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UniProtKB - P13513 (TRI5_FUSSP)

Entry version 97 (02 Jun 2021)
Sequence version 1 (01 Jan 1990)
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Protein

Trichodiene synthase

Gene

TRI5

Organism
Fusarium sporotrichioides
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

Trichodiene synthase; part of the core gene cluster that mediates the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin (PubMed:11352533, PubMed:2817906).

The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:3800398, PubMed:7873527, PubMed:8823172).

Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333).

TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichotriol (PubMed:16917519).

Isotrichotriol then undergoes a non-enzymatic isomerization and cyclization to form isotrichodermol (PubMed:2317042).

During this process, the oxygen at the C-2 position becomes the pyran ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042).

More complex type A trichothecenes are built by modifying isotrichodermol through a series of paired hydroxylation and acetylation or acylation steps (PubMed:11352533).

Isotrichodermol is converted to isotrichodermin by the acetyltransferase TRI101 (PubMed:10583973).

TRI101 encodes a C-3 transacetylase that acts as a self-protection or resistance factor during biosynthesis and that the presence of a free C-3 hydroxyl group is a key component of Fusarium trichothecene phytotoxicity (PubMed:10583973).

A second hydroxyl group is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing 15-decalonectrin, which is then acetylated by TRI3, producing calonectrin (PubMed:9435078, PubMed:8593041).

A third hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is subsequently acetylated by the acetyltransferase TRI7 (PubMed:12135578, PubMed:11352533).

A fourth hydroxyl group is added to C-8 by the cytochrome P450 monooxygenase TRI1, followed by the addition of an isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047).

Finally, the acetyl group is removed from the C-3 position by the trichothecene C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755).

12 Publications

Miscellaneous

Trichothecenes are sesquiterpenoid toxins that act by inhibiting protein biosynthesis.Curated

<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

Mg2+6 Publications, Mn2+1 PublicationNote: Some of the cofactor binding sites show unusual localization within the protein.Curated

<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

Benzyl triethylammonium cation (BTAC) acts as a competitive inhibitor of trichodiene synthase reaction in the presence of pyrophospahte (PPi) (PubMed:17678871).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

  1. KM=62.0 nM for farnesyl pyrophosphate2 Publications
  2. KM=78.0 nM for Mg2+1 Publication
  3. KM=84.8 nM for Mn2+1 Publication

    pH dependencei

    Optimum pH is 6.75-7.75.1 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: trichothecene biosynthesis

    This protein is involved in the pathway trichothecene biosynthesis, which is part of Sesquiterpene biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway trichothecene biosynthesis and in Sesquiterpene biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi100Magnesium 1Combined sources1 Publication1
    Metal bindingi164Magnesium 1Combined sources1 Publication1
    Metal bindingi225Magnesium 2Combined sources3 Publications1
    Metal bindingi229Magnesium 2Combined sources3 Publications1
    Metal bindingi233Magnesium 2Combined sources3 Publications1
    Metal bindingi239Magnesium 3Combined sources2 Publications1
    Metal bindingi241Magnesium 3; via carbonyl oxygenCombined sources2 Publications1
    <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 sitei295InhibitorCombined sources1 Publication1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionLyase
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		4.2.3.6, 2364

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

    More...    UniPathwayi    		UPA00267

    <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:
    Trichodiene synthase1 Publication (EC:4.2.3.65 Publications)
    Alternative name(s):
    Core trichothecene cluster (CTC) protein 51 Publication
    Sesquiterpene cyclase TRI51 Publication
    Short name:
    TS1 Publication
    <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:TRI51 Publication
    Synonyms:TOX 5
    <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>OrganismiFusarium sporotrichioides
    <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 identifieri5514 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Fusarium ›

    <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>Mutagenesisi100D → E: Does not significantly perturb the overall structure of trichodiene synthase but leads to an increased KM, a reduction in kcat, as well as to the production of anomalous sesquiterpene products in addition to trichodiene when incubated with farnesyl diphosphate. 2 Publications1
    Mutagenesisi101D → E: Leads to an increased KM for Mg(2+), a reduction in kcat, as well as to the production of anomalous sesquiterpene products in addition to trichodiene when incubated with farnesyl diphosphate. 1 Publication1
    Mutagenesisi104D → E: Does not significantly affect the KM and kcat for farnesyl diphosphate. 1 Publication1
    Mutagenesisi146C → F: Leads to the loss of activity. 1 Publication1
    Mutagenesisi190C → F: Increases the KM for farnesyl diphosphate by about 1.3-fold and reduces the kcat by about 2000-fold. 1 Publication1
    Mutagenesisi225N → D: Increases the KM for farnesyl diphosphate by about 6-fold and reduces the kcat by about 28-fold. Leads to complete loss of activity; when associated with S-229. 1 Publication1
    Mutagenesisi229S → T: Increases the KM for farnesyl diphosphate by about 77-fold and reduces the kcat by about 9-fold. Leads to complete loss of activity; when associated with D-225. 1 Publication1
    Mutagenesisi295Y → F: Does not affect the catalytic activity. 1 Publication1
    Mutagenesisi304R → K: Does not cause large changes in the overall structure but increases the KM for farnesyl diphosphate by about 25-fold, reduces the kcat by about 200-fold, and leads to conversion of farnesyl diphosphate not only to trichodiene but to at least 2 additional C(15)H(24) hydrocarbons. 2 Publications1
    Mutagenesisi305Y → F: Does not cause large changes in the overall structure but increases the KM for farnesyl diphosphate by about 7-fold. 2 Publications1
    Mutagenesisi305Y → T: Increases the KM for farnesyl diphosphate by about 80-fold, reduces the kcat by about 120-fold, and leads to the conversion of farneyl diphosphate to an approximately equal mixture of trichodiene and an unidentified sesquiterpene hydrocarbon. 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_00002215841 – 374Trichodiene synthaseAdd BLAST374

