ID   SYE1_EHRCJ              Reviewed;         469 AA.
AC   Q3YS31;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Glutamyl-tRNA synthetase 1;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 1;
DE            Short=GluRS 1;
GN   Name=gltX1; OrderedLocusNames=Ecaj_0432;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16707693; DOI=10.1128/JB.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
RA   Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
RA   Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
RA   Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000107; AAZ68474.1; -; Genomic_DNA.
DR   RefSeq; YP_303072.1; -.
DR   GeneID; 3617778; -.
DR   GenomeReviews; CP000107_GR; Ecaj_0432.
DR   KEGG; ecn:Ecaj_0432; -.
DR   HOGENOM; Q3YS31; -.
DR   OMA; Q3YS31; MARYDAN.
DR   BioCyc; ECAN269484:ECAJ_0432-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00022; -; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ic_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    469       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000237360.
FT   MOTIF        11     21       "HIGH" region.
FT   MOTIF       238    242       "KMSKS" region.
FT   BINDING     241    241       ATP (By similarity).
SQ   SEQUENCE   469 AA;  53980 MW;  F265F659A7DB3D4A CRC64;
     MSHDVITRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDKKR SSQELIDSII
     NAMSWLKIHY DGKAVLQSEN ISRHVEIANQ LMLNNKAYYC YCSEEEINKE KEESAKKGLY
     YKHNCIWKNK SAPNSNITRV VRLKSPTDGV TSFDDEVYGN ITVNNSQLDD MILLRSDNTP
     TYLLSVVVDD HDMNISHIIR GTDHLTNTAR QLLIYNALEW DPPKFAHIPL IHDENGNKLS
     KRHQAIGIHE YKNSGILPEA IFNYLLRMGW SHENDEVITI DQAIRWFSIE GIGQSPSRLD
     SKKLEFLNNH YINITDNETI LNMIIPIIEE KTGHIITDVK KGYLLKGLSE LKKRTKNLVN
     LAKESLFYVE DIPISIDQES ITVIKDYKHI FSILYDNLSK ISEKDWNHNI LMSIIKDISC
     NLEVKISIVY HCLRASITGR MNAPSIIEIM INLQHKECLQ RIKYALDVI
//