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Entry version 94 (12 Aug 2020)
Sequence version 2 (02 May 2006)
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Protein

Aorsin

Gene

aorO

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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

Serine endopeptidase which hydrolyzes a range of fluorogenic peptide substrates containing the basic residues arginine or lysine at the P1 position and prefers paired basic resides. Also hydrolyzes clupeine and salmine, activates plasminogen and converts trypsinogen to trypsin.1 Publication

<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

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

<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 antipain and leupeptin.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

The highest catalytic efficiency is observed for Boc-Leu-Lys-Arg-MCA.1 Publication
  1. KM=0.7 µM for Boc-Gln-Arg-Arg-MCA1 Publication
  2. KM=3.9 µM for Boc-Leu-Arg-Arg-MCA1 Publication
  3. KM=2.8 µM for Boc-Gly-Arg-Arg-MCA1 Publication
  4. KM=10.0 µM for Boc-Leu-Lys-Arg-MCA1 Publication
  5. KM=26.8 µM for Boc-Gly-Lys-Arg-MCA1 Publication
  6. KM=58.0 µM for Boc-Leu-Thr-Arg-MCA1 Publication
  7. KM=84.5 µM for Boc-Leu-Gly-Arg-MCA1 Publication
  8. KM=88.3 µM for Boc-Gln-Gly-Arg-MCA1 Publication
  1. Vmax=12.8 nmol/sec/mg enzyme with Z-Arg-Arg-MCA as substrate1 Publication

pH dependencei

Optimum pH is 4.0. Inactive below pH 3.0 and above pH 6.5. The half-life (t1/2) values for activity loss at 30 degrees Celsius are 150 min at pH 6.6, 5.5 min at pH 6.8 and 14 min at pH 2.4.1 Publication

Temperature dependencei

Remains fully active after heating at 50 degrees Celsius and pH 4.0 for 10 min. Retains 65% of its activity after heating at 55 degrees Celsius for 10 min. The half-life value for loss of activity at 60 degrees Celsius and pH 4.0 is 3.5 min.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 sitei301Charge relay systemBy similarity1
Active sitei305Charge relay systemBy similarity1
Active sitei569Charge relay systemBy similarity1
<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 bindingi610Calcium1 Publication1
Metal bindingi611Calcium; via carbonyl oxygenBy similarity1
Metal bindingi629Calcium; via carbonyl oxygenBy similarity1
Metal bindingi631CalciumBy similarity1

<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

  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: UniProtKB

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 functionHydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S53.007

<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:
Aorsin (EC:3.4.21.-)
<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:aorOImported
ORF Names:AO090026000083
<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>OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
<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 identifieri510516 [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. Circumdati
<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
  • UP000006564 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

<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>Mutagenesisi301E → D: 1000-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi301E → Q: 7000-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi305D → E: 2000-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi305D → N: 20-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi426D → E: 40000-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi426D → N: 8000-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi569S → T: 20000-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi610D → E or N: Active. Loss of calcium binding. 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_000002736823 – 215Removed in mature formSequence analysis1 PublicationAdd BLAST193
<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_0000027369216 – 652Aorsin1 PublicationAdd BLAST437

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>Glycosylationi112N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi218N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi247N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi331N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi445N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi613N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.1 Publication
O-glycosylated.1 PublicationCurated

Keywords - PTMi

Glycoprotein, Zymogen

<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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Activity found in solid culture only. Increases at the initial growth stage and decreases in the late growth stage.1 Publication

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini225 – 651Peptidase S53Add BLAST427

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013783_4_0_1

KEGG Orthology (KO)

More...
KOi
K01279

Identification of Orthologs from Complete Genome Data

More...
OMAi
DFELAYP

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04056, Peptidases_S53, 1 hit
cd11377, Pro-peptidase_S53, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036852, Peptidase_S8/S53_dom_sf
IPR015366, S53_propep
IPR030400, Sedolisin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09286, Pro-kuma_activ, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00944, Pro-kuma_activ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52743, SSF52743, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51695, SEDOLISIN, 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.

