Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 108 (08 May 2019)
Sequence version 2 (26 Nov 2014)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Aminopeptidase S

Gene

SGR_5809

Organism
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
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

An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).3 Publications

Miscellaneous

Most experiments use protein purified from a commercial source rather than protein that has been overexpressed.Curated

<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 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

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ 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

Calcium activates the enzyme, inhibited by 1,10-phenanthroline, EDTA and EGTA (PubMed:2503378). End-product inhibited by L-amino acids (PubMed:15388919). Non-competitively inhibited by NaF and NaH2PO4 (PubMed:17608735).4 Publications

<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 390 s(-1) with Leu-pNA.1 Publication
  1. KM=0.59 mM for Leu-NH-Np (with zinc as cofactor)1 Publication
  2. KM=0.13 mM for Leu-NH-Np (with manganese as cofactor)1 Publication
  3. KM=0.046 mM for Leu-NH-Np (with cobalt as cofactor)1 Publication
  4. KM=4.1 mM for Ala-NH-Np (with zinc as cofactor)1 Publication
  5. KM=1.74 mM for Ala-NH-Np (with cobalt as cofactor)1 Publication
  6. KM=0.57 mM for Leu-pNA (with zinc as cofactor)1 Publication

    Temperature dependencei

    Stable after heating at 69 degrees Celsius for 5 hours.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi48Calcium2 Publications1
    Metal bindingi49Calcium; via carbonyl oxygen2 Publications1
    Metal bindingi130Zinc 1; catalytic2 Publications1
    Metal bindingi142Zinc 1; catalytic2 Publications1
    Metal bindingi142Zinc 2; catalytic2 Publications1
    <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 sitei176Proton acceptor2 Publications1
    Metal bindingi177Zinc 2; catalytic2 Publications1
    Metal bindingi205Zinc 1; catalytic2 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei291Transition state stabilizer2 Publications1
    Metal bindingi292Zinc 2; catalytic2 Publications1
    Metal bindingi307Calcium2 Publications1
    Metal bindingi311Calcium2 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 functionAminopeptidase, Hydrolase, Protease
    LigandCalcium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    SGRI455632:G1G2X-5896-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.11.24 6035

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P80561

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M28.003

    <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:
    Aminopeptidase S (EC:3.4.11.24)
    Alternative name(s):
    API1 Publication
    SGAP1 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
    Ordered Locus Names:SGR_5809
    <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>OrganismiStreptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
    <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 identifieri455632 [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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
    <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
    • UP000001685 <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: Chromosome

    <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

    GO - Cellular componenti

    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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Sold by several companies as an extracellular extract called Pronase.3 Publications

    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>Mutagenesisi176E → A: KM halves (0.33 mM), kcat reduces by 5 orders of magnitude. 1 Publication1
    Mutagenesisi176E → D or Q: KM decreases (to 0.4 mM), kcat reduces by 4 orders of magnitude. 1 Publication1
    Mutagenesisi291Y → A, F or S: Activity decreases about 100-fold. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB04713 4-Iodo-D-phenylalanine
    DB03660 4-Iodo-L-phenylalanine
    DB02467 L-methionine (S)-S-oxide

    <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 – 452 PublicationsAdd BLAST45
    <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_000017414346 – 329Aminopeptidase SAdd BLAST284
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000431389330 – 445Removed in mature form1 PublicationAdd BLAST116

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bondi290 ↔ 2952 Publications

    Keywords - PTMi

    Disulfide bond, Zymogen

    <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.2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    455632.SGR_5809

    <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

    1445
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1CP7X-ray1.58A46-329[»]
    1F2OX-ray1.70A46-329[»]
    1F2PX-ray1.80A46-329[»]
    1QQ9X-ray1.53A46-329[»]
    1TF8X-ray1.30A46-329[»]
    1TF9X-ray1.30A46-329[»]
    1TKFX-ray1.20A46-329[»]
    1TKHX-ray1.25A46-329[»]
    1TKJX-ray1.15A46-329[»]
    1XBUX-ray1.20A46-322[»]
    1XJOX-ray1.75A46-329[»]

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

    More...
    SMRi
    P80561

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P80561

    <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_and_domains_section">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>Domaini325 – 445P/Homo BPROSITE-ProRule annotationAdd BLAST121

    <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 M28 family. M28A subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105IIU Bacteria
    COG2234 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000268660

    KEGG Orthology (KO)

    More...
    KOi
    K19702

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CDNTSNI

    Database of Orthologous Groups

    More...
    OrthoDBi
    1465483at2

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd03876 M28_SGAP_like, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.60.120.260, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008979 Galactose-bd-like_sf
    IPR041756 M28_SGAP-like
    IPR002884 P_dom
    IPR007484 Peptidase_M28

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01483 P_proprotein, 1 hit
    PF04389 Peptidase_M28, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF49785 SSF49785, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51829 P_HOMO_B, 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.

