Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 176 (29 Sep 2021)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). 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 PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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

Zn2+UniRule annotation10 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation10 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates.1 Publication
  1. KM=0.2 µM for tRNA(Tyr)1 Publication
  2. KM=0.7 µM for guanine1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tRNA-queuosine biosynthesis

This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei102Proton acceptorUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei156SubstrateUniRule annotation1 Publication1
Binding sitei203SubstrateUniRule annotation1 Publication1
Binding sitei230Substrate; via amide nitrogenUniRule annotation1 Publication1
Active sitei280NucleophileUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi318ZincUniRule annotation10 Publications1
Metal bindingi320ZincUniRule annotation10 Publications1
Metal bindingi323ZincUniRule annotation10 Publications1
Metal bindingi349Zinc; via pros nitrogenUniRule annotation10 Publications1

<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 - Molecular functioni

GO - Biological processi

<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

Molecular functionGlycosyltransferase, Transferase
Biological processQueuosine biosynthesis, tRNA processing
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.2.29, 6765

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00392

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 namesi
Recommended name:
Queuine tRNA-ribosyltransferaseUniRule annotation (EC:2.4.2.29UniRule annotation)
Alternative name(s):
Guanine insertion enzymeUniRule annotation
tRNA-guanine transglycosylaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:tgtUniRule annotation
Ordered Locus Names:ZMO0363
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri264203 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesZymomonadaceaeZymomonas
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001173 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi103S → A: Strongly reduces activity. 1 Publication1
Mutagenesisi156D → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi280D → N: Abolishes catalytic activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2987

Drug and drug target database

More...
DrugBanki
DB07452, 2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB04543, 2,6-Diamino-8-(1h-Imidazol-2-Ylsulfanylmethyl)-3h-Quinazoline-4-One
DB04004, 2,6-Diamino-8-(2-Dimethylaminoethylsulfanylmethyl)-3h-Quinazolin-4-One
DB02599, 2,6-Diamino-8-Propylsulfanylmethyl-3h-Quinazoline-4-One
DB03505, 2,6-diaminoquinazolin-4-ol
DB04239, 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One
DB01825, 2-amino-8-methyl-4(1H)-quinazolinone
DB03780, 2-Aminoquinazolin-4(3h)-One
DB02441, 2-Butyl-5,6-Dihydro-1h-Imidazo[4,5-D]Pyridazine-4,7-Dione
DB04169, 3,5-Diaminophthalhydrazide
DB08512, 6-amino-2-[(1-naphthylmethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB07564, 6-amino-2-[(2-morpholin-4-ylethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB08514, 6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB08511, 6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB07012, 6-AMINO-3,7-DIHYDRO-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
DB08267, 6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB07704, 6-AMINO-4-[2-(4-METHOXYPHENYL)ETHYL]-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
DB08268, 6-AMINO-4-[2-(4-METHYLPHENYL)ETHYL]-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
DB03074, 7-cyano-7-deazaguanine
DB03304, 7-Deaza-7-Aminomethyl-Guanine
DB02041, Isoluminol
DB14732, Queuine
DB07481, tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamate

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001355632 – 386Queuine tRNA-ribosyltransferaseAdd BLAST385

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.

UniRule annotation2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
264203.ZMO0363

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P28720

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P28720

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P28720

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni102 – 106Substrate bindingUniRule annotation1 Publication5
Regioni261 – 267RNA bindingUniRule annotation1 Publication7
Regioni285 – 289RNA binding; important for wobble base 34 recognitionUniRule annotation1 Publication5

<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

Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0343, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_022060_0_1_5

