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Database: UniProt/SWISS-PROT
Entry: SYE1_JANSC
LinkDB: SYE1_JANSC
Original site: SYE1_JANSC 
ID   SYE1_JANSC              Reviewed;         470 AA.
AC   Q28RA3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   01-OCT-2014, entry version 66.
DE   RecName: Full=Glutamate--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS 1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=Jann_1842;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E.,
RA   Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A.,
RA   Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00022}.
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DR   EMBL; CP000264; ABD54759.1; -; Genomic_DNA.
DR   RefSeq; WP_011454964.1; NC_007802.1.
DR   RefSeq; YP_509784.1; NC_007802.1.
DR   ProteinModelPortal; Q28RA3; -.
DR   STRING; 290400.Jann_1842; -.
DR   EnsemblBacteria; ABD54759; ABD54759; Jann_1842.
DR   GeneID; 3934293; -.
DR   KEGG; jan:Jann_1842; -.
DR   PATRIC; 22147416; VBIJanSp43325_1975.
DR   eggNOG; COG0008; -.
DR   HOGENOM; HOG000252722; -.
DR   KO; K01885; -.
DR   OMA; AMGWEVP; -.
DR   OrthoDB; EOG6DRPF7; -.
DR   BioCyc; JSP290400:GI1R-1857-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.1160.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR10119; PTHR10119; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; SSF48163; 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; Reference proteome.
FT   CHAIN         1    470       Glutamate--tRNA ligase 1.
FT                                /FTId=PRO_0000330975.
FT   MOTIF        15     25       "HIGH" region.
FT   MOTIF       241    245       "KMSKS" region.
FT   BINDING     244    244       ATP. {ECO:0000255|HAMAP-Rule:MF_00022}.
SQ   SEQUENCE   470 AA;  51878 MW;  EF92569AE1D3EFEE CRC64;
     MSSDAASPVV TRIAPSPTGT MHIGTARTGL FNWLFARKHG GKFVLRIEDT DRERSTPEAT
     QAILDGMAWL GLDYDGEAVS QFARADRHRE VAEQMLAEGH AYKCFSTQDE IAAFRDAAKA
     DGRSTLFLSP WREASDHPDA PYVIRLKAPR DGTTVIRDRV QSDVTIQNAT LDDMILLRSD
     GTPTYMHAVV VDDHDMGVTH VVRGDDHLNN AARQIQIYAA MGWAEPVWSH IPLIHGDDGK
     KLSKRHGATG VMEYAEMGIP AAAMRNYLTR LGWSHGDEEL FTDEQARDWF DLDGIGKSPS
     RLDMKKLANV TGWHIARTDD ADLVAQIEGY LALTGAPALS QAQHDGLTRA MYCLKDRAKS
     LPDLLDKGRF VLENRPFDYD EKSVTMLDPV SRSILRELTA QLQNARWTRD TLEGVLNAAA
     DSHGLKFGKL AGPLRAALSG RSVSPSVFDM MLVIGRDETL ARLDEAASLT
//
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