    <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 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.

    P80561-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRPNRFSLRR SPTAVAAVAL AAVLAAGAPA AQAAGAAAPT AAAAAAPDIP
    60 70 80 90 100
    LANVKAHLTQ LSTIAANNGG NRAHGRPGYK ASVDYVKAKL DAAGYTTTLQ
    110 120 130 140 150
    QFTSGGATGY NLIADWPGGD PNKVLMAGAH LDSVSSGAGI NDNGSGSAAV
    160 170 180 190 200
    LETALAVSRA GYQPDKHLRF AWWGAEELGL IGSKYYVNNL PSADRSKLAG
    210 220 230 240 250
    YLNFDMIGSP NPGYFVYDDD PVIEKTFKDY FAGLNVPTEI ETEGDGRSDH
    260 270 280 290 300
    APFKNVGVPV GGLFTGAGYT KSAAQAQKWG GTAGQAFDRC YHSSCDSLSN
    310 320 330 340 350
    INDTALDRNS DAAAHAIWTL SSGTGEPPTG EGVFSNTTDV AIPDAGAAVT
    360 370 380 390 400
    SSVAVTGRTG NAPAALQVGV DIKHTYRGDL VVDLLAPDGT AYRLKNSSSG
    410 420 430 440
    DSADNVIATY TVNASSEVAN GSWKLRVQDI ARQDTGYIDS WKLTF
    Length:445
    Mass (Da):45,940
    Last modified:November 26, 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:i6B42B63191F700C9
    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 conflicti185Y → F AA sequence (PubMed:8665903).1
    Sequence conflicti285Q → R no nucleotide entry (PubMed:15280041).1

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 29728±1.0 Da from positions 46 - 329. Determined by ESI. 1 Publication

    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
    AP009493 Genomic DNA Translation: BAG22638.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S66427

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012381549.1, NC_010572.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAG22638; BAG22638; SGR_5809

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    6210128

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sgr:SGR_5809

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|455632.4.peg.5952

    <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
    AP009493 Genomic DNA Translation: BAG22638.1
    PIRiS66427
    RefSeqiWP_012381549.1, NC_010572.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CP7X-ray1.58A46-329[»]
    1F2OX-ray1.70A46-329[»]
    1F2PX-ray1.80A46-329[»]
    1QQ9X-ray1.53A46-329[»]
    1TF8X-ray1.30A46-329[»]
    1TF9X-ray1.30A46-329[»]
    1TKFX-ray1.20A46-329[»]
    1TKHX-ray1.25A46-329[»]
    1TKJX-ray1.15A46-329[»]
    1XBUX-ray1.20A46-322[»]
    1XJOX-ray1.75A46-329[»]
    SMRiP80561
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi455632.SGR_5809

    Chemistry databases

    DrugBankiDB04713 4-Iodo-D-phenylalanine
    DB03660 4-Iodo-L-phenylalanine
    DB02467 L-methionine (S)-S-oxide

    Protein family/group databases

    MEROPSiM28.003

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAG22638; BAG22638; SGR_5809
    GeneIDi6210128
    KEGGisgr:SGR_5809
    PATRICifig|455632.4.peg.5952

    Phylogenomic databases

    eggNOGiENOG4105IIU Bacteria
    COG2234 LUCA
    HOGENOMiHOG000268660
    KOiK19702
    OMAiCDNTSNI
    OrthoDBi1465483at2

    Enzyme and pathway databases

    BioCyciSGRI455632:G1G2X-5896-MONOMER
    BRENDAi3.4.11.24 6035
    SABIO-RKiP80561

    Miscellaneous databases

    EvolutionaryTraceiP80561

    Family and domain databases

    CDDicd03876 M28_SGAP_like, 1 hit
    Gene3Di2.60.120.260, 1 hit
    InterProiView protein in InterPro
    IPR008979 Galactose-bd-like_sf
    IPR041756 M28_SGAP-like
    IPR002884 P_dom
    IPR007484 Peptidase_M28
    PfamiView protein in Pfam
    PF01483 P_proprotein, 1 hit
    PF04389 Peptidase_M28, 1 hit
    SUPFAMiSSF49785 SSF49785, 1 hit
    PROSITEiView protein in PROSITE
    PS51829 P_HOMO_B, 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 nameiAPX_STRGG
    <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: P80561
    Secondary accession number(s): B1W291
    <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: February 1, 1996
    Last sequence update: November 26, 2014
    Last modified: May 8, 2019
    This is version 108 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 programProkaryotic 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, 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
    3. Peptidase families
      Classification of peptidase families and list of entries
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again