Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Due to a server migration, the UniProt 'ID mapping', 'Peptide search' and 'community bibliography submission' tools will not be available on the 19th April 2021 during the morning (EST).
Entry version 84 (02 Dec 2020)
Sequence version 1 (24 May 2005)
Previous versions | rss
Add a publicationFeedback
Protein

4-hydroxy-2-oxovalerate aldolase

Gene

TTHB246

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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 retro-aldol cleavage of both 4-hydroxy-2-oxopentanoate (HOPA) and 4-hydroxy-2-oxohexanoate (HOHA) to pyruvate and acetaldehyde or propanaldehyde, respectively. The aldehydes produced by this reaction are directly channeled to the dehydrogenase TTHB247, ensuring that these toxic aldehydes are sequestered from cellular components. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds. Appears to be stereospecific since it can cleave (4S)-4-hydroxy-2-oxopentanoate but not the (4R) isomer. Is not able to catalyze the aldol addition of 2-oxobutyrate with acetaldehyde; this indicates that the enzyme is specific for pyruvate as the carbonyl donor.1 Publication

<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 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

Co2+1 Publication, Ni2+1 Publication, Mn2+1 PublicationNote: Divalent metal cation. Has the highest activity with Co2+ as cofactor, followed by Ni2+ and Mn2+. Mg2+ and Ca2+ are very poor metal cofactors.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Appears to be allosterically activated by NADH.1 Publication

<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

The catalytic efficiency is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate. In the presence of NADH, exhibits a 2-fold increase in kcat.
  1. KM=206 µM for 4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)1 Publication
  2. KM=41 µM for 4-hydroxy-2-oxopentanoate (in the presence of NADH and in complex with the dehydrogenase TTHB247, at pH 8 and 25 degrees Celsius)1 Publication
  3. KM=123 µM for 4-hydroxy-2-oxopentanoate (in the absence of NADH and in complex with the dehydrogenase TTHB247, at pH 8 and 25 degrees Celsius)1 Publication
  4. KM=210 µM for 4-hydroxy-2-oxohexanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)1 Publication
  5. KM=37 µM for 4-hydroxy-2-oxopentanoate (in the presence of NADH and in complex with the dehydrogenase TTHB247, at pH 8 and 25 degrees Celsius)1 Publication

    Temperature dependencei

    Has a half-life of 42 hours at 50 degrees Celsius. When TTHB246 is in complex with TTHB247, its half-life is reduced by approximately 30 hours.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei19Transition state stabilizerUniRule annotation1
    <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 bindingi20ManganeseUniRule annotation1
    <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 sitei23Proton acceptorUniRule annotation1
    <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 sitei173SubstrateUniRule annotation1
    Metal bindingi201Manganese; via tele nitrogenUniRule annotation1
    Binding sitei201SubstrateUniRule annotation1
    Metal bindingi203Manganese; via tele nitrogenUniRule annotation1
    Binding sitei292SubstrateUniRule annotation1

    <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 functionAllosteric enzyme, Lyase
    Biological processAromatic hydrocarbons catabolism
    LigandCobalt, Manganese, Metal-binding, Nickel

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.3.43, 2305

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q53WI0

    <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%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 namesi
    Recommended name:
    4-hydroxy-2-oxovalerate aldolaseUniRule annotation (EC:4.1.3.39UniRule annotation1 Publication)
    Short name:
    HOAUniRule annotation
    Alternative name(s):
    4-hydroxy-2-keto-pentanoic acid aldolaseUniRule annotation
    4-hydroxy-2-oxohexanoate aldolase (EC:4.1.3.431 Publication)
    4-hydroxy-2-oxopentanoate aldolaseUniRule annotation
    <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
    Ordered Locus Names:TTHB246
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pTT27
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri300852 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000000532 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Plasmid pTT27

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi324A → G: Increases the channeling efficiency of propanaldehyde from 57% to 94%. 1 Publication1

    <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 '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_00003879281 – 3474-hydroxy-2-oxovalerate aldolaseAdd BLAST347

    <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%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

    Homodimer. Can also form a heterotetramer composed of two aldolase (TTHB246) and two dehydrogenase (TTHB247) subunits. Upon complex formation, the aldolase shows a 5-fold increase in substrate affinity, while the dehydrogenase shows a 3-fold decrease; the kcat values of each enzyme are reduced by 2-fold when they are in a complex.

