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UniProtKB - P56221 (SCYD_MAGO7)

Protein

Scytalone dehydratase

Gene

SDH1

Organism
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
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

Scytalone dehydratase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:9571787). Within the pathway, catalyzes the dehydration of scytalone as well as of vermelone (PubMed:9571787, PubMed:9466791, PubMed:9466792, PubMed:9539706, PubMed:10320327, PubMed:10386945, PubMed:10386946, PubMed:10694394, PubMed:10913266, PubMed:10636235, PubMed:11790103, PubMed:12413868, PubMed:15056895). Is also able to dehydrate the alternate substrate 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one (DDBO) to 5-hydroxy-4H-1-benzopyran-4-one (HBO) (PubMed:9466791, PubMed:9466792, PubMed:10320327, PubMed:10386945, PubMed:11790103).13 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 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

(N-phenoxypropyl)-carboxamides such as carpropamid and derivatives of norephedrine act as inhibitors of scytalone dehydratase activity.6 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

  1. KM=15 µM for 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one (DDBO)2 Publications
  2. KM=33 µM for scytalone1 Publication
  3. KM=31 µM for vermelone2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: melanin biosynthesis

    This protein is involved in the pathway melanin biosynthesis, which is part of Pigment biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway melanin biosynthesis and in Pigment biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei30Substrate1 Publication1
    Binding sitei50Substrate1 Publication1
    Binding sitei53Substrate; via carbonyl oxygen1 Publication1
    <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 sitei851 Publication1
    Active sitei1101 Publication1
    Binding sitei131Substrate3 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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the 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 functionLyase
    Biological processMelanin biosynthesis
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		4.2.1.94 3152

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi
    UPA00785

    <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:
    Scytalone dehydratase1 Publication (EC:4.2.1.946 Publications)
    Short name:
    SD1 Publication
    Short name:
    SDH1 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:SDH1
    ORF Names:MGG_05059
    <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>OrganismiMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
    <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 identifieri242507 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe ›
    <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
    • UP000009058 <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 3

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		FungiDB:MGG_05059

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Endosome

    <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>Mutagenesisi30Y → F: Results in a 9-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. 2 Publications1
    Mutagenesisi31D → N: Reduces catalysis 5000-fold and substrate affinity about 4-fold with scytalone as the substrate. 1 Publication1
    Mutagenesisi50Y → F: Results in a 500-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. 2 Publications1
    Mutagenesisi53F → A: Leads to significantly higher relative substrate specificities (DDBO/vermelone). 1 Publication1
    Mutagenesisi53F → L: Affects the binding of inhibitors and has significantly higher relative substrate specificities (DDBO/vermelone). 2 Publications1
    Mutagenesisi69M → L: Affects the binding of inhibitors. 1 Publication1
    Mutagenesisi75V → A: Affects the binding of inhibitors and reduces more than 200-fold inhibition by carpropamid. 2 Publications1
    Mutagenesisi75V → M: Reduces strongly inhibition by carpropamid. 1 Publication1
    Mutagenesisi85H → N: Greatly decreases catalytic efficiency and decreases binding to salicylamide inhibitors. 2 Publications1
    Mutagenesisi110H → N: Causes a 250-fold decrease of activity and a 6-fold increase in Km with scytalone as the substrate, decreases binding of salicylamide inhibitors, and has significantly higher relative substrate specificities (DDBO/vermelone). 3 Publications1
    Mutagenesisi129S → A: Results in a 80-fold decrease of activity and a 7-fold increase in Km with scytalone as the substrate. 1 Publication1
    Mutagenesisi129S → T: Results in a 120-fold decrease of activity and a 23-fold increase in Km with scytalone as the substrate. 1 Publication1
    Mutagenesisi131N → A: Decreases turnover by nearly 90-fold and increases Km 8-fold with scytalone as the substrate, decreases strongly binding of salicylamide inhibitors, and has significantly higher relative substrate specificities (DDBO/vermelone). 3 Publications1
    Mutagenesisi158F → L: Affects the binding of inhibitors. 1 Publication1
    Mutagenesisi162F → L: Affects the binding of inhibitors. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL2578

    <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_00000976391 – 172Scytalone dehydrataseAdd BLAST172

