ID   SYN_AYWBP               Reviewed;         503 AA.
AC   Q2NIF5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=AYWB_671;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65788.1; -; Genomic_DNA.
DR   RefSeq; YP_456867.1; -.
DR   GeneID; 3865664; -.
DR   GenomeReviews; CP000061_GR; AYWB_671.
DR   KEGG; ayw:AYWB_671; -.
DR   HOGENOM; Q2NIF5; -.
DR   OMA; Q2NIF5; LQKKRHS.
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    503       Asparaginyl-tRNA synthetase.
FT                                /FTId=PRO_1000051375.
SQ   SEQUENCE   503 AA;  58286 MW;  59190A36EDBD1A90 CRC64;
     MKISIKDIFQ KPELFYQKKI LLNGWVRNCR YQKKLIFIDL NDGTFLENLQ IVCKEIKNIE
     TADINEFQEN QKFNNNNKSS NNINLEKLKE ILQIGASLQV EGILKATNNL KTPFEISAQN
     ISLLGTSDFS YPLQPKKHSK VFLRQISHLR VRTKLFGAVF RIRNTAFFAL HSFFQKKGFF
     HINTPIITPN DGEGVGELFQ ITTLNLEVLP QTKNIPNAFK PVNENTSKKG IDYKKDFFGK
     KVFLTVTGQL EAEAMALGLN KVYTFGPTFR SEKSNTTRHA AEFWMLEPEM AFCDLSQNLK
     VAQEMLQFVI SKCLEQNYQD IEFLDKTEKN GLIEELQNIA EEKEFLTVKY EQALEILQKS
     NTKFENPLFY GVDLATEHEK YLTEKHFKKP VFIVDWPKEI KAFYMKNNPD QKTVAAMDLL
     FPRVGELIGG SQREENLSVL IEKMNQMKIS QKDLEWYLDL RRFGGCIHSG FGLGFERLLI
     FLTGLDNIRD VIAFPRTYHN LVF
//