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Entry version 98 (29 Sep 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 pyrophosphate (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 sitei295(4s)-7-azabisabolene; inhibitorCombined 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

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 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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium

<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

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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

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EMBLi

GenBank nucleotide sequence database

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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

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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: September 29, 2021
This is version 98 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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