ID   G2K607_LISMN            Unreviewed;       430 AA.
AC   G2K607;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-APR-2013, entry version 12.
DE   RecName: Full=Asparagine--tRNA ligase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
GN   Name=asnS; ORFNames=LMKG_00439;
OS   Listeria monocytogenes FSL R2-561.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=393126;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FSL R2-561;
RA   Borowsky M., Young S.K., Zeng Q., Koehrsen M., Fitzgerald M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA   Walk T., White J., Yandava C., Borodovsky M., Wiedmann M.,
RA   Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C.,
RA   Higgins D., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Listeria monocytogenes strain FSL R2-561.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP002003; AEO26243.1; -; Genomic_DNA.
DR   RefSeq; YP_005968863.1; NC_017546.1.
DR   ProteinModelPortal; G2K607; -.
DR   EnsemblBacteria; AEO26243; AEO26243; LMKG_00439.
DR   GeneID; 12560167; -.
DR   KEGG; lmg:LMKG_00439; -.
DR   KO; K01893; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 1; -.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004522; Asn-tRNA-ligase_IIb.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF6; PTHR22594:SF6; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 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.
SQ   SEQUENCE   430 AA;  48999 MW;  70B97F2A85BABAAA CRC64;
     MKITINQASE FVGKEVTIGA WLANKRSSGK IAFLQLRDGT GFMQGVVVKA EVGDDIFATA
     KALTQETSLY VTGTINEDTR SPFGYEMAVS SVEVISESHD YPITPKEHGT EFLMDHRHLW
     LRSNRQHAIM KIRNEIIRAS YEFFNKEGFL KIDPPILTGS APEGTTELFH TKYFEEDAFL
     SQSGQLYMEA AAMAFGKVFS FGPTFRAEKS KTRRHLIEFW MIEPEMAFYK LEDSLQVQEN
     YVAFLVKAVL DNCRLELDRL GRDVSHLEKM VAPFPRITYT EAIERLHELG FDDIVWGDDF
     GAPHETAIAD SFEKPVFITH YPKAIKPFYM PEDPENDQVV LCADMIAPEG YGEIIGGSER
     IHDLETLQAR MEDFDLDQEA YSWYLDLARY GSVPHSGFGL GLERTVAWIS GTEHVRETIP
     FPRLLNRLYP
//