    1 Publication

    <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

    3D structure databases

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

    More...
    SMRi
    Q53WI0

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini11 – 262Pyruvate carboxyltransferaseUniRule annotationAdd BLAST252

    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>Regioni19 – 20Substrate bindingUniRule annotation2

    <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 4-hydroxy-2-oxovalerate aldolase family.UniRule annotationCurated

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_049173_0_0_0

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DLYKMMD

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q53WI0

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd07943, DRE_TIM_HOA, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.70, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01656, HOA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017629, 4OH_2_O-val_aldolase
    IPR013785, Aldolase_TIM
    IPR012425, DmpG_comm
    IPR035685, DRE_TIM_HOA
    IPR000891, PYR_CT

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07836, DmpG_comm, 1 hit
    PF00682, HMGL-like, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03217, 4OH_2_O_val_ald, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50991, PYR_CT, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    Q53WI0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSWDLSTAKP PVVVDTTLRD GSHAHRHQYT VEEARAIAQA LDEAGVYAIE
    60 70 80 90 100
    VSHGDGLGGS SLQYGFSRTD EMELIRAVRE TVRRAKVAAL LLPGIGTRKE
    110 120 130 140 150
    LKEAVEAGIQ MVRIATQCTE ADISEQHFGM AKEMGLEAVG FLMMSHMRPP
    160 170 180 190 200
    EFLAEQARLM EGYGADVVYI VDSAGAMLPE DAYARVKALK EALSRAKVGF
    210 220 230 240 250
    HAHNNLGLAI GNTLAALAAG ADWVDATLRG YGAGAGNAPL EVLAAVLDKA
    260 270 280 290 300
    GLNPGLDVFK LLDAAEYVMG PILHFQPYPD RDSVAIGYAG VYSTFLLHAK
    310 320 330 340
    RIGKELGVDP LAILLELGRR QAVAGQEDWI LRVALELKEK EAGALAD
    Length:347
    Mass (Da):37,214
    Last modified:May 24, 2005 - v1
    <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:i3E9DC806D6EAC64D
    GO

    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
    AP008227 Genomic DNA Translation: BAD72042.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011229063.1, NC_006462.1
    YP_145485.1, NC_006462.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAD72042; BAD72042; BAD72042

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3169557

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ttj:TTHB246

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|300852.9.peg.2202

    <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
    AP008227 Genomic DNA Translation: BAD72042.1
    RefSeqiWP_011229063.1, NC_006462.1
    YP_145485.1, NC_006462.1

    3D structure databases

    SMRiQ53WI0
    ModBaseiSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD72042; BAD72042; BAD72042
    GeneIDi3169557
    KEGGittj:TTHB246
    PATRICifig|300852.9.peg.2202

    Phylogenomic databases

    HOGENOMiCLU_049173_0_0_0
    OMAiDLYKMMD
    PhylomeDBiQ53WI0

    Enzyme and pathway databases

    BRENDAi4.1.3.43, 2305
    SABIO-RKiQ53WI0

    Family and domain databases

    CDDicd07943, DRE_TIM_HOA, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_01656, HOA, 1 hit
    InterProiView protein in InterPro
    IPR017629, 4OH_2_O-val_aldolase
    IPR013785, Aldolase_TIM
    IPR012425, DmpG_comm
    IPR035685, DRE_TIM_HOA
    IPR000891, PYR_CT
    PfamiView protein in Pfam
    PF07836, DmpG_comm, 1 hit
    PF00682, HMGL-like, 1 hit
    TIGRFAMsiTIGR03217, 4OH_2_O_val_ald, 1 hit
    PROSITEiView protein in PROSITE
    PS50991, PYR_CT, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiHOA_THET8
    <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: Q53WI0
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: May 24, 2005
    Last modified: December 2, 2020
    This is version 84 of the entry and version 1 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

    Plasmid, Reference proteome

    Documents

    1. 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