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Protein

mRNA cap guanine-N7 methyltransferase

Gene

ABD1

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
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

mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.1 Publication

<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=1 mM for GTP1 Publication
  2. KM=25 µM for S-adenosyl-L-methionine1 Publication
  3. KM=0.1 mM for cap dinucleotide GpppA1 Publication

    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 sitei39S-adenosyl-L-methioninePROSITE-ProRule annotation1
    Binding sitei57S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
    <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>Sitei60mRNA cap bindingPROSITE-ProRule annotation1
    Sitei66mRNA cap bindingPROSITE-ProRule annotation1
    Binding sitei79S-adenosyl-L-methioninePROSITE-ProRule annotation1
    Sitei91mRNA cap bindingPROSITE-ProRule annotation1
    Binding sitei107S-adenosyl-L-methionine; via amide nitrogenBy similarity1
    Binding sitei125S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
    Sitei129mRNA cap bindingPROSITE-ProRule annotation1
    Binding sitei130S-adenosyl-L-methionineBy similarity1
    Sitei210mRNA cap bindingPROSITE-ProRule annotation1
    Sitei269mRNA cap bindingPROSITE-ProRule annotation1

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

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionMethyltransferase, RNA-binding, Transferase
    Biological processmRNA capping, mRNA processing
    LigandS-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.1.56 7412

    <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:
    mRNA cap guanine-N7 methyltransferase (EC:2.1.1.56By similarity)
    Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
    mRNA cap methyltransferase
    <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:ABD1
    Ordered Locus Names:ECU10_0380
    <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>OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
    <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 identifieri284813 [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 lineageiEukaryotaFungiFungi incertae sedisMicrosporidiaUnikaryonidaeEncephalitozoon
    <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
    • UP000000819 <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 X

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    MicrosporidiaDB:ECU10_0380

    <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

    Nucleus

    <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>Mutagenesisi32R → A: No effect. Loss of activity; when associated with A-60. 1 Publication1
    Mutagenesisi35N → A: No effect. Loss of activity; when associated with A-269. 1 Publication1
    Mutagenesisi36N → A: Reduces activity by 85%. 2 Publications1
    Mutagenesisi36N → D: Reduces activity by 96%. 2 Publications1
    Mutagenesisi39K → A, Q or R: Loss of activity. 3 Publications1
    Mutagenesisi55D → A or N: Reduces activity by 95%. 2 Publications1
    Mutagenesisi55D → E: Reduces activity by 60%. 2 Publications1
    Mutagenesisi60K → A: Reduces activity by 92%. Loss of activity; when associated with A-32. 2 Publications1
    Mutagenesisi63D → A or N: Reduces activity by 99%. 3 Publications1
    Mutagenesisi63D → E: Reduces activity by 75%. 3 Publications1
    Mutagenesisi66K → A: Reduces activity by 80%. 2 Publications1
    Mutagenesisi66K → Q or R: Reduces activity by 90%. 2 Publications1
    Mutagenesisi79D → A or N: Loss of activity. 3 Publications1
    Mutagenesisi79D → E: Reduces activity by 77%. 3 Publications1
    Mutagenesisi80I → A: No effect. Strongly reduced activity; when associated with A-109. 1 Publication1
    Mutagenesisi91R → A or Q: Reduces activity by over 98%. 2 Publications1
    Mutagenesisi91R → K: Reduces activity by 96%. 2 Publications1
    Mutagenesisi107 – 108DS → AA: Slightly reduced activity. 1 Publication2
    Mutagenesisi109Y → A: Reduces activity by 83%. Strongly reduced activity; when associated with A-80. 2 Publications1
    Mutagenesisi126F → A or N: Loss of activity. 2 Publications1
    Mutagenesisi126F → H: Reduces activity by 92%. 2 Publications1
    Mutagenesisi126F → I: Reduces activity by 75%. 2 Publications1
    Mutagenesisi126F → L: Reduces activity by 55%. 2 Publications1
    Mutagenesisi126F → V: Reduces activity by 84%. 2 Publications1
    Mutagenesisi129H → A: Reduces activity by 53%. Reduces activity by 99%; when associated with L-130. 1 Publication1
    Mutagenesisi130Y → A, S or V: Reduces activity by 98%. 1 Publication1
    Mutagenesisi130Y → F: Reduces activity by 66%. 1 Publication1
    Mutagenesisi130Y → L: Reduces activity by 99%; when associated with A-129. 1 Publication1
    Mutagenesisi201L → A: No effect. 1 Publication1
    Mutagenesisi210E → A: Reduces activity by 87%. 1 Publication1
    Mutagenesisi269Y → A: Reduced activity. Loss of activity; when associated with A-35. 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_00002101421 – 283mRNA cap guanine-N7 methyltransferaseAdd BLAST283

