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UniProtKB - P37329 (MODA_ECOLI)

Entry version 161 (07 Apr 2021)
Sequence version 1 (01 Oct 1994)
Previous versions | rss
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Protein

Molybdate-binding protein ModA

Gene

modA

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

Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (PubMed:8576221). Binds molybdate with high affinity in vitro and with a similar affinity in vivo (PubMed:21861186, PubMed:28150901, PubMed:9545596, PubMed:8576221, PubMed:21784948, PubMed:8409926). Binds tungstate with high affinity in vitro (PubMed:28150901, PubMed:9545596, PubMed:8576221, PubMed:21784948). Binds unnatural anion perrhenate with high affinity in vitro (PubMed:21861186). Does not bind sulfate, phosphate, arsenate, selenate, chlorate, metavanadate, nitrate, perchlorate, permanganate or carbonate (PubMed:9545596, PubMed:28150901, PubMed:8576221).6 Publications

Caution

According to a report, does not bind chromate (PubMed:8576221). According to another report, binds chromate with high affinity and is able to remove it from an aqueous solution in vitro (PubMed:28150901).2 Publications
The mod operon containing this protein has previously been called the chlD locus.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi36MolybdateCombined sources1 Publication1
Metal bindingi63MolybdateCombined sources1 Publication1
Metal bindingi149Molybdate; via amide nitrogenCombined sources1 Publication1
Metal bindingi176Molybdate; via amide nitrogenCombined sources1 Publication1
Metal bindingi194MolybdateCombined 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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • molybdate ion transport Source: EcoCyc
  • response to chromate Source: UniProtKB-KW
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

Biological processChromate resistance, Transport
LigandMetal-binding, Molybdenum, Tungsten

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:MODA-MONOMER
MetaCyc:MODA-MONOMER

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.1.8.1, the atp-binding cassette (abc) superfamily

<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%5Fand%5Ftaxonomy%5Fsection">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:
Molybdate-binding protein ModA3 Publications
Alternative name(s):
Molybdate/tungstate-binding protein ModACurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:modA
Ordered Locus Names:b0763, JW0746
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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

May be useful in radiopharmaceutical applications as an engineered disulfide bond-containing protein with increased affinity for perrhenate (PubMed:21861186). May be used to remove chromate, which is toxic to many biological systems, from environmental aqueous solutions (PubMed:28150901).2 Publications

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells are unable to transport molybdate unless high levels of it is supplied in the culture medium.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi35A → C: About 5-fold increased binding affinity for perrhenate as a result of formation of an intramolecular disulfide bond with mutant C-177, which stabilizes the metal-bound closed conformation, but no increased binding affinity for molybdate; when associated with C-177. 1 Publication1
Mutagenesisi36S → A: Loss of chromate removal from a buffered solution; when associated with A-63. 1 Publication1
Mutagenesisi36S → C: Loss of binding to perrhenate. Slightly reduced chromate removal from a buffered solution. 2 Publications1
Mutagenesisi36S → D: Loss of binding to perrhenate. Slightly reduced chromate removal from a buffered solution. Significantly reduced chromate removal from a buffered solution; when associated with D-63. 2 Publications1
Mutagenesisi36S → E: Slightly reduced chromate removal from a buffered solution. 1 Publication1
Mutagenesisi63S → A: Loss of chromate removal from a buffered solution; when associated with A-36. 1 Publication1
Mutagenesisi63S → C: Reduced binding affinity for perrhenate. 1 Publication1
Mutagenesisi63S → D: Reduced binding affinity for perrhenate. Significantly reduced chromate removal from a buffered solution; when associated with D-36. 2 Publications1
Mutagenesisi175D → N: Reduced binding affinity for perrhenate. 1 Publication1
Mutagenesisi177R → C: About 5-fold increased binding affinity for perrhenate as a result of formation of an intramolecular disulfide bond with mutant C-35, which stabilizes the metal-bound closed conformation, but no increased binding affinity for molybdate; when associated with C-35. 1 Publication1
Mutagenesisi199V → A, Y or W: No change in affinity for perrhenate. 1 Publication1
Mutagenesisi218V → A, Y or W: No change in affinity for perrhenate. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 241 PublicationAdd BLAST24
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003182725 – 257Molybdate-binding protein ModAAdd BLAST233

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P37329

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

More...PaxDbi		P37329

PRoteomics IDEntifications database

More...PRIDEi		P37329

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P37329

<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 up-regulated by molybdate limitation (PubMed:7860583). Repressed by molybdate-bound ModE (PubMed:8550508).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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The complex is composed of two ATP-binding proteins (ModC), two transmembrane proteins (ModB) and a solute-binding protein (ModA).