Identification of Orthologs from Complete Genome Data

More...
OMAi
GIDLFDC

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.105, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00168, Q_tRNA_Tgt, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004803, TGT
IPR036511, TGT-like_sf
IPR002616, tRNA_ribo_trans-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01702, TGT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51713, SSF51713, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00430, Q_tRNA_tgt, 1 hit
TIGR00449, tgt_general, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P28720-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT
60 70 80 90 100
VKALKPETVR ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL
110 120 130 140 150
TDSGGYQVMS LSSLTKQSEE GVTFKSHLDG SRHMLSPERS IEIQHLLGSD
160 170 180 190 200
IVMAFDECTP YPATPSRAAS SMERSMRWAK RSRDAFDSRK EQAENAALFG
210 220 230 240 250
IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM FRVLDFSVPM
260 270 280 290 300
LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI
310 320 330 340 350
NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN
360 370 380
IAFYQQLMQK IRDSISEGRF SQFAQDFRAR YFARNS
Length:386
Mass (Da):42,843
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i26754E08600BD941
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA27704 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAA27705 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAG29862 differs from that shown. Reason: Erroneous initiation.Curated
The sequence Z11910 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti312T → K (PubMed:7665516).Curated1
Sequence conflicti312T → K (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L33777 Genomic DNA Translation: AAA27704.1 Different initiation.
L33777 Genomic DNA Translation: AAA27705.1 Different initiation.
AF313764 Genomic DNA Translation: AAG29862.1 Different initiation.
AE008692 Genomic DNA Translation: AAV88987.2
Z11910 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
T46898

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAV88987; AAV88987; ZMO0363

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
zmo:ZMO0363

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33777 Genomic DNA Translation: AAA27704.1 Different initiation.
L33777 Genomic DNA Translation: AAA27705.1 Different initiation.
AF313764 Genomic DNA Translation: AAG29862.1 Different initiation.
AE008692 Genomic DNA Translation: AAV88987.2
Z11910 Genomic DNA No translation available.
PIRiT46898

