ID   SYD_ANAPZ               Reviewed;         598 AA.
AC   Q2GLD8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=APH_0190;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (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; CP000235; ABD43428.1; -; Genomic_DNA.
DR   RefSeq; YP_504813.1; -.
DR   GeneID; 3930308; -.
DR   GenomeReviews; CP000235_GR; APH_0190.
DR   KEGG; aph:APH_0190; -.
DR   NMPDR; fig|212042.5.peg.183; -.
DR   TIGR; APH_0190; -.
DR   HOGENOM; Q2GLD8; -.
DR   OMA; Q2GLD8; YQLDVEM.
DR   BioCyc; APHA212042:APH_0190-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    598       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006632.
SQ   SEQUENCE   598 AA;  66205 MW;  FDC3C3C7BE94D9F3 CRC64;
     MNMYRTHLCN ALNLSHVGEE VTLSGWIFRK RDHGGILFID LRDFYGITQL VLNESSDQEL
     FNYARSIGLE SVITVKGTVA ARSEDTINTS LSTGHVEVAV HTLVTESAAD ALPIHVPTST
     NHPEDLRLKY RFLDLRCDKV KSNMLLRSAV ISEMRKAMES RGFIEVQTPI LTASSPEGAR
     DYLVPSRVHA GKFYALPQAP QIFKQLLMAS GFDKYFQIAP CFRDEDARAD RSPGEFYQLD
     VEMSFVTQED VFSVMEPVLR DIFTKFAGNR SVSPTFPRIT YKDAMLRYGT DKPDLRNPII
     IADVSEVFLR SNFKTFQEGV ARGMVVRAIP APKTSEHPRS FFDSKVEYAK KIGARGLGYI
     TFSTDNTVKG PVAKFLSDTE LANIQTLAGV GPGDSVFFVS DAADKAAELS GSVRELLGTE
     LNLIEKDTFK FCWIVDFPYF QYENGKLAFS HNPFSMPQGG LDALSSSNPL DIVAYQYDIV
     CNGIEISSGA IRNHKLDILY KAFSMVGYSP EAVDAEFGAL TRAFRFGVPP HGGIAPGVDR
     IVMLLADVPN IREIIYFPLT QMGEDLLMGA PSEVNQSHLK ELSLALNITP KAAGKTSS
//