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Entry version 136 (17 Jun 2020)
Sequence version 1 (01 Nov 1999)
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Protein

Flavin-dependent thymidylate synthase

Gene

thyX

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NAD(P)H and FADH2 as the reductant.2 Publications

Miscellaneous

Reaction mechanism involved a direct methylene transfer from mTHF to dUMP (PubMed:23019356). FDTS ionizes N3 of dUMP using the active-site Arg-174, providing a new mechanism for dUMP activation. The phosphate of dUMP is crucial for flavin oxidation, suggesting that it acts as the base that deprotonates C5 of the dUMP-methylene adduct (PubMed:27214228).2 Publications

<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

FAD1 Publication1 PublicationNote: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.2 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 1.2 sec(-1) (at 65 degrees Celsius).1 Publication
  1. KM=30 µM for dUMP (at 65 degrees Celsius)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: dTTP biosynthesis

    This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei55FAD; shared with neighboring subunitsCombined sources6 Publications1
    Binding sitei86FAD; shared with neighboring subunitsCombined sources7 Publications1
    Binding sitei147dUMPCombined sources6 Publications1
    Binding sitei169FADCombined sources7 Publications1
    <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 sitei174Involved in ionization of N3 of dUMP, leading to its activation1 Publication1
    Binding sitei174dUMP; shared with dimeric partnerCombined sources6 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi75 – 78dUMP; shared with dimeric partnerCombined sources6 Publications4
    Nucleotide bindingi78 – 81FADCombined sources7 Publications4
    Nucleotide bindingi86 – 90dUMPCombined sources6 Publications5
    Nucleotide bindingi163 – 165FAD; shared with neighboring subunitsCombined sources7 Publications3

    <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 functionMethyltransferase, Transferase
    Biological processNucleotide biosynthesis
    LigandFAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-15758

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.1.148 2604

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9WYT0

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

    More...
    UniPathwayi
    UPA00575

    <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:
    Flavin-dependent thymidylate synthase4 Publications (EC:2.1.1.1482 Publications)
    Short name:
    FDTS4 Publications
    Alternative name(s):
    FAD-dependent thymidylate synthaseUniRule annotation
    Thymidylate synthase ThyXUniRule annotation
    Short name:
    TSUniRule annotation
    Short name:
    TSaseUniRule 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
    Name:thyX1 Publication
    Synonyms:thy11 Publication
    Ordered Locus Names:TM_0449
    <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>OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    <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 identifieri243274 [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 lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    <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
    • UP000008183 <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: 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%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>Mutagenesisi53H → A: Shows 1.39% of wild-type activity. 1 Publication1
    Mutagenesisi88S → A or C: Still catalytically active although shows a large decrease in activity. 1 Publication1
    Mutagenesisi90R → A: Binds dUMP 670-fold weaker than wild-type. 1 Publication1
    Mutagenesisi144E → A: Shows 0.113% of wild-type activity. 1 Publication1
    Mutagenesisi144E → R: Shows 0.016% of wild-type activity. 1 Publication1
    Mutagenesisi174R → A: Still catalytically active although only shows 0.0008% of wild-type activity. Binds dUMP 7300-fold weaker than wild-type. 2 Publications1
    Mutagenesisi174R → K: Loss of catalytic activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB01903 5-Bromo-2'-deoxyuridine 5'-(dihydrogen phosphate)
    DB03761 5-fluoro-2'-deoxyuridine-5'-monophosphate
    DB03800 Deoxyuridine monophosphate
    DB03147 Flavin adenine dinucleotide

    <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_00001755791 – 220Flavin-dependent thymidylate synthaseAdd BLAST220

    <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

    Homotetramer.

    3 Publications

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-60076N

    STRING: functional protein association networks

    More...
    STRINGi
    243274.THEMA_02480

    <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

    1220
    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
    Q9WYT0

    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
    Q9WYT0

    <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>Domaini1 – 208ThyXPROSITE-ProRule annotationAdd BLAST208

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi78 – 88ThyX motifUniRule annotationAdd BLAST11

    <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 thymidylate synthase ThyX family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG41087GE Bacteria
    COG1351 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9WYT0

    KEGG Orthology (KO)

    More...
    KOi
    K03465

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QQGRPGK

    Database of Orthologous Groups

    More...
    OrthoDBi
    896350at2

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1360.170, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01408 ThyX, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003669 Thymidylate_synthase_ThyX
    IPR036098 Thymidylate_synthase_ThyX_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR34934 PTHR34934, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02511 Thy1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF69796 SSF69796, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02170 thyX, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51331 THYX, 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.

