ID   SYDC_PONAB              Reviewed;         501 AA.
AC   Q5R9I5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JUN-2009, entry version 28.
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   Pongo abelii (Sumatran orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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.
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DR   EMBL; CR859403; CAH91575.1; -; mRNA.
DR   RefSeq; NP_001125925.1; -.
DR   UniGene; Pab.19002; -.
DR   GeneID; 100172859; -.
DR   HOVERGEN; Q5R9I5; -.
DR   BRENDA; 6.1.1.12; 269192.
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_0000250735.
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;  57228 MW;  A72C205B15817901 CRC64;
     MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK SDRVLVRVRD LTIQKADEVV
     WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV
     RKVNQKIESC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL
     DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF
     KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
     EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV
     EMGDEDDLST PNEKLLGHLI KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM
     RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF
     LGLHNVRQTS MFPRDPKRLT P
//