ID A0A0G1D2E7_9BACT Unreviewed; 359 AA.
AC A0A0G1D2E7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glutamate-tRNA ligase {ECO:0000313|EMBL:KKS91882.1};
DE Flags: Fragment;
GN ORFNames=UV67_C0015G0001 {ECO:0000313|EMBL:KKS91882.1};
OS Parcubacteria group bacterium GW2011_GWC1_43_12.
OC Bacteria.
OX NCBI_TaxID=1618909 {ECO:0000313|EMBL:KKS91882.1, ECO:0000313|Proteomes:UP000034170};
RN [1] {ECO:0000313|EMBL:KKS91882.1, ECO:0000313|Proteomes:UP000034170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007894}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKS91882.1}.
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DR EMBL; LCFJ01000015; KKS91882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1D2E7; -.
DR STRING; 1618909.UV67_C0015G0001; -.
DR PATRIC; fig|1618909.3.peg.488; -.
DR Proteomes; UP000034170; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00464; gltX_bact; 1.
DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363037};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363037};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363037}.
FT DOMAIN 1..199
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 212..355
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKS91882.1"
SQ SEQUENCE 359 AA; 41606 MW; 3B576DCC9E2F571F CRC64;
RRCRKLSKEE IEKKLESGAP YVIRMKIPQG RKIEFDDIVR GKISYNSDEL DDQVLLKSDG
YPTYHLAVVV DDHLMQISHV TRTEEWLPST PKHILLYEYL GWEIPRFAHL PLLLNTDKTK
MSKRKGDVAV EDYIKKGYLP QAMINYLALL GWNPGLSPEV LAKGEHEQEM FSMQELIRNF
DLHKVHKAGA VFDIEKLNWF NSQYLRKFSD EELLEKTRPY LPNTKDFSNE QIIRMLNLEK
ERSATLAAIG ESVKFYFNLP EYESSLLKWK DMADSDIKKS LETSREIISQ TDEQSFTSQK
LSEVFLEKAK GFKNRGELLW PLRASLSGQK FSPPPFDILE ILGKGKSSER INAAIEKIS
//
