ID   SYE1_EHRCR              Reviewed;         443 AA.
AC   Q2GHQ1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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; Synonyms=gltX-1; OrderedLocusNames=ECH_0208;
OS   Ehrlichia chaffeensis (strain Arkansas).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920;
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   -!- 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; CP000236; ABD45168.1; -; Genomic_DNA.
DR   RefSeq; YP_507032.1; -.
DR   GeneID; 3927352; -.
DR   GenomeReviews; CP000236_GR; ECH_0208.
DR   KEGG; ech:ECH_0208; -.
DR   TIGR; ECH_0208; -.
DR   HOGENOM; Q2GHQ1; -.
DR   OMA; Q2GHQ1; LRLDDTD.
DR   BioCyc; ECHA205920:ECH_0208-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 1.
FT                                /FTId=PRO_0000237362.
FT   MOTIF         7     17       "HIGH" region.
FT   MOTIF       236    240       "KMSKS" region.
FT   BINDING     239    239       ATP (By similarity).
SQ   SEQUENCE   443 AA;  51094 MW;  715A3468A7CA1085 CRC64;
     MITRFAPSPT GYLHVGNVRT ALVCWLYARK QNGKFLLRFD DTDTQRSKDE YIREIENDLV
     WLNINWDSSF RQSSRFDRYE DVFNYLLKEG LIYPCYESKE ELEFKRKMKL KLGLPPIYDR
     SALNLTQAEK DKYSERAPYF RFKIDQNQLI SWNDEVRGKV SFNSENISDP IIRRVDGTYT
     YMLPSIIDDM DFNVTHIIRG EDHISNTAVQ IQMLHALKAS IPIFSHLSLL YSDDNKISKR
     VGGSSVKDMQ SYGLEPMAIN SYFAKIGTSN PVSVHTRMCG LIDSFDITTF SQAPTKFNID
     DVLKLNPKVL CSMSFDDVRN RLQSFNITSP SFWNFVCGNI DKFSDIEGWA KICSGDMIPV
     IGQDDKDFIM LALNMLPQGE VRDNTWNLWI SNIKQHTDRR AKNLFTPLRL ALTGLSTGPE
     LAKLLPLIGR VEIVRRLSYS EVQ
//