
DR   AlphaFoldDB; B2UXS0; -.
DR   SMR; B2UXS0; -.
DR   KEGG; cbt:CLH_0134; -.
DR   HOGENOM; CLU_004553_2_0_9; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 1138123at2; -.
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..464
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_1000128204"
SQ   SEQUENCE   464 AA;  53341 MW;  F63ADDFD06982A1A CRC64;
     MKNTVLIKKI YRETDQFLSK EVMISGWIRT LRASNAFGFI EINDGSFFKN IQVVFDDKLG
     NFKEISKLPI SSSISVVGTL VATPDAKQPF EIQAKEIVIE GMSNSDYPLQ KKRHTFEYLR
     SIAHLRPRSN AFSATFRVRS VAAFAIHKFF QEQGFVYTHT PIITGSDCEG AGEMFRVTTL
     DPKAPELTKE GNIDYTKDFF GKETNLTVSG QLNAECFALA FRNIYTFGPT FRAENSNTTR
     HAAEFWMIEP EIAFADLQDD MELAEAMLKY VIKYVMDECP EELQFFNSFV DKGLLERLNH
     VVSSDFAKVT YTEAVEILEK CDKEFDYDVS WGIDLQTEHE RYLTEEHFKK PLFVTDYPKE
     IKAFYMRMNE DNKTVAATDL LVPGIGEIIG GSQREERLDV LEARMAELGL KKEDYWWYLE
     LRKYGETKHA GFGLGFERLI MYITGMTNIR DVIPFPRTPG TSEF