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UniProtKB - P45425 (NANK_ECOLI)

Entry version 134 (11 Dec 2019)
Sequence version 2 (15 Dec 1998)
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Protein

N-acetylmannosamine kinase

Gene

nanK

Organism
Escherichia coli (strain K12)
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

Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. Has also low level glucokinase activity in vitro.2 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

Catalytic efficiency with N-acyl-D-mannosamine as substrate is 136-fold higher than that with D-glucose.
  1. KM=0.36 mM for N-acyl-D-mannosamine (at 25 degrees Celsius and pH 7.6)2 Publications
  2. KM=0.26 mM for ATP (at 25 degrees Celsius and pH 7.6)2 Publications
  3. KM=20 mM for D-glucose (at 25 degrees Celsius and pH 7.6)2 Publications
  4. KM=84 mM for D-mannose (at 25 degrees Celsius and pH 7.6)2 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: N-acetylneuraminate degradation

    This protein is involved in step 2 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA)
    2. N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK)
    3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE), Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
    4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
    5. Glucosamine-6-phosphate deaminase (nagB), Glucosamine-6-phosphate deaminase (nagB)
    This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi156Zinc1
    Metal bindingi166Zinc1
    Metal bindingi168Zinc1
    Metal bindingi173Zinc1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi5 – 12ATPSequence analysis8
    Nucleotide bindingi132 – 139ATPSequence analysis8

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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    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 functionKinase, Transferase
    Biological processCarbohydrate metabolism
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:NANK-MONOMER
    ECOL316407:JW5538-MONOMER
    MetaCyc:NANK-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P45425

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

    More...    UniPathwayi    		UPA00629;UER00681

    <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:
    N-acetylmannosamine kinase (EC:2.7.1.60)
    Alternative name(s):
    ManNAc kinase
    N-acetyl-D-mannosamine kinase
    <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:nanK
    Synonyms:yhcI
    Ordered Locus Names:b3222, JW5538
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    <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>Mutagenesisi84L → P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication1
    Mutagenesisi138V → M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation. 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_00000956951 – 291N-acetylmannosamine kinaseAdd BLAST291

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P45425

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P45425

    PRoteomics IDEntifications database

    More...    PRIDEi    		P45425

    <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

    Negatively regulated by the transcriptional repressor NanR. Induced by N-acetylneuraminate, via inactivation of NanR.1 Publication

    <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

    Homodimer.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4261227, 316 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-12282N

    Protein interaction database and analysis system

    More...    IntActi    		P45425, 1 interactor

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3222

    <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

    1291
    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    		P45425

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P45425

    <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 ROK (NagC/XylR) family. NanK subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG41061DF Bacteria
    COG1940 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000150087

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P45425

    KEGG Orthology (KO)

    More...    KOi    		K00885

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P45425

    Family and domain databases

    HAMAP database of protein families

    More...    HAMAPi    		MF_01234 ManNAc_kinase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR023945 ManNAc_kinase_bac
    IPR000600 ROK

    The PANTHER Classification System

    More...    PANTHERi    		PTHR18964 PTHR18964, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00480 ROK, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS01125 ROK, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_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.

    P45425-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS 
            60         70         80         90        100
    PLQAHAQRVA IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT 
           110        120        130        140        150
    IAINDAQAAA WAEFQALDGD ITDMVFITVS TGVGGGVVSG CKLLTGPGGL 
           160        170        180        190        200
    AGHIGHTLAD PHGPVCGCGR TGCVEAIASG RGIAAAAQGE LAGADAKTIF 
           210        220        230        240        250
    TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG GSVGLAEGYL 
           260        270        280        290 
    ALVETYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L
    Length:291
    Mass (Da):29,644
    Last modified:December 15, 1998 - 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:iE3109E2756B08612
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA58024 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    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
    		U18997 Genomic DNA Translation: AAA58024.1 Different initiation.
    U00096 Genomic DNA Translation: AAC76254.2
    AP009048 Genomic DNA Translation: BAE77265.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		H65113

    NCBI Reference Sequences

    More...    RefSeqi    		NP_417689.4, NC_000913.3
    WP_000209011.1, NZ_SSZK01000034.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC76254; AAC76254; b3222
    BAE77265; BAE77265; BAE77265

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		947757

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW5538
    eco:b3222

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.3506

    <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
    		U18997 Genomic DNA Translation: AAA58024.1 Different initiation.
    U00096 Genomic DNA Translation: AAC76254.2
    AP009048 Genomic DNA Translation: BAE77265.1
    PIRiH65113
    RefSeqiNP_417689.4, NC_000913.3
    WP_000209011.1, NZ_SSZK01000034.1

    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
    2AA4X-ray2.20A/B1-289[»]
    SMRiP45425
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4261227, 316 interactors
    DIPiDIP-12282N
    IntActiP45425, 1 interactor
    STRINGi511145.b3222

    Proteomic databases

    jPOSTiP45425
    PaxDbiP45425
    PRIDEiP45425

    Genome annotation databases

    EnsemblBacteriaiAAC76254; AAC76254; b3222
    BAE77265; BAE77265; BAE77265
    GeneIDi947757
    KEGGiecj:JW5538
    eco:b3222
    PATRICifig|1411691.4.peg.3506

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB2666

    Phylogenomic databases

    eggNOGiENOG41061DF Bacteria
    COG1940 LUCA
    HOGENOMiHOG000150087
    InParanoidiP45425
    KOiK00885
    PhylomeDBiP45425

    Enzyme and pathway databases

    UniPathwayiUPA00629;UER00681
    BioCyciEcoCyc:NANK-MONOMER
    ECOL316407:JW5538-MONOMER
    MetaCyc:NANK-MONOMER
    SABIO-RKiP45425

    Miscellaneous databases

    EvolutionaryTraceiP45425

    Protein Ontology

    More...    PROi    		PR:P45425

    Family and domain databases

    HAMAPiMF_01234 ManNAc_kinase, 1 hit
    InterProiView protein in InterPro
    IPR023945 ManNAc_kinase_bac
    IPR000600 ROK
    PANTHERiPTHR18964 PTHR18964, 1 hit
    PfamiView protein in Pfam
    PF00480 ROK, 1 hit
    PROSITEiView protein in PROSITE
    PS01125 ROK, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNANK_ECOLI
    <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: P45425
    Secondary accession number(s): Q2M8Z1
    <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: November 1, 1995
    Last sequence update: December 15, 1998
    Last modified: December 11, 2019
    This is version 134 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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