CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005572
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamyl-Q tRNA(Asp) synthetase 
Protein Synonyms/Alias
 Glu-Q-RSs 
Gene Name
 gluQ 
Gene Synonyms/Alias
 yadB; b0144; JW5892 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
165GIIHADEKLAREDFIacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis. 
Sequence Annotation
 REGION 19 23 Glutamate binding.
 MOTIF 22 32 "HIGH" region.
 MOTIF 238 242 "KMSKS" region.
 METAL 111 111 Zinc.
 METAL 113 113 Zinc.
 METAL 125 125 Zinc.
 METAL 129 129 Zinc.
 BINDING 55 55 Glutamate.
 BINDING 182 182 Glutamate.
 BINDING 200 200 Glutamate.
 BINDING 241 241 ATP (By similarity).  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Metal-binding; Nucleotide-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 308 AA 
Protein Sequence
MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW LVRIEDIDPP 60
REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHDAYREALA WLHEQGLSYY CTCTRARIQS 120
IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT QFTDQLRGII HADEKLARED FIIHRRDGLF 180
AYNLAVVVDD HFQGVTEIVR GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS 240
KQNHAPALPK GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWRL TAVPESAIVN 300
STFSNASC 308 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; ISS:EcoCyc.
 GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
 GO:0002097; P:tRNA wobble base modification; IDA:EcoCyc. 
Interpro
 IPR022380; Glu-Q_TRNA(Asp)_Synthase.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00749; tRNA-synt_1c 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.