ID   SYDM_RAT                Reviewed;         652 AA.
AC   Q3KRD0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Aspartyl-tRNA synthetase, mitochondrial;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase;
DE            Short=AspRS;
DE   Flags: Precursor;
GN   Name=Dars2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; BC105774; AAI05775.1; -; mRNA.
DR   IPI; IPI00372374; -.
DR   RefSeq; NP_001029315.1; -.
DR   UniGene; Rn.137838; -.
DR   PRIDE; Q3KRD0; -.
DR   Ensembl; ENSRNOG00000002813; Rattus norvegicus.
DR   GeneID; 304919; -.
DR   KEGG; rno:304919; -.
DR   NMPDR; fig|10116.3.peg.9359; -.
DR   RGD; 1308286; Dars2.
DR   HOVERGEN; Q3KRD0; -.
DR   OMA; Q3KRD0; VDRRRDH.
DR   BRENDA; 6.1.1.12; 248.
DR   NextBio; 653833; -.
DR   ArrayExpress; Q3KRD0; -.
DR   GermOnline; ENSRNOG00000002813; Rattus norvegicus.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; 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   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Transit peptide.
FT   TRANSIT       1     46       Mitochondrion (Potential).
FT   CHAIN        47    652       Aspartyl-tRNA synthetase, mitochondrial.
FT                                /FTId=PRO_0000250738.
SQ   SEQUENCE   652 AA;  73953 MW;  6CB570CC05F30086 CRC64;
     MYLGSWLNRL GRGLSRPIGK TKQPIWGSLS RSLTLSSQRV PEFSSFVART NTCGELRSSH
     LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA SVRRTLCEAP VESVVRVSGT
     VIARPLGQEN PKMPTGEIEI KAKTAELLNA CKKLPFEIKD FVKKTEALRL QYRYLDLRSS
     QMQHNLRLRS QMVMKMREYL CTLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGRFYSLPQ
     SPQQFKQLLM VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVDQT GIQHLVEGLL
     HYSWPEDKDP LVAPFPSMTF AEALATYGTD KPDTRFGMKI VDISDVFRNT EIRFLQDALA
     KPQGTVKAIC VHEGAKYLRK EDIEFIRKFA AHHFSQEVLP IFLNARKNWS SPFAKFITEE
     ERLELTRLME IQEDDMVLLT AGQHEKACSL LGKLRLECAD LLETRGLALR DPALFSFLWV
     LDFPLFLAKE ESPTELESAH HPFTAPHPGD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSI
     RIHDAQLQRY ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV
     IAFPKSYRGH DLMSNAPDTV SPEDLKPYHI HVSWPTDSEE RASATPSKYL SS
//