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Entry version 137 (29 Sep 2021)
Sequence version 2 (02 May 2006)
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Protein

Aspergillopepsin-1

Gene

pepA

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

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A. Hydrolyzes bovine chymotrysinogen A between positions 'Arg-15' and 'Ile-16'.

1 Publication

<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

  • Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.1 Publication EC:3.4.23.18

<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 sodium lauryl sulfonate.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

kcat is 1.65 sec(-1) with Z-His-Phe-Phe-OEt as substrate, 0.35 sec(-1) with Z-Ala-Ala-Phe-Phe-OPy4Pr as substrate, 13 sec(-1) with bovine trypsinogen as substrate and 1.14 sec(-1) with bovine chymotrysinogen A as substrate.1 Publication
  1. KM=0.064 mM for Z-His-Phe-Phe-OEt1 Publication
  2. KM=0.037 mM for Z-Ala-Ala-Phe-Phe-OPy4Pr1 Publication
  3. KM=0.1 mM for bovine trypsinogen1 Publication
  4. KM=0.18 mM for bovine chymotrysinogen A1 Publication

pH dependencei

Optimum pH is 3.0-4.2.1 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 sitei111PROSITE-ProRule annotation1
Active sitei293PROSITE-ProRule annotation1

<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 functionAspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.23.18, 522

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A01.026

<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:
Aspergillopepsin-1Curated (EC:3.4.23.181 Publication)
Alternative name(s):
Acid protease A21 Publication
Aspartic protease pepA
Aspergillopepsin I
Aspergillopepsin O1 Publication
Short name:
PEPO
Aspergillopeptidase A
Short name:
PEPA
<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:pepA1 Publication
Synonyms:pepO1 Publication
ORF Names:AO090120000474
<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 5

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:AO090120000474

<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

Keywords - Cellular componenti

Secreted

<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 – 20Sequence analysisAdd BLAST20
<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_000002592221 – 77Activation peptideBy similarityAdd BLAST57
<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_000002592378 – 404Aspergillopepsin-1Add BLAST327

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>Glycosylationi140N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi329 ↔ 364PROSITE-ProRule annotation

<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

Two isozymes of this enzyme exist which differ only by their non-covalent association with carbohydrate.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

<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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q06902

Database of comparative protein structure models

More...
ModBasei
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

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>Domaini95 – 401Peptidase A1PROSITE-ProRule annotationAdd BLAST307

<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 peptidase A1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013253_0_1_1

Identification of Orthologs from Complete Genome Data

More...
OMAi
PSSHCRF

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06097, Aspergillopepsin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.70.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001461, Aspartic_peptidase_A1
IPR001969, Aspartic_peptidase_AS
IPR034163, Aspergillopepsin-like_cat_dom
IPR033121, PEPTIDASE_A1
IPR021109, Peptidase_aspartic_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR47966, PTHR47966, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00026, Asp, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00792, PEPSIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50630, SSF50630, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00141, ASP_PROTEASE, 2 hits
PS51767, PEPTIDASE_A1, 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.

Q06902-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVILSKVAAV AVGLSTVASA LPTGPSHSPH ARRGFTINQI TRQTARVGPK
60 70 80 90 100
TASFPAIYSR ALAKYGGTVP AHLKSAVASG HGTVVTSPEP NDIEYLTPVN
110 120 130 140 150
IGGTTLNLDF DTGSADLWVF SEELPKSEQT GHDVYKPSGN ASKIAGASWD
160 170 180 190 200
ISYGDGSSAS GDVYQDTVTV GGVTAQGQAV EAASKISDQF VQDKNNDGLL
210 220 230 240 250
GLAFSSINTV KPKPQTTFFD TVKDQLDAPL FAVTLKYHAP GSYDFGFIDK
260 270 280 290 300
SKFTGELAYA DVDDSQGFWQ FTADGYSVGK GDAQKAPITG IADTGTTLVM
310 320 330 340 350
LDDEIVDAYY KQVQGAKNDA SAGGYVFPCE TELPEFTVVI GSYNAVIPGK
360 370 380 390 400
HINYAPLQEG SSTCVGGIQS NSGLGLSILG DVFLKSQYVV FDSQGPRLGF

AAQA
Length:404
Mass (Da):42,313
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:iBFC21C29EC0A24DF
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 conflicti289T → S in BAA02994 (PubMed:7763981).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
D13894 Genomic DNA Translation: BAA02994.1
M92927 Genomic DNA Translation: AAA32704.1
AP007166 Genomic DNA Translation: BAE63042.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JN0630

NCBI Reference Sequences

More...
RefSeqi
XP_001824175.1, XM_001824123.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
BAE63042; BAE63042; AO090120000474

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5996434

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
aor:AO090120000474

<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
D13894 Genomic DNA Translation: BAA02994.1
M92927 Genomic DNA Translation: AAA32704.1
AP007166 Genomic DNA Translation: BAE63042.1
PIRiJN0630
RefSeqiXP_001824175.1, XM_001824123.2

3D structure databases

SMRiQ06902
ModBaseiSearch...

Protein family/group databases

MEROPSiA01.026

Genome annotation databases

EnsemblFungiiBAE63042; BAE63042; AO090120000474
GeneIDi5996434
KEGGiaor:AO090120000474

Organism-specific databases

VEuPathDBiFungiDB:AO090120000474

Phylogenomic databases

HOGENOMiCLU_013253_0_1_1
OMAiPSSHCRF

Enzyme and pathway databases

BRENDAi3.4.23.18, 522

Family and domain databases

CDDicd06097, Aspergillopepsin_like, 1 hit
Gene3Di2.40.70.10, 2 hits
InterProiView protein in InterPro
IPR001461, Aspartic_peptidase_A1
IPR001969, Aspartic_peptidase_AS
IPR034163, Aspergillopepsin-like_cat_dom
IPR033121, PEPTIDASE_A1
IPR021109, Peptidase_aspartic_dom_sf
PANTHERiPTHR47966, PTHR47966, 1 hit
PfamiView protein in Pfam
PF00026, Asp, 1 hit
PRINTSiPR00792, PEPSIN
SUPFAMiSSF50630, SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS00141, ASP_PROTEASE, 2 hits
PS51767, PEPTIDASE_A1, 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 nameiPEPA_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: Q06902
Secondary accession number(s): Q00249, Q2U5X3
<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: February 1, 1995
Last sequence update: May 2, 2006
Last modified: September 29, 2021
This is version 137 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

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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