    <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
    284813.NP_586153.1

    <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

    1283
    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
    Q8SR66

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

    More...
    SMRi
    Q8SR66

    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
    Q8SR66

    <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>Domaini1 – 283mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST283

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni35 – 36mRNA cap binding2

    <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 class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1975 Eukaryota
    ENOG410Y7HG LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000242614

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q8SR66

    KEGG Orthology (KO)

    More...
    KOi
    K00565

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C2SMS

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004971 mRNA_G-N7_MeTrfase_dom
    IPR016899 mRNA_G-N7_MeTrfase_euk
    IPR039753 RG7MT1
    IPR029063 SAM-dependent_MTases

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR12189 PTHR12189, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03291 Pox_MCEL, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF028762 ABD1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53335 SSF53335, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51562 RNA_CAP0_MT, 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.

    Q8SR66-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEGKKEEIRE HYNSIRERGR ESRQRSKTIN IRNANNFIKA CLIRLYTKRG
    60 70 80 90 100
    DSVLDLGCGK GGDLLKYERA GIGEYYGVDI AEVSINDARV RARNMKRRFK
    110 120 130 140 150
    VFFRAQDSYG RHMDLGKEFD VISSQFSFHY AFSTSESLDI AQRNIARHLR
    160 170 180 190 200
    PGGYFIMTVP SRDVILERYK QGRMSNDFYK IELEKMEDVP MESVREYRFT
    210 220 230 240 250
    LLDSVNNCIE YFVDFTRMVD GFKRLGLSLV ERKGFIDFYE DEGRRNPELS
    260 270 280
    KKMGLGCLTR EESEVVGIYE VVVFRKLVPE SDA
    Length:283
    Mass (Da):33,074
    Last modified:May 29, 2013 - 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:i40ABA7B1522C7001
    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
    AL590449 Genomic DNA Translation: CAD25757.2

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_586153.1, NM_001041986.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    859802

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecu:ECU10_0380

    <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
    AL590449 Genomic DNA Translation: CAD25757.2
    RefSeqiNP_586153.1, NM_001041986.1

    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
    1RI1X-ray2.50A1-283[»]
    1RI2X-ray2.70A1-283[»]
    1RI3X-ray2.50A1-283[»]
    1RI4X-ray2.40A1-283[»]
    1RI5X-ray2.10A1-283[»]
    1Z3CX-ray2.20A1-283[»]
    2HV9X-ray2.60A1-283[»]
    ProteinModelPortaliQ8SR66
    SMRiQ8SR66
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi284813.NP_586153.1

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi859802
    KEGGiecu:ECU10_0380

    Organism-specific databases

    EuPathDBiMicrosporidiaDB:ECU10_0380

    Phylogenomic databases

    eggNOGiKOG1975 Eukaryota
    ENOG410Y7HG LUCA
    HOGENOMiHOG000242614
    InParanoidiQ8SR66
    KOiK00565
    OrthoDBiEOG092C2SMS

    Enzyme and pathway databases

    BRENDAi2.1.1.56 7412

    Miscellaneous databases

    EvolutionaryTraceiQ8SR66

    Family and domain databases

    InterProiView protein in InterPro
    IPR004971 mRNA_G-N7_MeTrfase_dom
    IPR016899 mRNA_G-N7_MeTrfase_euk
    IPR039753 RG7MT1
    IPR029063 SAM-dependent_MTases
    PANTHERiPTHR12189 PTHR12189, 1 hit
    PfamiView protein in Pfam
    PF03291 Pox_MCEL, 1 hit
    PIRSFiPIRSF028762 ABD1, 1 hit
    SUPFAMiSSF53335 SSF53335, 1 hit
    PROSITEiView protein in PROSITE
    PS51562 RNA_CAP0_MT, 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 nameiMCES_ENCCU
    <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: Q8SR66
    <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, 2005
    Last sequence update: May 29, 2013
    Last modified: December 5, 2018
    This is version 88 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
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