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression is induced in the stationary phase, when melanin synthesis occurs (PubMed:9571787). Expression is specifically induced during appressorium formation (PubMed:15378734).2 Publications

    <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

    Homotrimer (PubMed:7866745). Each subunit contains an active site, located in the central part of the hydrophobic core of the monomer, which functions independently (PubMed:7866745).1 Publication

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P56221

    <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

    1172
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P56221

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

    More...    SMRi    		P56221

    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    		P56221

    <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 scytalone dehydratase family.Curated

    Phylogenomic databases

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P56221

    KEGG Orthology (KO)

    More...    KOi    		K17740

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		RKCIAPT

    Database of Orthologous Groups

    More...    OrthoDBi    		EOG092C4YYV

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR032710 NTF2-like_dom_sf
    IPR004235 Scytalone_dehydratase

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02982 Scytalone_dh, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF024851 SCD1, 1 hit

    ProDom; a protein domain database

    More...    ProDomi    		View protein in ProDom or Entries sharing at least one domain
    PD022193 Scytalone_dehydratase, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF54427 SSF54427, 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.

    P56221-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGSQVQKSDE ITFSDYLGLM TCVYEWADSY DSKDWDRLRK VIAPTLRIDY 
            60         70         80         90        100
    RSFLDKLWEA MPAEEFVGMV SSKQVLGDPT LRTQHFIGGT RWEKVSEDEV 
           110        120        130        140        150
    IGYHQLRVPH QRYKDTTMKE VTMKGHAHSA NLHWYKKIDG VWKFAGLKPD 
           160        170 
    IRWGEFDFDR IFEDGRETFG DK
    Length:172
    Mass (Da):20,250
    Last modified:July 15, 1998 - v1
    <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:i2FA56296D5EE00DC
    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
    		AB004741 mRNA Translation: BAA34046.1
    CM001233 Genomic DNA Translation: EHA52765.1

    NCBI Reference Sequences

    More...    RefSeqi    		XP_003712572.1, XM_003712524.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...    EnsemblFungii    		MGG_05059T0; MGG_05059T0; MGG_05059

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		2675492

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mgr:MGG_05059

    <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
    		AB004741 mRNA Translation: BAA34046.1
    CM001233 Genomic DNA Translation: EHA52765.1
    RefSeqiXP_003712572.1, XM_003712524.1

    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
    1IDPX-ray1.45A/B/C1-172[»]
    1STDX-ray2.90A1-172[»]
    2STDX-ray2.10A1-172[»]
    3STDX-ray1.65A/B/C10-172[»]
    4STDX-ray2.15A/B/C10-172[»]
    5STDX-ray1.95A/B/C10-172[»]
    6STDX-ray1.80A/B/C10-172[»]
    7STDX-ray1.80A/B/C10-172[»]
    ProteinModelPortaliP56221
    SMRiP56221
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP56221
    ChEMBLiCHEMBL2578

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiMGG_05059T0; MGG_05059T0; MGG_05059
    GeneIDi2675492
    KEGGimgr:MGG_05059

    Organism-specific databases

    EuPathDBiFungiDB:MGG_05059

    Phylogenomic databases

    InParanoidiP56221
    KOiK17740
    OMAiRKCIAPT
    OrthoDBiEOG092C4YYV

    Enzyme and pathway databases

    UniPathwayi
    UPA00785

    BRENDAi4.2.1.94 3152

    Miscellaneous databases

    EvolutionaryTraceiP56221

    Protein Ontology

    More...    PROi    		PR:P56221

    Family and domain databases

    InterProiView protein in InterPro
    IPR032710 NTF2-like_dom_sf
    IPR004235 Scytalone_dehydratase
    PfamiView protein in Pfam
    PF02982 Scytalone_dh, 1 hit
    PIRSFiPIRSF024851 SCD1, 1 hit
    ProDomiView protein in ProDom or Entries sharing at least one domain
    PD022193 Scytalone_dehydratase, 1 hit
    SUPFAMiSSF54427 SSF54427, 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 nameiSCYD_MAGO7
    <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: P56221
    Secondary accession number(s): A4QTI6, G4N445
    <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: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: December 5, 2018
    This is version 113 of the entry and version 1 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, Direct protein sequencing, 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
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