ID D2NRC2_ROTMD Unreviewed; 341 AA.
AC D2NRC2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 01-MAY-2013, entry version 25.
DE RecName: Full=Glutamyl-Q tRNA(Asp) synthetase;
DE Short=Glu-Q-RSs;
DE EC=6.1.1.-;
GN Name=gluQ; OrderedLocusNames=RMDY18_03660;
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micrococcineae; Micrococcaceae; Rothia.
OX NCBI_TaxID=680646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18;
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate
CC in presence of ATP and the subsequent transfer of glutamate onto a
CC tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-
CC dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the
CC wobble position of the QUC anticodon (By similarity).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. GluQ subfamily.
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DR EMBL; AP011540; BAI64198.1; -; Genomic_DNA.
DR RefSeq; YP_003362018.1; NC_013715.1.
DR ProteinModelPortal; D2NRC2; -.
DR EnsemblBacteria; BAI64198; BAI64198; RMDY18_03660.
DR GeneID; 8693381; -.
DR KEGG; rmu:RMDY18_03660; -.
DR PATRIC; 35271511; VBIRotMuc152186_0316.
DR HOGENOM; HOG000252723; -.
DR KO; K01885; -.
DR OMA; HAWRLDM; -.
DR BioCyc; RMUC680646:GH63-412-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_01428; Glu_Q_tRNA_synth; 1; -.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR022380; Glu-Q_TRNA(Asp)_Synthase.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth_Ib.
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 PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW Metal-binding; Nucleotide-binding; Zinc.
FT REGION 22 26 Glutamate binding (By similarity).
FT MOTIF 25 35 "HIGH" region (By similarity).
FT MOTIF 269 273 "KMSKS" region (By similarity).
FT METAL 132 132 Zinc (By similarity).
FT METAL 134 134 Zinc (By similarity).
FT METAL 153 153 Zinc (By similarity).
FT METAL 157 157 Zinc (By similarity).
FT BINDING 58 58 Glutamate (By similarity).
FT BINDING 213 213 Glutamate (By similarity).
FT BINDING 231 231 Glutamate (By similarity).
FT BINDING 272 272 ATP (By similarity).
SQ SEQUENCE 341 AA; 37106 MW; 8AA11E568011E56D CRC64;
MTSSLTSSST PSNLPFPSGT GRYAPSPSGD LHLGNLRTAI LAWAMARRGG KPFYLRVEDL
DRVRPGAAER QIADLATLGL DWDASPGAPT ERVEGSESTE GKEAGVLYQS TRLAAYEQAV
AQLREANLVY ECFCTRREIQ EASSAPHGAP GAYPGTCREL SKAQREERRT QRPPALRLRA
ECTSYTVQDD FYGTYTGLVD DFVLVRNDGT YAYNLTSVVD DAFVGVEQIV RGDDLLPSAP
RQSYLAQLLG LMQPRYAHVP LALNTEGKRL AKRDGAVTLP QLREAGVEIP RILGWIAASI
PVYNADGSAH SADVPVPNAA AILERFDPAR MASEPWVVRD L
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