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFZX-ray2.00A1-386[»]
1ENUX-ray1.95A1-386[»]
1F3EX-ray1.85A1-386[»]
1K4GX-ray1.70A1-386[»]
1K4HX-ray1.80A1-386[»]
1N2VX-ray2.10A1-386[»]
1OZMX-ray1.95A2-386[»]
1OZQX-ray1.90A2-386[»]
1P0BX-ray1.70A2-386[»]
1P0DX-ray1.90A2-386[»]
1P0EX-ray2.40A2-386[»]
1PUDX-ray1.85A1-386[»]
1PXGX-ray1.70A2-383[»]
1Q2RX-ray2.90A/B/C/D1-386[»]
1Q2SX-ray3.20A/B/C/D1-386[»]
1Q4WX-ray1.93A1-386[»]
1Q63X-ray1.85A1-386[»]
1Q65X-ray2.10A1-386[»]
1Q66X-ray1.75A1-386[»]
1R5YX-ray1.20A1-386[»]
1S38X-ray1.81A1-386[»]
1S39X-ray1.95A1-386[»]
1WKDX-ray2.60A1-386[»]
1WKEX-ray2.20A1-386[»]
1WKFX-ray2.20A1-386[»]
1Y5VX-ray1.58A2-386[»]
1Y5WX-ray1.58A2-386[»]
1Y5XX-ray2.10A/D2-386[»]
2BBFX-ray1.70A1-386[»]
2NQZX-ray1.46A2-386[»]
2NSOX-ray1.60A1-386[»]
2OKOX-ray1.50A2-386[»]
2POTX-ray1.80A1-386[»]
2PWUX-ray1.77A1-386[»]
2PWVX-ray1.70A1-386[»]
2QIIX-ray1.70A1-386[»]
2QZRX-ray1.95A2-386[»]
2Z1VX-ray1.55A1-386[»]
2Z1WX-ray1.63A1-386[»]
2Z1XX-ray1.63A1-386[»]
2Z7KX-ray1.28A1-386[»]
3BL3X-ray2.25A1-386[»]
3BLDX-ray1.19A1-386[»]
3BLLX-ray1.26A1-386[»]
3BLOX-ray1.60A1-386[»]
3C2YX-ray1.78A1-386[»]
3EOSX-ray1.78A1-386[»]
3EOUX-ray1.93A1-386[»]
3GC4X-ray1.80A1-386[»]
3GC5X-ray1.40A1-386[»]
3GE7X-ray1.50A1-386[»]
3HFYX-ray2.00A1-386[»]
3RR4X-ray1.68A1-386[»]
3S1GX-ray1.82A1-386[»]
3SM0X-ray1.57A1-386[»]
3TLLX-ray1.37A1-386[»]
3UNTX-ray1.80A1-386[»]
3UVIX-ray1.55A1-386[»]
4DXXX-ray1.66A1-386[»]
4DY1X-ray2.04A1-386[»]
4E2VX-ray1.18A1-386[»]
4FPSX-ray1.45A1-386[»]
4FR1X-ray1.74A1-386[»]
4FR6X-ray1.59A1-386[»]
4FSAX-ray1.62A1-386[»]
4GCXX-ray1.42A1-386[»]
4GD0X-ray1.29A1-386[»]
4GG9X-ray1.48A1-386[»]
4GH1X-ray1.45A1-386[»]
4GH3X-ray2.06A1-386[»]
4GHRX-ray2.00A1-386[»]
4GI4X-ray1.97A1-386[»]
4GIYX-ray1.75A1-386[»]
4GKTX-ray1.53A1-386[»]
4H6EX-ray1.42A1-386[»]
4H7ZX-ray1.68A1-386[»]
4HQVX-ray1.66A2-386[»]
4HSHX-ray1.56A2-386[»]
4HTBX-ray1.90A1-386[»]
4HVXX-ray1.82A1-386[»]
4IPPX-ray1.33A1-386[»]
4JBRX-ray2.92A1-386[»]
4KWOX-ray1.32A1-386[»]
4L56X-ray1.70A1-386[»]
4LBUX-ray1.17A1-386[»]
4LEQX-ray1.40A1-386[»]
4PUJX-ray1.42A1-386[»]
4PUKX-ray1.49A1-386[»]
4PULX-ray1.65A1-386[»]
4PUMX-ray1.93A1-386[»]
4PUNX-ray1.25A1-386[»]
4Q4MX-ray1.62A1-386[»]
4Q4OX-ray1.35A1-386[»]
4Q4PX-ray1.54A1-386[»]
4Q4QX-ray1.41A1-386[»]
4Q4RX-ray1.45A1-386[»]
4Q4SX-ray1.25A1-386[»]
4Q8MX-ray1.24A1-386[»]
4Q8NX-ray1.45A1-386[»]
4Q8OX-ray1.89A1-386[»]
4Q8PX-ray1.45A1-386[»]
4Q8QX-ray1.72A1-386[»]
4Q8TX-ray1.40A1-386[»]
4Q8UX-ray1.31A1-386[»]
4Q8VX-ray1.40A1-386[»]
4Q8WX-ray1.14A1-386[»]
5EGRX-ray1.55A1-386[»]
5I00X-ray1.49A1-385[»]
5I02X-ray1.25A1-385[»]
5I03X-ray1.73A1-386[»]
5I06X-ray1.36A1-386[»]
5I07X-ray1.89A/B1-386[»]
5I09X-ray1.44A1-386[»]
5J9MX-ray1.33A1-386[»]
5J9NX-ray1.64A1-386[»]
5J9OX-ray1.41A1-386[»]
5JGMX-ray1.38A1-386[»]
5JGOX-ray1.37A1-386[»]
5JSVX-ray1.17A1-386[»]
5JSWX-ray1.22A1-386[»]
5JT5X-ray1.21A1-386[»]
5JT6X-ray1.54A1-386[»]
5JT7X-ray1.70A1-386[»]
5JXQX-ray1.20A1-386[»]
5LPOX-ray1.42A1-386[»]
5LPPX-ray1.99A1-386[»]
5LPQX-ray2.52A/B1-386[»]
5LPSX-ray1.27A1-386[»]
5LPTX-ray2.36A/B1-386[»]
5N6FX-ray1.12A10-384[»]
5SW3X-ray1.38A10-384[»]
5UTIX-ray1.36A10-384[»]
5UTJX-ray1.55A10-384[»]
5V3CX-ray1.42A10-384[»]
6FMNX-ray1.36A1-386[»]
6FPUX-ray1.36A1-386[»]
6FSOX-ray1.45A10-384[»]
6H7CX-ray1.68A1-386[»]
6RKQX-ray1.67A10-384[»]
6RKTX-ray1.75A10-384[»]
6YFWX-ray1.26A1-386[»]
6YFXX-ray1.38A1-386[»]
6YGKX-ray1.40A1-386[»]
6YGLX-ray1.48A1-386[»]
6YGMX-ray1.23A1-386[»]
6YGOX-ray1.26A1-386[»]
6YGPX-ray1.33A1-386[»]
6YGRX-ray1.70A1-386[»]
6YGSX-ray1.40A1-386[»]
6YGVX-ray1.63A1-386[»]
6YGWX-ray1.16A1-386[»]
6YGXX-ray1.35A1-386[»]
6YGYX-ray1.52A1-386[»]
6YGZX-ray1.86A1-386[»]
6YH1X-ray1.55A1-386[»]
6YH2X-ray1.19A1-386[»]
6YH3X-ray1.49A1-386[»]
6YHDX-ray1.25A1-386[»]
6YHEX-ray1.54A1-386[»]
6YIQX-ray1.58A/B1-386[»]
6YRYX-ray1.82A1-386[»]
6YYZX-ray1.21A1-386[»]
6Z0DX-ray1.65A1-386[»]
7A0BX-ray1.77A1-386[»]
7A3VX-ray1.70A1-386[»]
7A3XX-ray1.85A1-386[»]
7A4KX-ray1.68A1-386[»]
7A4XX-ray2.05A1-386[»]
7A6DX-ray1.59A1-386[»]
7A9EX-ray1.76A1-386[»]
7ADNX-ray1.92A1-386[»]
7APLX-ray1.99A1-386[»]
7APMX-ray1.66A1-386[»]
SMRiP28720
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi264203.ZMO0363