Curated

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262087, 14 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-4342, Molybdate ABC transporter complex

Protein interaction database and analysis system

More...IntActi		P37329, 1 interactor

STRING: functional protein association networks

More...STRINGi		511145.b0763

<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

1257
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		P37329

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		P37329

<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 bacterial solute-binding protein ModA family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0725, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_065520_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P37329

Database for complete collections of gene phylogenies

More...PhylomeDBi		P37329

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005950, ModA

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF004846, ModA, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01256, modA, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P37329-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARKWLNLFA GAALSFAVAG NALADEGKIT VFAAASLTNA MQDIATQFKK 
        60         70         80         90        100
EKGVDVVSSF ASSSTLARQI EAGAPADLFI SADQKWMDYA VDKKAIDTAT 
       110        120        130        140        150
RQTLLGNSLV VVAPKASVQK DFTIDSKTNW TSLLNGGRLA VGDPEHVPAG 
       160        170        180        190        200
IYAKEALQKL GAWDTLSPKL APAEDVRGAL ALVERNEAPL GIVYGSDAVA 
       210        220        230        240        250
SKGVKVVATF PEDSHKKVEY PVAVVEGHNN ATVKAFYDYL KGPQAAEIFK 

RYGFTIK
Length:257
Mass (Da):27,364
Last modified:October 1, 1994 - 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:i847DB740EE0564E7
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
L34009 Genomic DNA Translation: AAB00835.1
U27192 Genomic DNA Translation: AAB60171.1
U07867 Genomic DNA Translation: AAB06893.1
U00096 Genomic DNA Translation: AAC73850.1
AP009048 Genomic DNA Translation: BAA35427.1

Protein sequence database of the Protein Information Resource

More...PIRi		C64812

NCBI Reference Sequences

More...RefSeqi		NP_415284.1, NC_000913.3
WP_000101984.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73850; AAC73850; b0763
BAA35427; BAA35427; BAA35427

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57728442
945364

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0746
eco:b0763

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1515

<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
L34009 Genomic DNA Translation: AAB00835.1
U27192 Genomic DNA Translation: AAB60171.1
U07867 Genomic DNA Translation: AAB06893.1
U00096 Genomic DNA Translation: AAC73850.1
AP009048 Genomic DNA Translation: BAA35427.1
PIRiC64812
RefSeqiNP_415284.1, NC_000913.3
WP_000101984.1, NZ_LN832404.1

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
1AMFX-ray1.75A25-257[»]
1WODX-ray1.75A25-257[»]
3AXFX-ray2.00A/B/C25-257[»]
3R26X-ray1.70A25-257[»]
4XXUX-ray1.43A/B1-257[»]
SMRiP37329
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262087, 14 interactors
ComplexPortaliCPX-4342, Molybdate ABC transporter complex
IntActiP37329, 1 interactor
STRINGi511145.b0763

Protein family/group databases

TCDBi3.A.1.8.1, the atp-binding cassette (abc) superfamily

2D gel databases

SWISS-2DPAGEiP37329

Proteomic databases

jPOSTiP37329
PaxDbiP37329
PRIDEiP37329

Genome annotation databases

EnsemblBacteriaiAAC73850; AAC73850; b0763
BAA35427; BAA35427; BAA35427
GeneIDi57728442
945364
KEGGiecj:JW0746
eco:b0763
PATRICifig|1411691.4.peg.1515

Organism-specific databases

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

More...EchoBASEi		EB2325

Phylogenomic databases

eggNOGiCOG0725, Bacteria
HOGENOMiCLU_065520_3_0_6
InParanoidiP37329
PhylomeDBiP37329

Enzyme and pathway databases

BioCyciEcoCyc:MODA-MONOMER
MetaCyc:MODA-MONOMER

Miscellaneous databases

EvolutionaryTraceiP37329

Protein Ontology

More...PROi		PR:P37329

Family and domain databases

InterProiView protein in InterPro
IPR005950, ModA
PIRSFiPIRSF004846, ModA, 1 hit
TIGRFAMsiTIGR01256, modA, 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 nameiMODA_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: P37329
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 7, 2021
This is version 161 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, 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
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