ID   SYD_ANAVT               Reviewed;         614 AA.
AC   Q3MGL3;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Aspartyl-tRNA synthetase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase;
DE            Short=AspRS;
GN   Name=aspS; OrderedLocusNames=Ava_0247;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000117; ABA19873.1; -; Genomic_DNA.
DR   RefSeq; YP_320768.1; -.
DR   GeneID; 3683011; -.
DR   GenomeReviews; CP000117_GR; Ava_0247.
DR   KEGG; ava:Ava_0247; -.
DR   NMPDR; fig|240292.3.peg.730; -.
DR   HOGENOM; Q3MGL3; -.
DR   OMA; Q3MGL3; VDRRRDH.
DR   BioCyc; AVAR240292:AVA_0247-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    614       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_0000235505.
SQ   SEQUENCE   614 AA;  70073 MW;  977CD7F03977C7E1 CRC64;
     MGRLWHSLAN LARKNKLTTM RTHYCGELRQ KDIGETVTLY GWVDRRRDHG GVIFLDLRDR
     SGIVQVVSDP QRTPDSYELA NSLRNEYVVE ITGRVTQRPE ESLNSRIPTG EVEIYADKIE
     LLNGVRKQLP FQVSTADTET VREDLRLKYR YLDLRRDRMA RNIQLRHQVV KAMRRYLEDV
     EGFIEVETPI LTRSTPEGAR DYVLPSRVNP GEWFALPQSP QLFKQILMVS GMDRYYQIAR
     CFRDEDLRAD RQPEFTQLDM EMSFMSEEEI IQLNEKLVSY IFKTVKGVEL PLPFPRLTYA
     EAMERYGCDK PDTRYDLQLV NVSDVMKDSG FKVFRDAVAN GGIVKILPIP NGNEQISNVR
     IKPGGDLFRE ASEAGAKGLA YIRVREDGEI DTIGAIKDNL SEEQKQEILQ RTGAKPGHLL
     LFGAGDAATV NKTLDRLRQA IAKEFGLIDP DKINLLWVVD FPMFEWNADE KRLEALHHPF
     TAPHPDDLHD LKTARAQAYD LVFNGFEVGG GSRRIYQREV QEQVFETIGL SPEEAQNKFG
     FLLEAFEYGT PPHGGIAYGL DRLVMLFAGE ESIRDVIAFP KTQQARCLLT DAPSGVDVKQ
     LKELHVASTY KPKS
//