(data stored in ACNUC7421 zone)

HOGENOM: DICZE_1_PE1009

ID   DICZE_1_PE1009                       STANDARD;      PRT;   302 AA.
AC   DICZE_1_PE1009; C6CNI2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase; Short=Glu-Q-RSs; EC=6.1.1
DE   -; (DICZE_1.PE1009).
GN   Name=gluQ; OrderedLocusNames=Dd1591_1031;
OS   DICKEYA ZEAE ECH1591.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICZE_1.PE1009.
CC       Dickeya zeae Ech1591 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6CNI2_DICZE
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.
CC   -!- GENE_FAMILY: HOG000252723 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6CNI2; -.
DR   EMBL; CP001655; ACT05903.1; -; Genomic_DNA.
DR   RefSeq; YP_003003382.1; NC_012912.1.
DR   STRING; C6CNI2; -.
DR   GeneID; 8120304; -.
DR   GenomeReviews; CP001655_GR; Dd1591_1031.
DR   KEGG; dze:Dd1591_1031; -.
DR   OMA; IKRSDGL; -.
DR   ProtClustDB; CLSK2814670; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   HAMAP; MF_01428; Glu_Q_tRNA_synth; 1; -.
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   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 2.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   TIGRFAMs; TIGR03838; Queuosine_YadB; 1.
DR   HOGENOMDNA; DICZE_1.PE1009; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Metal-binding; Nucleotide-binding; Zinc.
SQ   SEQUENCE   302 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSESRPYIGR FAPSPSGDLH FGSLIAALGS YLQARSRHGR WLVRIEDIDP PREVPGAASR
     ILRQLEQYGL FWDGDVAYQS RRHDLYLSVL DELQRQGKCY YCTCTRQRIQ QIGGHYDGHC
     RDRGLPPGNA ALRLRQTHPV VHFHDRLRGQ IDADPMLARE DFIIHRRDGL FAYNLAVVVD
     DHEQGVTDIV RGADLIEPTV RQLSLYQQLN YPAPTYMHLP LALNTDGNKL SKQNHAPALP
     EGDPRAVLAL ALTFLRQPLP AHWRDLDRDA LLAWAVAHWS LSAVPVEAAL TSPEITSAFS
     KG
//

If you have problems or comments...

PBIL Back to PBIL home page