ID   SYD1_SYNAS              Reviewed;         723 AA.
AC   Q2LPW5;
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 1;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase 1;
DE            Short=AspRS 1;
GN   Name=aspS1; OrderedLocusNames=SYNAS_04480; ORFNames=SYN_02602;
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; ABC76327.1; -; Genomic_DNA.
DR   RefSeq; YP_460495.1; -.
DR   GeneID; 3885262; -.
DR   GenomeReviews; CP000252_GR; SYNAS_04480.
DR   KEGG; sat:SYN_02602; -.
DR   NMPDR; fig|56780.10.peg.448; -.
DR   HOGENOM; Q2LPW5; -.
DR   OMA; Q2LPW5; NEYAKEI.
DR   BioCyc; SACI56780:SYN_02602-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; atypical; 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    723       Aspartyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000235571.
SQ   SEQUENCE   723 AA;  80508 MW;  A62EAFBD7D3303FF CRC64;
     MPNRGAHFSI SRRKDFLMDF SERVFCGHLT PDHTGRRVLL AGWVDAFRDH GGLLFIHLRD
     RNGIIQIVFS PEAASADVYR QAASLRAEYC VAVQGEVRKR LPGTENPHIE TGDIEVFVSE
     LTVLSESEAL PFAISDKAMV AGASSAGADH VNEDLRMQYR YLDIRRPAMQ KNLILRHRIS
     QCVREFLDSR GFVEVETPVL TMSTPEGARD YLVPSRIHPR SFYALPQSPQ LFKQLLMIGG
     MERYFQLARC FRDEDLRPNR QPEFTQLDIE ASFIDEEFLY ELIEELTVRM FAIGGIALSR
     PFPRMTYAEA MDTTGSDRPD LRFGLRMADV TGVFSRTSYS IFKQILQRGG SIKGINIKGQ
     SEKLSKNVLQ NEYAKEIAPS FGAKGMTWMR AEEGKLESNI VQFFSADELE ALKRVFQVED
     GDVLIMVADP SCAIVNSALG QLRLHLGNRL GLIPEGVFYP VWITEFPLFE PTDEGGVTSS
     HHPFTAPDRT DFDPGNIEEL LSLRSRAYDL VVNGEELGGG SIRINDREVQ RRIFAALGLT
     EEDVKNKFGF FLRAFDFAAP PHGGLALGMD RVVSMILQTP SIREVIAFPK NRSAACPLTG
     APSEVKREQL AELGLLNLGD KDVLPGDAEK EDRIDHLSWV SRIGIAEGER PVMESILAQA
     EELAAQVGDL AGNEEPVRSV APVANRVREG LEAVRLSFSG TGRLLKNAPA VKGDYFKVAG
     ILD
//