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Entry version 94 (02 Jun 2021)
Sequence version 2 (21 Mar 2006)
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Protein

Tryptophan dimethylallyltransferase

Gene

dmaW

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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

Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831).

DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460, PubMed:23435153).

The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity).

The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592).

EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482).

EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482).

Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831).

Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).

By similarity8 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 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=4 µM for dimethylallyl diphosphate1 Publication
  2. KM=8 µM for L-tryptophan1 Publication
  1. Vmax=0.198 µmol/min/mg enzyme1 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: ergot alkaloid biosynthesis

This protein is involved in the pathway ergot alkaloid biosynthesis, which is part of Alkaloid biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway ergot alkaloid biosynthesis and in Alkaloid biosynthesis.

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 sitei89L-tryptophan1 Publication1
Binding sitei100Substrate1 Publication1
Binding sitei187Substrate1 Publication1
Binding sitei189Substrate1 Publication1
Binding sitei191L-tryptophan1 Publication1
Binding sitei244L-tryptophan1 Publication1
Binding sitei257Substrate1 Publication1
Binding sitei259Substrate1 Publication1
Binding sitei261Substrate1 Publication1
Binding sitei343Substrate1 Publication1
Binding sitei345Substrate1 Publication1
Binding sitei409Substrate1 Publication1
Binding sitei413Substrate1 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 functionTransferase
Biological processAlkaloid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15369

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.5.1.34, 508

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q50EL0

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

More...
UniPathwayi
UPA00327

<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:
Tryptophan dimethylallyltransferaseCurated (EC:2.5.1.341 Publication)
Alternative name(s):
4-dimethylallyltryptophan synthase1 Publication
All-trans-hexaprenyl-diphosphate synthaseCurated
L-tryptophan dimethylallyl transferaseCurated
Short name:
DMATSCurated
<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:dmaW1 Publication
Synonyms:fgaPT21 Publication
ORF Names:AFUA_2G18040
<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>OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
<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 identifieri330879 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Fumigati
<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
  • UP000002530 <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> Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:Afu2g18040

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Ergot alkaloids are known for their toxic effects on humans who consume contaminated grains or livestock that graze on grasses harboring ergot alkaloid-producing fungi (PubMed:19523108). Due to their strong affinity for monoamine neurotransmitter receptors they may also have clinical uses such as treatment of migraines, Parkinson's disease and cerebrovascular insufficiency (PubMed:19523108).1 Publication

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impairs the production of ergot alkaloids including festuclavine, fumigaclavine A, fumigaclavine B and fumigaclavine C (PubMed:15933009).1 Publication

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>Mutagenesisi89E → A: Abolishes tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi100R → D or Q: Nearly abolishes tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi174K → E: Nearly abolishess tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi174K → Q: Impairs tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi187K → E: Nearly abolishes tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi259K → E: Nearly abolishes tryptophan dimethylallyltransferase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4523316

<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_00002286871 – 459Tryptophan dimethylallyltransferaseAdd BLAST459

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q50EL0

<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

The expression of the ergot alkaloid synthesis cluster which leads to the synthesis of fumigaclavines is positively regulated by the brlA and stuA transcription factors (PubMed:19028996).1 Publication

<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.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
746128.CADAFUBP00003306

<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

1459
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
Q50EL0

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
Q50EL0

<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>Regioni80 – 81L-tryptophan binding1 Publication2

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502S2XP, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_037431_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q50EL0

Database of Orthologous Groups

More...
OrthoDBi
1531660at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd13929, PT-DMATS_CymD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033964, Aro_prenylTrfase
IPR017795, Aro_prenylTrfase_DMATS
IPR012148, DMATS-type_fun
IPR017796, Trp_dimethylallylTrfase

The PANTHER Classification System

More...
PANTHERi
PTHR40627, PTHR40627, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11991, Trp_DMAT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000509, Trp_DMAT, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDS00036, Aromatic_Prenyltransferase, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03429, arom_pren_DMATS, 1 hit
TIGR03430, trp_dimet_allyl, 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.

