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Entry version 40 (11 Dec 2019)
Sequence version 1 (11 Jul 2012)
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Protein

Dye-decolorizing peroxidase AauDyP1

Gene

dyp1

Organism
Auricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae)
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

Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5.5 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

heme b4 PublicationsNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.4 Publications

<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

Inhibited by imidazole.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>Absorptioni

Abs(max)=405 nmDye-decolorizing peroxidase AauDyP1. The value for Dye-decolorizing peroxidase AauDyP2 is 406 nm.

Kineticsi

  1. KM=20 µM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)1 Publication
  2. KM=283 µM for ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 3)1 Publication
  3. KM=20 µM for ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)1 Publication
  4. KM=10 µM for H2O2 (Dye-decolorizing peroxidase AauDyP1)1 Publication
  5. KM=5 µM for H2O2 (Dye-decolorizing peroxidase AauDyP2)1 Publication
  6. KM=23 µM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3)1 Publication
  7. KM=3.1 µM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3)1 Publication
  8. KM=15 µM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at pH 3)1 Publication
  9. KM=27 µM for 2,6-Dimethoxyphenol (DMP)(Dye-decolorizing peroxidase AauDyP1, at pH 4.5)1 Publication
  10. KM=27 µM for DMP (Dye-decolorizing peroxidase AauDyP1, at pH 5)1 Publication
  11. KM=23 µM for DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)1 Publication
  1. Vmax=134 µmol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3)1 Publication
  2. Vmax=375 µmol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at pH 3)1 Publication
  3. Vmax=331 µmol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)1 Publication
  4. Vmax=471 µmol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)1 Publication
  5. Vmax=105 µmol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)1 Publication
  6. Vmax=130 µmol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)1 Publication
  7. Vmax=315 µmol/min/mg enzyme toward H2O2 (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)1 Publication
  8. Vmax=348 µmol/min/mg enzyme toward H2O2 (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)1 Publication

pH dependencei

Optimum pH is 4.5 for oxidation of 2,6-dimethoxyphenol (PubMed:23111597). Retains 100% activity after incubation at pH 2.5 for 4 hours (PubMed:23111597, PubMed:19756587, PubMed:25153532). Retains >60% activity after incubation at pH 2-11 at 4 degrees Celsius (PubMed:25153532). Retains >60% activity after incubation at pH 3-9 at room temperature (PubMed:25153532).3 Publications

Temperature dependencei

Retains >80% activity after incubation at temperatures up to 60 degrees Celsius for 10 minutes. Retains 50% activity after incubation at 65.5 degrees Celsius for 10 minutes. Activity is lost after incubation at 70 degrees Celsius for 10 minutes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei229Proton acceptor1 Publication1
<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 bindingi365Iron (heme axial ligand); via tele nitrogenCombined sources5 Publications1

<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

<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 functionOxidoreductase, Peroxidase
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.11.1.19, 12259

<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:
Dye-decolorizing peroxidase AauDyP11 Publication (EC:1.11.1.193 Publications, EC:1.11.1.75 Publications)
Alternative name(s):
AjP I1 Publication
Manganese-independent peroxidase I1 Publication
Cleaved into the following chain:
Dye-decolorizing peroxidase AauDyP21 Publication (EC:1.11.1.192 Publications, EC:1.11.1.72 Publications)
Alternative name(s):
AjP II1 Publication
Manganese-independent peroxidase II1 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:dyp1Imported
<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>OrganismiAuricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae)Imported
<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 identifieri29892 [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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAuricularialesAuriculariaceaeAuricularia

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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>Mutagenesisi208Y → F: No significant effect on enzyme kinetics; when associated with F-398. 1 Publication1
Mutagenesisi208Y → S: No significant effect on enzyme kinetics. 1 Publication1
Mutagenesisi229D → N: Drastically decreased catalytic efficiency in reducing H(2)O(2). 1 Publication1
Mutagenesisi230G → L: Complete loss of activity for ABTS and Reactive Blue 19 but not DMP. 1 Publication1
Mutagenesisi393R → L: Drastically decreased catalytic efficiency in reducing H(2)O(2). 1 Publication1
Mutagenesisi398Y → F: No significant effect on enzyme kinetics; when associated with F-208. 1 Publication1
Mutagenesisi398Y → S: No significant effect on enzyme kinetics. 1 Publication1
Mutagenesisi418L → G: Acquires new moderate non-stereoselective sulfoxidase activity (KM=0.6 mM for methyl-phenyl sulfide(MPS)). No activity towards the bigger substrate methyl-p-tolyl sulfide (MTS). 1 Publication1
Mutagenesisi420F → G: Acquires new strong stereoselective sulfoxidase activity favoring the S enantiomer (KM=0.37 mM for methyl-phenyl sulfide(MPS), KM=0.13 mM for methyl-p-tolyl sulfide (MTS)). 1 Publication1
Mutagenesisi420F → H: Does not acquire new sulfoxidase activity. 1 Publication1
Mutagenesisi420F → W: Does not acquire new sulfoxidase activity. 1 Publication1
Mutagenesisi438W → S: Complete loss of activity or at least greatly reduced substrate affinity, enzyme activity and catalytic efficiency. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22Sequence analysisAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044402323 – 611 PublicationAdd BLAST39
<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_500365717062 – 509Dye-decolorizing peroxidase AauDyP11 PublicationAdd BLAST448
ChainiPRO_0000444024171 – 509Dye-decolorizing peroxidase AauDyP21 PublicationAdd BLAST339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi343N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Glycosylationi383N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi410N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Glycosylationi476N-linked (GlcNAc...) asparagineCombined sources3 Publications1