Q8NK92-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRPLSHLSFF NGLLLGLSAL SAATSVVHER REATSSNWVK RARVNPSDKH
60 70 80 90 100
VVRIGLTQSS LEEAHDLLMD VSNPSSPNYA RFYSADEVAA KFAPSTETVN
110 120 130 140 150
EVQNWLTEKG INASRVAQTQ NHGWLVFHAT SKEIENLFDT TYYEYHNRKT
160 170 180 190 200
GKKAIACEQY HVPASVQKHI DYVHPGVNLN PSSGKPSSIR RRAAASKKTK
210 220 230 240 250
LPARGPRPIQ QHDVKGLNVT NCDQLITPEC IRALYKIPSA RAAPHPNNSL
260 270 280 290 300
GIFEEGDYYA QEDLDLFFKT FAKDIPQGTH PIPAFIDGAE APVPVTKAGG
310 320 330 340 350
ESDLDFELAY PIVHPQSITL YQTDDANWAS NTTGFLNTFL DALDGSYCTY
360 370 380 390 400
CAYGECGNDP SLDPVYPDDA GYDGQLMCGV FKPTNVISVS YGEQENDLPA
410 420 430 440 450
NYQQRQCMEF LKLGLQGVSV LFASGDNGVA GPPGDGNSVN GCLNNGTVFS
460 470 480 490 500
PAFPNSCPYI TNVGATKVYP GYTVSQPESA VYDPDGLYSY ASGGGFSNIY
510 520 530 540 550
PIPDYQAEAV ATYFKDHNPP YPYYEGAENL GKNGGLYNRL GRGYPDVAAN
560 570 580 590 600
GDNIAVFNGG EFGSSGGTSA STPIFASIIN RIIDERLAVG KGPVGFINPV
610 620 630 640 650
LYKNPSVLND ITNGTNPGCG TDGFSTAPGW DPATGLGTPN YPKMLKLWLD

LP
Length:652
Mass (Da):70,501
Last modified:May 2, 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:i865BB1A1BC8235EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti118Q → R in BAB97387 (PubMed:12519073).Curated1

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
AB084899 Genomic DNA Translation: BAB97387.1
AP007159 Genomic DNA Translation: BAE59580.1

NCBI Reference Sequences

More...
RefSeqi
XP_001821582.1, XM_001821530.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
BAE59580; BAE59580; AO090026000083

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5993610

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
aor:AO090026000083

<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
AB084899 Genomic DNA Translation: BAB97387.1
AP007159 Genomic DNA Translation: BAE59580.1
RefSeqiXP_001821582.1, XM_001821530.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein family/group databases

MEROPSiS53.007

Genome annotation databases

EnsemblFungiiBAE59580; BAE59580; AO090026000083
GeneIDi5993610
KEGGiaor:AO090026000083

Phylogenomic databases

HOGENOMiCLU_013783_4_0_1
KOiK01279
OMAiDFELAYP

Family and domain databases

CDDicd04056, Peptidases_S53, 1 hit
cd11377, Pro-peptidase_S53, 1 hit
Gene3Di3.40.50.200, 1 hit
InterProiView protein in InterPro
IPR036852, Peptidase_S8/S53_dom_sf
IPR015366, S53_propep
IPR030400, Sedolisin_dom
PfamiView protein in Pfam
PF09286, Pro-kuma_activ, 1 hit
SMARTiView protein in SMART
SM00944, Pro-kuma_activ, 1 hit
SUPFAMiSSF52743, SSF52743, 1 hit
PROSITEiView protein in PROSITE
PS51695, SEDOLISIN, 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 nameiAORSN_ASPOR
<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: Q8NK92
Secondary accession number(s): Q2UFT5
<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 1, 2005
Last sequence update: May 2, 2006
Last modified: August 12, 2020
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

Direct protein sequencing, Reference proteome
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