ID   SYD2_SYNAS              Reviewed;         591 AA.
AC   Q2LTE0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Aspartyl-tRNA synthetase 2;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase 2;
DE            Short=AspRS 2;
GN   Name=aspS2; OrderedLocusNames=SYNAS_14750; ORFNames=SYN_02535;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A.,
RA   Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.;
RT   "The genome of the syntrophic bacterium Syntrophus aciditrophicus:
RT   Life dependent on negative change in electrical potential.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000252; ABC77354.1; -; Genomic_DNA.
DR   RefSeq; YP_461522.1; -.
DR   GeneID; 3884913; -.
DR   GenomeReviews; CP000252_GR; SYNAS_14750.
DR   KEGG; sat:SYN_02535; -.
DR   NMPDR; fig|56780.10.peg.1464; -.
DR   HOGENOM; Q2LTE0; -.
DR   OMA; Q2LTE0; VDRRRDH.
DR   BioCyc; SACI56780:SYN_02535-MON; -.
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; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    591       Aspartyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000235572.
SQ   SEQUENCE   591 AA;  67123 MW;  271B104C5AC7CC8A CRC64;
     MSDFITIKKR THYCGQLDSS DSGKEVILMG WVHRRRDHGG VIFVDFRDRE GLVQIVFNPE
     YSPVAHQEAH KIRSEYVLAV RGAVRNRPEG MVNPDMKTGA IEVMVEELEI LNESQTPPFS
     LESESDISEN IRLKYRYLDL RRPQIQRNIM LRNRVAAETR QFFQSNGFIE IETPFLTKST
     PEGARDYLVP SRINKGTFYA LPQSPQIFKQ LLMVSGFDRY FQIVKCFRDE DLRADRQPEF
     TQIDVEMSFI TEDDIIEIME GLMTHLFSRC LNRTFSTPFP RLSYAEAIGR YGKDNPDIRF
     GLELRDLTDI LADSGLTVFR EAAAGGGMIK AIRIPEGKRL SRKDLDDLQN FVSIYGARGL
     AWARVLADGW TSPIFKFLTA DEVRQINGRM EAVEGDVLVF VADTPTVVND SLGNLRIHLA
     KKLNLIDPEQ FAFVWITEFP LMEFSDTEKR YVSTHHPFTS PVPDDVKYLP GEPGKVRARA
     YDLVLNGSEV GGGSIRIHRK EIQSLIFEAL GLENEEVRSK FGFLLDALEF GTPPHGGIAF
     GLDRLVMMMT GAESIRDVIA FPKTQKATCL MTDAPSRVSI EQLMELSLKI V
//