Q50EL0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAANASSAE AYRVLSRAFR FDNEDQKLWW HSTAPMFAKM LETANYTTPC
60 70 80 90 100
QYQYLITYKE CVIPSLGCYP TNSAPRWLSI LTRYGTPFEL SLNCSNSIVR
110 120 130 140 150
YTFEPINQHT GTDKDPFNTH AIWESLQHLL PLEKSIDLEW FRHFKHDLTL
160 170 180 190 200
NSEESAFLAH NDRLVGGTIR TQNKLALDLK DGRFALKTYI YPALKAVVTG
210 220 230 240 250
KTIHELVFGS VRRLAVREPR ILPPLNMLEE YIRSRGSKST ASPRLVSCDL
260 270 280 290 300
TSPAKSRIKI YLLEQMVSLE AMEDLWTLGG RRRDASTLEG LSLVRELWDL
310 320 330 340 350
IQLSPGLKSY PAPYLPLGVI PDERLPLMAN FTLHQNDPVP EPQVYFTTFG
360 370 380 390 400
MNDMAVADAL TTFFERRGWS EMARTYETTL KSYYPHADHD KLNYLHAYIS
410 420 430 440 450
FSYRDRTPYL SVYLQSFETG DWAVANLSES KVKCQDAACQ PTSLPPDLSK

TGVYYSGLH
Length:459
Mass (Da):52,463
Last modified:March 21, 2006 - v2
<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:iED7AAB193E9A46C8
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence EAL94103 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti443S → A in strain: B5233 / ATCC 13073. 1

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
AY775787 mRNA Translation: AAX08549.1
AAHF01000001 Genomic DNA Translation: EAL94103.2 Sequence problems.

NCBI Reference Sequences

More...
RefSeqi
XP_756141.2, XM_751048.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3512716

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
afm:AFUA_2G18040

<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
AY775787 mRNA Translation: AAX08549.1
AAHF01000001 Genomic DNA Translation: EAL94103.2 Sequence problems.
RefSeqiXP_756141.2, XM_751048.2

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
3I4XX-ray2.10A/B1-459[»]
3I4ZX-ray1.76A/B1-459[»]
SMRiQ50EL0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi746128.CADAFUBP00003306

Chemistry databases

ChEMBLiCHEMBL4523316

Proteomic databases

PRIDEiQ50EL0

Genome annotation databases

GeneIDi3512716
KEGGiafm:AFUA_2G18040

Organism-specific databases

VEuPathDBiFungiDB:Afu2g18040

Phylogenomic databases

eggNOGiENOG502S2XP, Eukaryota
HOGENOMiCLU_037431_0_0_1
InParanoidiQ50EL0
OrthoDBi1531660at2759

Enzyme and pathway databases

UniPathwayiUPA00327
BioCyciMetaCyc:MONOMER-15369
BRENDAi2.5.1.34, 508
SABIO-RKiQ50EL0

Miscellaneous databases

EvolutionaryTraceiQ50EL0

Family and domain databases

CDDicd13929, PT-DMATS_CymD, 1 hit
InterProiView protein in InterPro
IPR033964, Aro_prenylTrfase
IPR017795, Aro_prenylTrfase_DMATS
IPR012148, DMATS-type_fun
IPR017796, Trp_dimethylallylTrfase
PANTHERiPTHR40627, PTHR40627, 1 hit
PfamiView protein in Pfam
PF11991, Trp_DMAT, 1 hit
PIRSFiPIRSF000509, Trp_DMAT, 1 hit
SFLDiSFLDS00036, Aromatic_Prenyltransferase, 1 hit
TIGRFAMsiTIGR03429, arom_pren_DMATS, 1 hit
TIGR03430, trp_dimet_allyl, 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 nameiDMAW_ASPFU
<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: Q50EL0
Secondary accession number(s): Q4WZ62
<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: March 21, 2006
Last sequence update: March 21, 2006
Last modified: June 2, 2021
This is version 94 of the entry and version 2 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, 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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