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression is positively regulated by the trichothecene cluster-specific transcription activator TRI10 (PubMed:12732543). Expression is induced between 18h and 21h growth on GYEP medium (PubMed:16347944). The initial detection of trichothecenes occurs several hours after the initial detection of TRI5 (PubMed:16347944). The initiation of trichothecene biosynthesis occurs with a high concentration of glucose remaining in the culture medium (PubMed:16347944).2 Publications

    <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

    1374
    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    		P13513

    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    		P13513

    <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>Regioni100 – 104Aspartate-rich domain1 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 trichodiene synthase family.Curated

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.600.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR008949, Isoprenoid_synthase_dom_sf
    IPR010458, TRI5_ascomyc
    IPR024652, Trichodiene_synth

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF06330, TRI5, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001388, TRI5, 1 hit

    Structure-Function Linkage Database

    More...    SFLDi    		SFLDG01021, Trichodiene_Synthase_Like, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF48576, SSF48576, 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.

    P13513-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MENFPTEYFL NTTVRLLEYI RYRDSNYTRE ERIENLHYAY NKAAHHFAQP 
            60         70         80         90        100
    RQQQLLKVDP KRLQASLQTI VGMVVYSWAK VSKECMADLS IHYTYTLVLD 
           110        120        130        140        150
    DSKDDPYPTM VNYFDDLQAG REQAHPWWAL VNEHFPNVLR HFGPFCSLNL 
           160        170        180        190        200
    IRSTLDFFEG CWIEQYNFGG FPGSHDYPQF LRRMNGLGHC VGASLWPKEQ 
           210        220        230        240        250
    FNERSLFLEI TSAIAQMENW MVWVNDLMSF YKEFDDERDQ ISLVKNYVVS 
           260        270        280        290        300
    DEISLHEALE KLTQDTLHSS KQMVAVFSDK DPQVMDTIEC FMHGYVTWHL 
           310        320        330        340        350
    CDRRYRLSEI YEKVKEEKTE DAQKFCKFYE QAANVGAVSP SEWAYPPVAQ 
           360        370 
    LANVRSKDVK EVQKPFLSSI ELVE
    Length:374
    Mass (Da):44,000
    Last modified:January 1, 1990 - 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:i189E8FC1663C3763
    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
    		AF364179 Genomic DNA Translation: AAD13657.1
    AF359360 Genomic DNA Translation: AAK33074.1
    AY032745 mRNA Translation: AAK77935.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		JU0064, SYFUTP

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ag:AAD13657

    <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
    		AF364179 Genomic DNA Translation: AAD13657.1
    AF359360 Genomic DNA Translation: AAK33074.1
    AY032745 mRNA Translation: AAK77935.1
    PIRiJU0064, SYFUTP

    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
    1JFAX-ray2.50A/B1-374[»]
    1JFGX-ray2.50A/B1-374[»]
    1KIYX-ray2.40A/B1-374[»]
    1KIZX-ray2.60A/B1-374[»]
    1YJ4X-ray2.30A/B1-374[»]
    1YYQX-ray2.10A/B1-374[»]
    1YYRX-ray2.50A/B1-374[»]
    1YYSX-ray2.75A/B1-374[»]
    1YYTX-ray2.90A/B1-374[»]
    1YYUX-ray2.95A/B1-374[»]
    2AEKX-ray2.90A/B1-374[»]
    2AELX-ray2.50A/B1-374[»]
    2AETX-ray2.75A/B1-374[»]
    2PS4X-ray2.46A/B1-374[»]
    2PS5X-ray2.10A/B1-374[»]
    2PS6X-ray2.60A/B1-374[»]
    2PS7X-ray2.35A/B1-374[»]
    2PS8X-ray2.67A/B1-374[»]
    2Q9YX-ray2.85A/B1-374[»]
    2Q9ZX-ray2.95A/B1-374[»]
    SMRiP13513
    ModBaseiSearch...
    PDBe-KBiSearch...

    Genome annotation databases

    KEGGiag:AAD13657

    Enzyme and pathway databases

    UniPathwayiUPA00267
    BRENDAi4.2.3.6, 2364

    Miscellaneous databases

    EvolutionaryTraceiP13513

    Family and domain databases

    Gene3Di1.10.600.10, 1 hit
    InterProiView protein in InterPro
    IPR008949, Isoprenoid_synthase_dom_sf
    IPR010458, TRI5_ascomyc
    IPR024652, Trichodiene_synth
    PfamiView protein in Pfam
    PF06330, TRI5, 1 hit
    PIRSFiPIRSF001388, TRI5, 1 hit
    SFLDiSFLDG01021, Trichodiene_Synthase_Like, 1 hit
    SUPFAMiSSF48576, SSF48576, 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 nameiTRI5_FUSSP
    <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: P13513
    Secondary accession number(s): Q7LP67
    <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: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: June 2, 2021
    This is version 97 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 programFungal 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

    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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