ID   SYD_AYWBP               Reviewed;         576 AA.
AC   Q2NIN3;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=AYWB_593;
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-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
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; ABC65710.1; -; Genomic_DNA.
DR   RefSeq; YP_456789.1; -.
DR   GeneID; 3866086; -.
DR   GenomeReviews; CP000061_GR; AYWB_593.
DR   KEGG; ayw:AYWB_593; -.
DR   HOGENOM; Q2NIN3; -.
DR   OMA; Q2NIN3; VDRRRDH.
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; 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; 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    576       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_0000235507.
SQ   SEQUENCE   576 AA;  66679 MW;  3E6068732DD2AB20 CRC64;
     MKTKYSYYNN QLTLIHQGKI VFLKGFIFRK RNLGKTLFFD LRDVSGIVQL LVKENNPQYD
     KIALIKLETV VQIKGQVIER INKNPDLPTG DIEILVSHIE ILSEAQTLPL NVFQSQESLE
     ETRLKYRYLD LRNPEVKHFL IQRHHITQSI RQTLLKNDFL ELETPILSKS TPEGARDYLV
     PSRIYPGNFY ALPQSPQLFK QLYMIAGFER YFQVARCFRD EDLRSDRQPE FSQIDIETSF
     LNQDEIMSLT EEIIVDLFAN IWKKPLLQPF LRLTYQQAFE LYGSDKPDLR NPLKITDFTT
     FFDTNTYSQN IFAGKIKGFK VSKTAFLTRR KLDEYQLFFS KHFNLKLFSF VKKNDKIIGG
     ISQFIQDDSF LKNEEICFVV SGKKDIIHKA LGIFRTKLAL DLSLVDTTQE ALLWIVDFPL
     FETIQEDLSP PNRLYSLHHP FTAPRDATIL KSNPQKALAN AYDLVWNGYE VGGGSLRINN
     HQTQELIFSL LGFLQEEVQN RFGFLIEALK YGTPPHGGIA LGLDRLVMLF TKTNNIKDVI
     AFPKTQSAKD LMLEAPSAVN QEQLNTLKLQ LKCNFN
//