ID   SYD_BARHE               Reviewed;         596 AA.
AC   Q6G330;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 37.
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=BH09790;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27772.1; -; Genomic_DNA.
DR   RefSeq; YP_033770.1; -.
DR   GeneID; 2866084; -.
DR   GenomeReviews; BX897699_GR; BH09790.
DR   KEGG; bhe:BH09790; -.
DR   NMPDR; fig|283166.1.peg.898; -.
DR   HOGENOM; Q6G330; -.
DR   OMA; Q6G330; YQLDVEM.
DR   BioCyc; BHEN283166:BH09790-MON; -.
DR   BRENDA; 6.1.1.12; 277357.
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    596       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_0000110831.
SQ   SEQUENCE   596 AA;  67626 MW;  BEFD90DE89257CED CRC64;
     MHRYRSHHCA ALRKCDVGIK ARLSGWVHRV RDHGGILFVD LRDHFGITQI VADPASPAFK
     IIEKVRSEWV IRVDGEVRAR SDEVINTSLP TGEIEIFAKE VEILSKSDEL PLPVFGEPDY
     PEDIRLKYRF LDLRRETMHR NIMRRTEIIA AIRRSMQENG FTEFTTPLLT ASSPEGARDF
     LVPSRIHQGK FYALPQAPQQ YKQLLMMSGF DRYFQIAPCF RDEDPRADRL PGEFYQLDVE
     MSFVEQEDVL VTMEPIMRSL FEEFADGKPV TQSFPRLSYE EAMRKYGSDK PDLRNPIIME
     DVSQHFYDSG FKVFAQILAN DENARVWAIP AKTGGSRAFC DRMNGWAQSE GQPGLGYIFW
     REEQGKFEGA GPIAKNIGEQ RTEALRMQLG LENGDACFFV AGDPKKFLPF AGAARTRVGE
     ELDLVDRDCF SLAWIVDFPF FEWNEEEKKL DFAHNPFSMP QGGKDALECQ DPLTLKAFQY
     DLVCNGYEIA SGGIRNHSPE MMLKVFNLAG LSKEVVEDRF GGLYRAFHYG APPHGGMAAG
     VDRIIMLLQG VKNLREVALF PMNQQALDLL MSAPSDVSPV QLRDLGIRIA PAAKND
//