    Q9WYT0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKIDILDKGF VELVDVMGND LSAVRAARVS FDMGLKDEER DRHLIEYLMK
    60 70 80 90 100
    HGHETPFEHI VFTFHVKAPI FVARQWFRHR IASYNELSGR YSKLSYEFYI
    110 120 130 140 150
    PSPERLEGYK TTIPPERVTE KISEIVDKAY RTYLELIESG VPREVARIVL
    160 170 180 190 200
    PLNLYTRFFW TVNARSLMNF LNLRADSHAQ WEIQQYALAI ARIFKEKCPW
    210 220
    TFEAFLKYAY KGDILKEVQV
    Length:220
    Mass (Da):26,004
    Last modified:November 1, 1999 - 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:iE3B9712014185907
    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
    AE000512 Genomic DNA Translation: AAD35532.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B72375

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_228259.1, NC_000853.1
    WP_004081517.1, NZ_CP011107.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAD35532; AAD35532; TM_0449

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    897468

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tma:TM0449

    <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
    AE000512 Genomic DNA Translation: AAD35532.1
    PIRiB72375
    RefSeqiNP_228259.1, NC_000853.1
    WP_004081517.1, NZ_CP011107.1

    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
    1KQ4X-ray2.25A/B/C/D1-220[»]
    1O24X-ray2.00A/B/C/D1-220[»]
    1O25X-ray2.40A/B/C/D1-220[»]
    1O26X-ray1.60A/B/C/D1-220[»]
    1O27X-ray2.30A/B/C/D1-220[»]
    1O28X-ray2.10A/B/C/D1-220[»]
    1O29X-ray2.00A/B/C/D1-220[»]
    1O2AX-ray1.80A/B/C/D1-220[»]
    1O2BX-ray2.45A/B/C/D1-220[»]
    3G4AX-ray1.95A/B/C/D1-220[»]
    3G4CX-ray2.05A/B/C/D1-220[»]
    3N0BX-ray2.30A/B/C/D1-220[»]
    3N0CX-ray2.30A/B/C/D1-220[»]
    4GT9X-ray1.39A1-220[»]
    4GTAX-ray1.50A1-220[»]
    4GTBX-ray1.70A1-220[»]
    4GTCX-ray1.97A/B/C/D1-220[»]
    4GTDX-ray1.76A/B/C/D1-220[»]
    4GTEX-ray1.89A/B/C/D1-220[»]
    4GTFX-ray1.77A1-220[»]
    4GTLX-ray2.17A/B/C/D1-220[»]
    4KARX-ray2.03A/B/C/D1-220[»]
    4KASX-ray1.85A/B/C/D1-220[»]
    4KATX-ray2.14A/B/C/D1-220[»]
    5CHPX-ray1.70A1-220[»]
    5IOQX-ray1.93A/B/C/D1-220[»]
    5IORX-ray1.95A1-220[»]
    5IOSX-ray1.90A/B/C/D1-220[»]
    5IOTX-ray2.00A/B/C/D1-220[»]
    5JFEX-ray2.03A1-220[»]
    SMRiQ9WYT0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    DIPiDIP-60076N
    STRINGi243274.THEMA_02480

    Chemistry databases

    DrugBankiDB01903 5-Bromo-2'-deoxyuridine 5'-(dihydrogen phosphate)
    DB03761 5-fluoro-2'-deoxyuridine-5'-monophosphate
    DB03800 Deoxyuridine monophosphate
    DB03147 Flavin adenine dinucleotide

    Genome annotation databases

    EnsemblBacteriaiAAD35532; AAD35532; TM_0449
    GeneIDi897468
    KEGGitma:TM0449

    Phylogenomic databases

    eggNOGiENOG41087GE Bacteria
    COG1351 LUCA
    InParanoidiQ9WYT0
    KOiK03465
    OMAiQQGRPGK
    OrthoDBi896350at2

    Enzyme and pathway databases

    UniPathwayiUPA00575
    BioCyciMetaCyc:MONOMER-15758
    BRENDAi2.1.1.148 2604
    SABIO-RKiQ9WYT0

    Miscellaneous databases

    EvolutionaryTraceiQ9WYT0

    Family and domain databases

    Gene3Di3.30.1360.170, 1 hit
    HAMAPiMF_01408 ThyX, 1 hit
    InterProiView protein in InterPro
    IPR003669 Thymidylate_synthase_ThyX
    IPR036098 Thymidylate_synthase_ThyX_sf
    PANTHERiPTHR34934 PTHR34934, 1 hit
    PfamiView protein in Pfam
    PF02511 Thy1, 1 hit
    SUPFAMiSSF69796 SSF69796, 1 hit
    TIGRFAMsiTIGR02170 thyX, 1 hit
    PROSITEiView protein in PROSITE
    PS51331 THYX, 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 nameiTHYX_THEMA
    <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: Q9WYT0
    <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: July 11, 2001
    Last sequence update: November 1, 1999
    Last modified: June 17, 2020
    This is version 136 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

    3D-structure, 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
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