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UniProtKB - Q06902 (PEPA_ASPOR)

Entry version 133 (17 Jun 2020)
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

    Complete GO annotation on QuickGO ...

    <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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › 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

    <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 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

    KEGG Orthology (KO)

    More...    KOi    		K06004

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		FQQLSMT

    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    		PTHR13683 PTHR13683, 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

    Phylogenomic databases

    HOGENOMiCLU_013253_0_1_1
    KOiK06004
    OMAiFQQLSMT

    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
    PANTHERiPTHR13683 PTHR13683, 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

    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 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: June 17, 2020
    This is version 133 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. SIMILARITY comments
      Index of protein domains and families
    2. Peptidase families
      Classification of peptidase families and list of entries
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