Chemistry databases

BindingDBiP28720
ChEMBLiCHEMBL2987
DrugBankiDB07452, 2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB04543, 2,6-Diamino-8-(1h-Imidazol-2-Ylsulfanylmethyl)-3h-Quinazoline-4-One
DB04004, 2,6-Diamino-8-(2-Dimethylaminoethylsulfanylmethyl)-3h-Quinazolin-4-One
DB02599, 2,6-Diamino-8-Propylsulfanylmethyl-3h-Quinazoline-4-One
DB03505, 2,6-diaminoquinazolin-4-ol
DB04239, 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One
DB01825, 2-amino-8-methyl-4(1H)-quinazolinone
DB03780, 2-Aminoquinazolin-4(3h)-One
DB02441, 2-Butyl-5,6-Dihydro-1h-Imidazo[4,5-D]Pyridazine-4,7-Dione
DB04169, 3,5-Diaminophthalhydrazide
DB08512, 6-amino-2-[(1-naphthylmethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB07564, 6-amino-2-[(2-morpholin-4-ylethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB08514, 6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB08511, 6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB07012, 6-AMINO-3,7-DIHYDRO-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
DB08267, 6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
DB07704, 6-AMINO-4-[2-(4-METHOXYPHENYL)ETHYL]-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
DB08268, 6-AMINO-4-[2-(4-METHYLPHENYL)ETHYL]-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
DB03074, 7-cyano-7-deazaguanine
DB03304, 7-Deaza-7-Aminomethyl-Guanine
DB02041, Isoluminol
DB14732, Queuine
DB07481, tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamate

Genome annotation databases

EnsemblBacteriaiAAV88987; AAV88987; ZMO0363
KEGGizmo:ZMO0363

Phylogenomic databases

eggNOGiCOG0343, Bacteria
HOGENOMiCLU_022060_0_1_5
OMAiGIDLFDC

Enzyme and pathway databases

UniPathwayiUPA00392
BRENDAi2.4.2.29, 6765

Miscellaneous databases

EvolutionaryTraceiP28720

Protein Ontology

More...
PROi
PR:P28720

Family and domain databases

Gene3Di3.20.20.105, 1 hit
HAMAPiMF_00168, Q_tRNA_Tgt, 1 hit
InterProiView protein in InterPro
IPR004803, TGT
IPR036511, TGT-like_sf
IPR002616, tRNA_ribo_trans-like
PfamiView protein in Pfam
PF01702, TGT, 1 hit
SUPFAMiSSF51713, SSF51713, 1 hit
TIGRFAMsiTIGR00430, Q_tRNA_tgt, 1 hit
TIGR00449, tgt_general, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTGT_ZYMMO
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P28720
Secondary accession number(s): Q5NQL7, Q60247, Q9F5L7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 176 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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