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UniProtKB - P0AF24 (NAGD_ECOLI)

Entry version 112 (13 Nov 2019)
Sequence version 1 (20 Dec 2005)
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Protein

Ribonucleotide monophosphatase NagD

Gene

nagD

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 dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P).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 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

Mg2+2 Publications, Mn2+2 Publications, Co2+2 Publications, Zn2+2 PublicationsNote: Magnesium. Can also use other divalent metal cations as manganese, cobalt or zinc.2 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=160 µM for UMP (at pH 7 and at 25 degrees Celsius)1 Publication
  2. KM=400 µM for GMP (at pH 7 and at 25 degrees Celsius)1 Publication
  3. KM=840 µM for AMP (at pH 7 and at 25 degrees Celsius)1 Publication
  4. KM=840 µM for ribose-5-phosphate (at pH 7 and at 25 degrees Celsius)1 Publication
  5. KM=1470 µM for CMP (at pH 7 and at 25 degrees Celsius)1 Publication
  6. KM=1500 µM for dTMP (at pH 7 and at 25 degrees Celsius)1 Publication
  7. KM=1500 µM for pyridoxal 5-phosphate (at pH 7 and at 25 degrees Celsius)1 Publication
  8. KM=1700 µM for glycerol 3-phosphate (at pH 7 and at 25 degrees Celsius)1 Publication
  9. KM=5900 µM for glucose 6-phosphate (at pH 7 and at 25 degrees Celsius)1 Publication
  10. KM=6000 µM for glucosamine 6-phosphate (at pH 7 and at 25 degrees Celsius)1 Publication
  11. KM=6000 µM for dCMP (at pH 7 and at 25 degrees Celsius)1 Publication
  12. KM=6500 µM for dAMP (at pH 7 and at 25 degrees Celsius)1 Publication
  13. KM=7600 µM for dGMP (at pH 7 and at 25 degrees Celsius)1 Publication
  14. KM=7700 µM for dGMP (at pH 7 and at 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei9Nucleophile1 Publication1
    <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 bindingi9MagnesiumCombined sources1 Publication1
    Active sitei11Proton donor/acceptor1 Publication1
    Metal bindingi11Magnesium; via carbonyl oxygenCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei11Substrate1
    <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>Sitei55Orients D-11 for proton transfer during catalytic turnover1 Publication1
    Sitei146Confers substrate specificity1
    Binding sitei176Substrate1
    Metal bindingi201MagnesiumCombined sources1 Publication1

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

    • 5'-nucleotidase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • phosphatase activity Source: GO_Central
    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 functionHydrolase
    Biological processCarbohydrate metabolism
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG10634-MONOMER
    ECOL316407:JW0661-MONOMER
    MetaCyc:EG10634-MONOMER

    <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:
    Ribonucleotide monophosphatase NagD (EC:3.1.3.51 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:nagD
    Ordered Locus Names:b0675, JW0661
    <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 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

    Complete GO annotation on QuickGO ...

    <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_00000966941 – 250Ribonucleotide monophosphatase NagDAdd BLAST250

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P0AF24

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0AF24

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

    More...    PaxDbi    		P0AF24

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0AF24

    <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

    By N-acetylglucosamine.Curated

    <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.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4259613, 11 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-6861N

    Protein interaction database and analysis system

    More...    IntActi    		P0AF24, 4 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0675

    <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

    1250
    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    		P0AF24

    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    		P0AF24

    <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

    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>Regioni42 – 43Substrate binding2
    Regioni202 – 205Substrate binding4

    <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 HAD-like hydrolase superfamily. NagD family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105D4U Bacteria
    COG0647 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000068105

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0AF24

    KEGG Orthology (KO)

    More...    KOi    		K02566

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0AF24

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.1000, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR036412 HAD-like_sf
    IPR006357 HAD-SF_hydro_IIA
    IPR023214 HAD_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF13344 Hydrolase_6, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF56784 SSF56784, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01460 HAD-SF-IIA, 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.

    P0AF24-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTIKNVICDI DGVLMHDNVA VPGAAEFLHG IMDKGLPLVL LTNYPSQTGQ 
            60         70         80         90        100
    DLANRFATAG VDVPDSVFYT SAMATADFLR RQEGKKAYVV GEGALIHELY 
           110        120        130        140        150
    KAGFTITDVN PDFVIVGETR SYNWDMMHKA AYFVANGARF IATNPDTHGR 
           160        170        180        190        200
    GFYPACGALC AGIEKISGRK PFYVGKPSPW IIRAALNKMQ AHSEETVIVG 
           210        220        230        240        250
    DNLRTDILAG FQAGLETILV LSGVSSLDDI DSMPFRPSWI YPSVAEIDVI
    Length:250
    Mass (Da):27,163
    Last modified:December 20, 2005 - 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:iCC256AE6FF58DEBA
    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 conflicti97H → Y in AAC09327 (PubMed:2190615).Curated1

    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
    		X14135 Genomic DNA Translation: CAA32355.1
    AF052007 Genomic DNA Translation: AAC09327.1
    U00096 Genomic DNA Translation: AAC73769.1
    AP009048 Genomic DNA Translation: BAA35318.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		B64802

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415201.1, NC_000913.3
    WP_000153129.1, NZ_STEB01000044.1
    WP_000153136.1, NZ_CP014272.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73769; AAC73769; b0675
    BAA35318; BAA35318; BAA35318

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		945283

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0661
    eco:b0675

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|511145.12.peg.700

    <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
    		X14135 Genomic DNA Translation: CAA32355.1
    AF052007 Genomic DNA Translation: AAC09327.1
    U00096 Genomic DNA Translation: AAC73769.1
    AP009048 Genomic DNA Translation: BAA35318.1
    PIRiB64802
    RefSeqiNP_415201.1, NC_000913.3
    WP_000153129.1, NZ_STEB01000044.1
    WP_000153136.1, NZ_CP014272.1

    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
    2C4NX-ray1.80A1-250[»]
    SMRiP0AF24
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259613, 11 interactors
    DIPiDIP-6861N
    IntActiP0AF24, 4 interactors
    STRINGi511145.b0675

    Proteomic databases

    EPDiP0AF24
    jPOSTiP0AF24
    PaxDbiP0AF24
    PRIDEiP0AF24

    Genome annotation databases

    EnsemblBacteriaiAAC73769; AAC73769; b0675
    BAA35318; BAA35318; BAA35318
    GeneIDi945283
    KEGGiecj:JW0661
    eco:b0675
    PATRICifig|511145.12.peg.700

    Organism-specific databases

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

    More...    EchoBASEi    		EB0628

    Phylogenomic databases

    eggNOGiENOG4105D4U Bacteria
    COG0647 LUCA
    HOGENOMiHOG000068105
    InParanoidiP0AF24
    KOiK02566
    PhylomeDBiP0AF24

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10634-MONOMER
    ECOL316407:JW0661-MONOMER
    MetaCyc:EG10634-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP0AF24

    Protein Ontology

    More...    PROi    		PR:P0AF24

    Family and domain databases

    Gene3Di3.40.50.1000, 2 hits
    InterProiView protein in InterPro
    IPR036412 HAD-like_sf
    IPR006357 HAD-SF_hydro_IIA
    IPR023214 HAD_sf
    PfamiView protein in Pfam
    PF13344 Hydrolase_6, 1 hit
    SUPFAMiSSF56784 SSF56784, 1 hit
    TIGRFAMsiTIGR01460 HAD-SF-IIA, 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 nameiNAGD_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: P0AF24
    Secondary accession number(s): P15302
    <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: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: November 13, 2019
    This is version 112 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 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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