ID   D7MB89_ARALL            Unreviewed;       557 AA.
AC   D7MB89;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   06-MAR-2013, entry version 20.
DE   SubName: Full=Putative uncharacterized protein;
GN   ORFNames=ARALYDRAFT_491623;
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47;
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A.,
RA   Schneeberger K., Spannagl M., Wang X., Yang L., Nasrallah M.E.,
RA   Bergelson J., Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X.,
RA   Van de Peer Y., Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome
RT   size change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; GL348719; EFH45600.1; -; Genomic_DNA.
DR   RefSeq; XP_002869341.1; XM_002869295.1.
DR   GeneID; 9303383; -.
DR   KEGG; aly:ARALYDRAFT_491623; -.
DR   KO; K01876; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 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; IPR004523; Asp-tRNA_synthase.
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:SF10; PTHR22594:SF10; 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; TIGR00458; aspS_nondisc; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   557 AA;  63013 MW;  A908E7F4471440B6 CRC64;
     MSSESEIPPS SSTTAPEESG EKISKKAAKK EAAKLEKLRR RQEQDEATRK TASMSLEENE
     EYSSNYGDVT LNELQSTADP KAGKWREAVE GKDWTDVSDL VEEMVESEVL IRGRVHINRP
     TSSKLGFLIL RESGSTVQCV VRQSEKTKVG ANMVKYSEQL SRESFVDVIG VVVLPKEPLT
     GTTQQVEIQV RKVYCINKAL AKLPLSVEDA ARSEADIEKS LQTEKPAARV NQDTRLNHRV
     LDLRTPANQA IFRLQCQVEN SFREKLIFKD FVGIHTPKLM AGSSEGGSAV FRLEYKGQPA
     CLAQSPQLHK QMAICGDLRR VFEVGPVFRA EDSFTHRHLC EFVGLDVEME IRKHYSEIMD
     LVDELFVFIF TSLNEKCKKE LEAVRKQYPF EPLKFLPKTL RLTFEEGVQM LKEAGVEVDP
     LGDLNTESER KLGQLVLEKY NTEFYILHRY PKAVRPFYTM TCADNPLYSN SFDVFIRGEE
     IISGAQRVHI PEILEQRAGE FGIDVKTIST YIDSFRYGAP PHGGFGVGLE RVVMLFCGLN
     NIRKTSLFPR DPQRLAP
//