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Protein

Dual function macrocyclase-peptidase POPB

Gene

POPB

Organism
Galerina marginata (strain CBS 339.88)
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

Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=23 µM for the full alpha-amanitin 35mer proprotein1 Publication
  2. KM=51 µM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIC1 Publication
  3. KM=19 µM for the 25mer LWGIGCNPWTAEHVDQTLASGNDIC1 Publication
  4. KM=8 µM for the 25mer IFGIGCNPWTAEHVDQTLASGNDIC1 Publication
  5. KM=28 µM for the 25mer IWGIGSNPWTAEHVDQTLASGNDIC1 Publication
  6. KM=10 µM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIS1 Publication
  7. KM=25 µM for the 19mer IWGIGCNPDQTLASGNDIC1 Publication
  8. KM=380 µM for the 14mer IWGIGCNPWTAEHV1 Publication
  9. KM=24.4 µM for the 13mer IWGIGCNPWTAEH1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei577Charge relay systemPROSITE-ProRule annotation1 Publication1
    Active sitei661Charge relay systemPROSITE-ProRule annotation1 Publication1
    Active sitei698Charge relay systemPROSITE-ProRule annotation1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    <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

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...
    ESTHERi
    9agar-h2e7q8 S9N_PPCE_Peptidase_S9

    <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_and_taxonomy_section">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:
    Dual function macrocyclase-peptidase POPB1 Publication (EC:3.4.21.262 Publications)
    Alternative name(s):
    Prolyl oligopeptidase B1 Publication
    Short name:
    POP B1 Publication
    Toxin-processing prolyl oligopeptidase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:POPB1 Publication
    ORF Names:GALMADRAFT_78538
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiGalerina marginata (strain CBS 339.88)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri685588 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesStrophariaceaeGalerina
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000027222 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unassembled WGS sequence

    <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_and_biotech_section">'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>Mutagenesisi577S → A: Impairs catalytic activity but still binds bith 35mer and 25mer substrates. 1 Publication1
    Mutagenesisi661D → A: Impairs catalytic activity but still binds bith 35mer and 25mer substrates. 1 Publication1
    Mutagenesisi663R → A, K or Q: Leads to diminished activities for both peptide bond hydrolysis and macrocyclization. 1 Publication1
    Mutagenesisi695Missing : Leads to diminished activities for both peptide bond hydrolysis and macrocyclization. 1 Publication1
    Mutagenesisi698H → A: Impairs catalytic activity but still binds bith 35mer and 25mer substrates. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004437171 – 730Dual function macrocyclase-peptidase POPBAdd BLAST730

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.By similarity

    <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

    1730
    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
    H2E7Q8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 peptidase S9A family.Curated

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1820, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058 AB_hydrolase
    IPR002471 Pept_S9_AS
    IPR023302 Pept_S9A_N
    IPR001375 Peptidase_S9
    IPR002470 Peptidase_S9A

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00326 Peptidase_S9, 1 hit
    PF02897 Peptidase_S9_N, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00862 PROLIGOPTASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53474 SSF53474, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00708 PRO_ENDOPEP_SER, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    H2E7Q8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSSVTWAPGN YPSTRRSDHV DTYQSASKGE VPVPDPYQWL EESTDEVDKW
    60 70 80 90 100
    TTAQADLAQS YLDQNADIQK LAEKFRASRN YAKFSAPTLL DDGHWYWFYN
    110 120 130 140 150
    RGLQSQSVLY RSKEPALPDF SKGDDNVGDV FFDPNVLAAD GSAGMVLCKF
    160 170 180 190 200
    SPDGKFFAYA VSHLGGDYST IYVRSTSSPL SQASVAQGVD GRLSDEVKWF
    210 220 230 240 250
    KFSTIIWTKD SKGFLYQRYP ARERHEGTRS DRNAMMCYHK VGTTQEEDII
    260 270 280 290 300
    VYQDNEHPEW IYGADTSEDG KYLYLYQFKD TSKKNLLWVA ELDEDGVKSG
    310 320 330 340 350
    IHWRKVVNEY AADYNIITNH GSLVYIKTNL NAPQYKVITI DLSKDEPEIR
    360 370 380 390 400
    DFIPEEKDAK LAQVNCANEE YFVAIYKRNV KDEIYLYSKA GVQLTRLAPD
    410 420 430 440 450
    FVGAASIANR QKQTHFFLTL SGFNTPGTIA RYDFTAPETQ RFSILRTTKV
    460 470 480 490 500
    NELDPDDFES TQVWYESKDG TKIPMFIVRH KSTKFDGTAA AIQYGYGGFA
    510 520 530 540 550
    TSADPFFSPI ILTFLQTYGA IFAVPSIRGG GEFGEEWHKG GRRETKVNTF
    560 570 580 590 600
    DDFIAAAQFL VKNKYAAPGK VAINGASNGG LLVMGSIVRA PEGTFGAAVP
    610 620 630 640 650
    EGGVADLLKF HKFTGGQAWI SEYGNPSIPE EFDYIYPLSP VHNVRTDKVM
    660 670 680 690 700
    PATLITVNIG DGRVVPMHSF KFIATLQHNV PQNPHPLLIK IDKSWLGHGM
    710 720 730
    GKPTDKNVKD AADKWGFIAR ALGLELKTVE
    Length:730
    Mass (Da):81,781
    Last modified:January 22, 2014 - 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:i354827749ED68A4B
    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
    JN827314 mRNA Translation: AEX26938.2
    KL142408 Genomic DNA Translation: KDR68475.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    KDR68475; KDR68475; GALMADRAFT_78538

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Protein Spotlight

    More to it - Issue 202 of April 2018

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    JN827314 mRNA Translation: AEX26938.2
    KL142408 Genomic DNA Translation: KDR68475.1

    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
    5N4BX-ray1.44A/B1-730[»]
    5N4CX-ray2.19A/B/C/D1-730[»]
    5N4DX-ray1.62A/B1-730[»]
    5N4EX-ray2.90A/B1-730[»]
    5N4FX-ray2.40A1-730[»]
    SMRiH2E7Q8
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERi9agar-h2e7q8 S9N_PPCE_Peptidase_S9

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiKDR68475; KDR68475; GALMADRAFT_78538

    Family and domain databases

    Gene3Di3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR002471 Pept_S9_AS
    IPR023302 Pept_S9A_N
    IPR001375 Peptidase_S9
    IPR002470 Peptidase_S9A
    PfamiView protein in Pfam
    PF00326 Peptidase_S9, 1 hit
    PF02897 Peptidase_S9_N, 1 hit
    PRINTSiPR00862 PROLIGOPTASE
    SUPFAMiSSF53474 SSF53474, 1 hit
    PROSITEiView protein in PROSITE
    PS00708 PRO_ENDOPEP_SER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiPOPB_GALM3
    <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: H2E7Q8
    Secondary accession number(s): A0A067SC43
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2018
    Last sequence update: January 22, 2014
    Last modified: December 5, 2018
    This is version 24 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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