ID   SYE2_EHRCJ              Reviewed;         443 AA.
AC   Q3YR29;
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 2;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 2;
DE            Short=GluRS 2;
GN   Name=gltX2; OrderedLocusNames=Ecaj_0795;
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; AAZ68826.1; -; Genomic_DNA.
DR   RefSeq; YP_303424.1; -.
DR   GeneID; 3617585; -.
DR   GenomeReviews; CP000107_GR; Ecaj_0795.
DR   KEGG; ecn:Ecaj_0795; -.
DR   HOGENOM; Q3YR29; -.
DR   OMA; Q3YR29; LRLDDTD.
DR   BioCyc; ECAN269484:ECAJ_0795-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    443       Glutamyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000237361.
FT   MOTIF         7     17       "HIGH" region.
FT   MOTIF       236    240       "KMSKS" region.
FT   BINDING     239    239       ATP (By similarity).
SQ   SEQUENCE   443 AA;  51549 MW;  3508EE2D6663FD3D CRC64;
     MITRFAPSPT GYLHVGNVRT ALICWLYVRK QKGKFLLRFD DTDTQRSQEE YIKEIENDLK
     WLNMNWDASF RQSSRFDRYE DVFQYLLKEG FLYPCYESKE ELEFKRKMKL KSGLPPIYDR
     SALNLTQAEK DKYFGRAPYF RFKINQDQLI NWDDEIRGKV SFNPKNISDP IIRRVDGTYT
     YMLPSVIDDM DFNVTHVIRG EDHISNTAVQ IQMLDALKAK VPMFAHLSLL YSDDNKISKR
     VGGSSVKDMQ LYELEPMAIN SYFAKIGTSH PIDVHINMLG LINSFDITAF SQAPTKFNID
     DILKLNPKIL HNMSFDDVKD RLKELKIDKP AFWDFVCGNI EKFSDIEEWI KICSRDMVPV
     VKQDDKDFIT LALNMFPQGE VHDSTWNTWV SNIKQQTDRR GKNLFAPLRL ALTGLAAGPE
     LAKLLPLIGR EEIVRRLSYS VTQ
//