Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

The annotation and conditions in this rule are derived from the following entries: Q9BXR0 (TGT_HUMAN), P28720 (TGT_ZYMMO), P0A847 (TGT_ECOLI), Q9JMA2 (TGT_MOUSE)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00168
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 349 - 349 aligns to "H" in entry P28720 Subsequence at position 320 - 320 aligns to "C" in entry P28720 Subsequence at position 318 - 318 aligns to "C" in entry P28720 Subsequence at position 323 - 323 aligns to "C" in entry P28720
  • Subsequence at position 349 - 349 aligns to "H" in entry P28720 (applies "Zinc; via pros nitrogen") Subsequence at position 320 - 320 aligns to "C" in entry P28720 (applies "Zinc") Subsequence at position 318 - 318 aligns to "C" in entry P28720 (applies "Zinc") Subsequence at position 323 - 323 aligns to "C" in entry P28720 (applies "Zinc")
    • Subsequence at position 230 - 230 aligns to "G" in entry P28720 (individually applies "Substrate; via amide nitrogen")
    • Subsequence at position 102 - 106 aligns to "D-S-G-G-[FY]" in entry P28720 (individually applies "Substrate binding")
    • Subsequence at position 280 - 280 aligns to "D" in entry P28720 (individually applies "Nucleophile")
    • Subsequence at position 285 - 289 aligns to "[TA]-[RK]-x(2)-R" in entry P28720 (individually applies "RNA binding; important for wobble base 34 recognition")
    • Subsequence at position 156 - 156 aligns to "D" in entry P28720 (individually applies "Substrate")
    • Subsequence at position 261 - 267 aligns to "G-[VIG]-G-x(4)" in entry P28720 (individually applies "RNA binding")
    • Subsequence at position 203 - 203 aligns to "Q" in entry P28720 (individually applies "Substrate")
    • Subsequence at position 102 - 102 aligns to "D" in entry P28720 (individually applies "Proton acceptor")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namei

  • Recommended name:
    Queuine tRNA-ribosyltransferase catalytic subunit 1 (EC:2.4.2.64)
    Alternative name(s):
    Guanine insertion enzyme
    tRNA-guanine transglycosylase

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi

  • Name:QTRT1
  • Name:tgt-1

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2.
  • Heterodimer of a catalytic subunit and an accessory subunit.

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Nucleophile (to residues corresponding to position 280)
  • Proton acceptor (to residues corresponding to position 102)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Zinc; via pros nitrogen (to residues corresponding to position 349)
  • Zinc (to residues corresponding to position 320)
  • Zinc (to residues corresponding to position 318)
  • Zinc (to residues corresponding to position 323)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • Substrate; via amide nitrogen (to residues corresponding to position 230)
  • Substrate (to residues corresponding to position 156)
  • Substrate (to residues corresponding to position 203)

<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • Substrate binding (to residues corresponding to positions 102 - 106)
  • RNA binding; important for wobble base 34 recognition (to residues corresponding to positions 285 - 289)
  • RNA binding (to residues corresponding to positions 261 - 267)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again