ID   SYE1_ANAPZ              Reviewed;         450 AA.
AC   Q2GLP6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=APH_0072;
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   -!- 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; CP000235; ABD44338.1; -; Genomic_DNA.
DR   RefSeq; YP_504705.1; -.
DR   GeneID; 3930848; -.
DR   GenomeReviews; CP000235_GR; APH_0072.
DR   KEGG; aph:APH_0072; -.
DR   NMPDR; fig|212042.5.peg.69; -.
DR   TIGR; APH_0072; -.
DR   HOGENOM; Q2GLP6; -.
DR   OMA; Q2GLP6; LRLDDTD.
DR   BioCyc; APHA212042:APH_0072-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    450       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000237337.
FT   MOTIF         7     17       "HIGH" region.
FT   MOTIF       236    240       "KMSKS" region.
FT   BINDING     239    239       ATP (By similarity).
SQ   SEQUENCE   450 AA;  51850 MW;  BF90C31A9B4A4ACD CRC64;
     MITRFAPSPT GYMHVGNART ALICWLYARS KSGKFLLRID DTDASRSEHK YIEGIKQDLD
     WLALDWDSCF QQSTRLERYQ EVFDLLLDQG VIYPCYETQE ELDMKRSMML KMGLPPIYDR
     SALKMTEQEM QACSGRLPYF RLKIDQSREI TWEDEVRGRV SFQAKNISDP IIKRTDGTYT
     YMFPSVVDDI DFAITHIIRG EDHVSNTATQ ICIFDILKAK VPVFVHLPLV HFRDAKISKR
     VGSDDIEIRH LRDIGMEPMA IKSYLARMGT SLPVEPQENH DVLVESFDIR TFNQAPIKFS
     LDDISRLNSR IVQCLSFDKV KDRFVQQGLE CTEEFWYLIR DNVNTVEDVR EWINICNSQI
     TTAIDDKDRT FISEAKALLP DTELDEEVCK AWLQRIKETS NRSTRDVLLP LRLATTGVTT
     GPGLAQLLPF IGRAEVVRRL ECASKGHNAN
//