ID   SYDC_BOVIN              Reviewed;         501 AA.
AC   Q3SYZ4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Aspartyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase;
DE            Short=AspRS;
GN   Name=DARS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer; also part of a multisubunit complex that
CC       groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and
CC       Pro (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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; BC103319; AAI03320.1; -; mRNA.
DR   IPI; IPI00715362; -.
DR   RefSeq; NP_001030257.1; -.
DR   UniGene; Bt.48837; -.
DR   Ensembl; ENSBTAG00000009949; Bos taurus.
DR   GeneID; 510162; -.
DR   KEGG; bta:510162; -.
DR   HOVERGEN; Q3SYZ4; -.
DR   BRENDA; 6.1.1.12; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:EC.
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   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; IPR004523; Asp-tRNA-synth_IIb_arc/euk.
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; TIGR00458; aspS_arch; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN         1    501       Aspartyl-tRNA synthetase, cytoplasmic.
FT                                /FTId=PRO_0000245022.
FT   REGION      411    415       Binding site for the 3'-end of tRNA
FT                                (Potential).
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphothreonine; by PKA (Potential).
SQ   SEQUENCE   501 AA;  57036 MW;  A8E00861B2C3E607 CRC64;
     MPSANASRRS QEKPREIMDA AEDYAKERYG VSSMIQSQEK PDRVLVRISD LTVQKAGEVV
     WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV
     RKVNQKIGSC TQQDVELHVQ KIYVISSAEP RLPLQLDDAV RPEVEGEEEG RATVNQDTRL
     DNRVIDLRTS TSQAIFRLQS GICHPFRETL TNKGFVEIQT PKIISAASEG GANVFTVSYF
     KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
     EVVEEIADTL VQIFKGLQKR FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGI
     EMGDEEDLST PNEKLLGRLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM
     RGEEILSGAQ RIHDPQLVTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF
     LGLHNVRQTS MFPRDPKRLT P
//