ID   SYD_BORAP               Reviewed;         586 AA.
AC   Q0SN63;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Aspartyl-tRNA synthetase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase;
DE            Short=AspRS;
GN   Name=aspS; OrderedLocusNames=BAPKO_0468;
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-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
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; CP000395; ABH01715.1; -; Genomic_DNA.
DR   RefSeq; YP_709891.1; -.
DR   GeneID; 4227768; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0468.
DR   KEGG; baf:BAPKO_0468; -.
DR   NMPDR; fig|390236.5.peg.508; -.
DR   HOGENOM; Q0SN63; -.
DR   OMA; Q0SN63; VDRRRDH.
DR   BioCyc; BAFZ390236:BAPKO_0468-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-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:0006422; P:aspartyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00044; -; 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; IPR002312; Asp-tRNA-synth_IIb.
DR   InterPro; IPR004524; Asp-tRNA-synth_IIb_bac/mt.
DR   InterPro; IPR018153; Asp-tRNA-synth_IIb_C_bac/mt.
DR   InterPro; IPR004115; GAD.
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   PANTHER; PTHR22594:SF5; AspS_bac; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   TIGRFAMs; TIGR00459; aspS_bact; 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    586       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006640.
SQ   SEQUENCE   586 AA;  68229 MW;  FBE8B893802988DC CRC64;
     MFKVIKCNEL NEKLINKKVE INAWVKKIRH HGKFTFLDIR DRYEKAQVLI TEEHLLKIVE
     KIKLEYCIKI QGLLIKRPSN MINANMTTGY FEILAKNIEI ISKCNELPFM IEDDNNASEN
     SKLKYRYLDL RRDSLKNKII LRCQATHLIR NFLVKRKFLE LETPTFVKST PEGARDFVIP
     SRIHKGSFYA LPQSPQLYKQ LIMIAGFDKY FQIARCYRDE DSRGDRQPEF TQLDLEMSFV
     KKENIFKLIE NMLFSIFKNC LNIKLSKKFK KITYKTAMNK YGSDKPDTRF ELTLQDISRN
     LKNSEFNVFK DILNNKGSIK TLIVKDKADT FSRAKINNLE EIAKLYKTQG LYFTKIENNK
     FSGGIAKFLK TEEQQLIKAY SLENNDIIFF IANNKWEIAC KAMGQIRIKI ANDLGLIDEN
     KFEFLWVYDF PLFEYDENTK TYIPAHHMFS IPKKRYISNL EKNPNKAIGE IYDLVLNGVE
     LGSGSIRIHN KELQQRIFNI IGFQKEKSED RFGFFLKALE YGAPNHGGIA IGIDRLIMLM
     TKSTSIKDVI LFPKNSFAAS PLDNSPSKIS NEQLKELGIN IAPDDT
//