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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 ‘Function’ 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 ‘Function’ 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 ‘Function’ 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 lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
    <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
    DB04239 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One
    DB01825 2-Amino-8-Methylquinazolin-4(3h)-One
    DB03780 2-Aminoquinazolin-4(3h)-One
    DB03304 7-Deaza-7-Aminomethyl-Guanine
    DB03074 7-Deaza-7-Cyano-Guanine
    DB02041 Isoluminol

    <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.<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

    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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P28720

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

    More...
    SMRi
    P28720

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000223473

    KEGG Orthology (KO)

    More...
    KOi
    K00773

    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>.<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 at several positions.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[»]
    ProteinModelPortaliP28720
    SMRiP28720
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP28720
    ChEMBLiCHEMBL2987
    DrugBankiDB04239 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One
    DB01825 2-Amino-8-Methylquinazolin-4(3h)-One
    DB03780 2-Aminoquinazolin-4(3h)-One
    DB03304 7-Deaza-7-Aminomethyl-Guanine
    DB03074 7-Deaza-7-Cyano-Guanine
    DB02041 Isoluminol

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAV88987; AAV88987; ZMO0363
    KEGGizmo:ZMO0363

    Phylogenomic databases

    HOGENOMiHOG000223473
    KOiK00773
    OMAiGIDLFDC

    Enzyme and pathway databases

    UniPathwayi
    UPA00392

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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: December 5, 2018
    This is version 161 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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