Keywords - PTMi

Glycoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
I2DBY1

<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

1509
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
I2DBY1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<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 DyP-type peroxidase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011008, Dimeric_a/b-barrel
IPR006314, Dyp_peroxidase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04261, Dyp_perox, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54909, SSF54909, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01413, Dyp_perox_fam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51404, DYP_PEROXIDASE, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

I2DBY1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLSPVFVAL LSGLLAADLG LARSVAPRVA DSPAAVTGTR KTSLLKNVAG
60 70 80 90 100
LPPVPSAAQV AATSLNTDDI QGDILVGMHK QKQLFYFFAI NDPATFKTHL
110 120 130 140 150
ASDIAPVVAS VTQLSNVATQ PLVALNIAFS NTGLLALGVT DNLGDSLFAN
160 170 180 190 200
GQAKDATSFK ESTSSWVPQF AGTGIHGVII LASDTTDLID QQVASIESTF
210 220 230 240 250
GSSISKLYSL SASIRPGNEA GHEMFGFLDG IAQPAINGFN TPLPGQNIVD
260 270 280 290 300
AGVIITGATN DPITRPSWAV GGSFLAFRQL EQLVPEFNKY LLDNAPAGSG
310 320 330 340 350
SLQARADLLG ARMVGRWKSG APIDLTPTAD DPALGADAQR NNNFTYSHAG
360 370 380 390 400
FDLGSDQSHC PFSAHIRKTR PRADLGGSLT PPNLSAGANS IMRSGIPYGP
410 420 430 440 450
EVTSAESASN TTTQERGLAF VAYQAQLSQG FHFLQQTWAD NANFPPGKTP
460 470 480 490 500
ATVGLDPIIG QNNGQPRVVN GLLPSNSSAS LSIPQFVVSH GGEYFFSPPI

SAIGGRLSA
Length:509
Mass (Da):52,992
Last modified:July 11, 2012 - 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:i5BAE13D122C13C8A
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
JQ650250 mRNA Translation: AFJ79723.1

<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
JQ650250 mRNA Translation: AFJ79723.1

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
4AU9X-ray2.10A/B62-509[»]
4UZIX-ray2.10A/B64-509[»]
4W7JX-ray1.79A/B/C/D62-509[»]
4W7KX-ray1.05A/B62-509[»]
4W7LX-ray1.05A/B62-509[»]
4W7MX-ray1.15A/B62-509[»]
4W7NX-ray1.40A/B62-509[»]
4W7OX-ray1.20A62-509[»]
5AG0X-ray1.75A/B64-509[»]
5AG1X-ray1.85A/B64-509[»]
5IKDX-ray1.11A64-509[»]
5IKGX-ray1.95A65-509[»]
SMRiI2DBY1
ModBaseiSearch...
PDBe-KBiSearch...

PTM databases

iPTMnetiI2DBY1

Enzyme and pathway databases

BRENDAi1.11.1.19, 12259

Family and domain databases

InterProiView protein in InterPro
IPR011008, Dimeric_a/b-barrel
IPR006314, Dyp_peroxidase
PfamiView protein in Pfam
PF04261, Dyp_perox, 1 hit
SUPFAMiSSF54909, SSF54909, 1 hit
TIGRFAMsiTIGR01413, Dyp_perox_fam, 1 hit
PROSITEiView protein in PROSITE
PS51404, DYP_PEROXIDASE, 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 nameiDYP_AURAJ
<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: I2DBY1
<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: April 25, 2018
Last sequence update: July 11, 2012
Last modified: December 11, 2019
This is version 40 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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