ID   SYN_BORAP               Reviewed;         462 AA.
AC   Q0SP63;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Asparaginyl-tRNA synthetase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparagine--tRNA ligase;
DE            Short=AsnRS;
GN   Name=asnS; OrderedLocusNames=BAPKO_0102;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000395; ABH01365.1; -; Genomic_DNA.
DR   RefSeq; YP_709541.1; -.
DR   GeneID; 4227349; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0102.
DR   KEGG; baf:BAPKO_0102; -.
DR   NMPDR; fig|390236.5.peg.166; -.
DR   HOGENOM; Q0SP63; -.
DR   OMA; Q0SP63; LQKKRHS.
DR   BioCyc; BAFZ390236:BAPKO_0102-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro.
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   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00534; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004522; Asn-tRNA-synth_IIb.
DR   InterPro; IPR002312; Asp-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA_bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   TIGRFAMs; TIGR00457; asnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    462       Asparaginyl-tRNA synthetase.
FT                                /FTId=PRO_1000051382.
SQ   SEQUENCE   462 AA;  53039 MW;  6E71F055E9993DB7 CRC64;
     MFASIKDILE NPILNSNVTI NGWIRTKRSN GKIGFIEIND GSTLKGIQAV INEEENQFDE
     KDLKNLTTGA SISLTGLLVE SPAKGQNYEI KTCGFNVIGE ADPKTYPLQK KRHTFEFLRE
     IPHLRIRTNT FGAVARVRSK ISYKIHEYFQ KNGFFYINTP IITSNDGEGA GEMFRVSTLK
     FNKPNNDLGN IDFKDDFFGK EAFLSVTGQL HGEAYAMALS KIYTFGPTFR AENSNTTRHA
     SEFWMIEPEM AFYKLNDNIT LAEDLLKYLL SSILNECSQD MDFLENYIEK GLIKKLENVI
     NSNFEVITYT KAIEILESSK KNFEIKPYWG IDLQTEHERF LTEETFKKPV VVIDYPKNFK
     AFYMKINKDN KTVKGMDVLV PKIGEIIGGS EREDNLQKLE NRIKELNLSI EHLNWYLDLR
     RFGSTPHSGF GLGLERFVQY STGISNIRDS IPFPRTPKNL YF
//