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Entry version 134 (12 Aug 2020)
Sequence version 1 (01 Oct 1994)
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Protein

DNA integrity scanning protein DisA

Gene

disA

Organism
Bacillus subtilis (strain 168)
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

Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged (PubMed:9141693, PubMed:16713562). Forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. Its ability to scan through the chromosome rapidly is due to its non-specific DNA-binding. When a lesion is present, DisA pauses at the lesion site (PubMed:21566650). This triggers a cellular response that culminates in a temporary block in sporulation initiation. It is required, at least partially, to inhibit the activity of the transcription factor spo0A, which controls, among others, early sporulation genes. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis (PubMed:22211522); it is toxic when present in excess (PubMed:26240071).5 Publications
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria (PubMed:23192352). Has diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (PubMed:18439896, PubMed:25616256). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis. Does not convert GTP to c-di-GMP (PubMed:18439896).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Diadenylate cyclase activity is inhibited by the interaction with RadA (By similarity). Diadenylate cyclase activity is not affected by ssDNA or dsDNA, but three- and four-way junctions strongly inhibit the activity of DisA, suggesting the enzyme is regulated by branched nucleic acids.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei78ATP; via amide nitrogenUniRule annotation1
Binding sitei96ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi109 – 113ATPUniRule annotation5

<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

GO - Biological processi

<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 functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU00880-MONOMER
MetaCyc:BSU00880-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.85, 658

<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:
DNA integrity scanning protein DisAUniRule annotation
Alternative name(s):
Cyclic di-AMP synthaseUniRule annotation
Short name:
c-di-AMP synthaseUniRule annotation
Diadenylate cyclaseUniRule annotation (EC:2.7.7.85UniRule annotation1 Publication)
Short name:
DAC
<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:disAUniRule annotation
Synonyms:comY1 Publication, orf61 Publication, yacK
Ordered Locus Names:BSU00880
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<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

Keywords - Cellular componenti

Cytoplasm

<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 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

Decreases c-di-AMP levels in mid-exponential phase from about 3.8 µM to about 2.8 µM in strain BG214 (PubMed:25616256). No change in sensitivity to methyl methanesulfonate (MMS), decreased survival after UV irradiation in transition and stationary phase, strong decrease in competence (PubMed:9141693). Cells lacking this gene show a reduced c-di-AMP level compared to wild-type and cannot properly trigger the DNA damage response (PubMed:21566650). No effect on antibiotic sensitivity to the beta-lactam antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP phosphodiesterase GdpP increased sensitivity to CEF (PubMed:22211522). Double disA-cdaA mutants cannot be made, suggesting they are lethal, while double disA-cdaS and cdaA-cdaS mutants are viable (PubMed:22211522, PubMed:23192352). Depletion of cdaA in double disA-cdaA deletion cells leads to cell lysis (PubMed:22211522). Exponentially growing cells are 100-fold more sensitive to MMS, no change in response to H2O2 or nalidixic acid; a double disA-radA deletion suppresses H2O2 sensitivity of the radA mutant, but has no effect on MMS sensitivity, suggesting radA and disA might work in the same DNA repair pathway (PubMed:25616256).4 Publications

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>Mutagenesisi77D → N: Loss of enzymatic activity. Fails to form the normal DisA focus. Cannot trigger the DNA damage response. Increased sensitivity to methyl methanesulfonate. 3 Publications1
Mutagenesisi334G → E: Reduction in the capability of the four-way junction DNA to inhibit diadenylate cyclase. Reduction in DNA-binding. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000494501 – 360DNA integrity scanning protein DisAAdd BLAST360

Proteomic databases

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

More...
PaxDbi
P37573

PRoteomics IDEntifications database

More...
PRIDEi
P37573

<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 increases during late exponential phase and at the onset of sporulation (PubMed:16713562). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).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

Homooligomer (PubMed:18439896).

Interacts with RadA (PubMed:23760274).

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU00880

<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

3D structure databases

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

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SMRi
P37573

Database of comparative protein structure models

More...
ModBasei
Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini11 – 149DACPROSITE-ProRule annotationAdd BLAST139

<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 DisA family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
COG1623, Bacteria

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P37573

KEGG Orthology (KO)

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KOi
K07067

Identification of Orthologs from Complete Genome Data

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OMAi
MRLIALY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P37573

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1260.110, 1 hit
3.40.1700.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01438, DisA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038331, DisA_sf
IPR036888, DNA_integrity_DisA_N_sf
IPR018906, DNA_integrity_scan_DisA_link
IPR003390, DNA_integrity_scan_DisA_N
IPR023763, DNA_integrity_scanning_protein
IPR010994, RuvA_2-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10635, DisA-linker, 1 hit
PF02457, DisA_N, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF143597, SSF143597, 1 hit
SSF47781, SSF47781, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51794, DAC, 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.

P37573-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEKEKKGAKH ELDLSSILQF VAPGTPLRAG MENVLRANTG GLIVVGYNDK
60 70 80 90 100
VKEVVDGGFH INTAFSPAHL YELAKMDGAI ILSDSGQKIL YANTQLMPDA
110 120 130 140 150
TISSSETGMR HRTAERVAKQ TGCLVIAISE RRNVITLYQE NMKYTLKDIG
160 170 180 190 200
FILTKANQAI QTLEKYKTIL DKTINALNAL EFEELVTFSD VLSVMHRYEM
210 220 230 240 250
VLRIKNEINM YIKELGTEGH LIKLQVIELI TDMEEEAALF IKDYVKEKIK
260 270 280 290 300
DPFVLLKELQ DMSSYDLLDD SIVYKLLGYP ASTNLDDYVL PRGYRLLNKI
310 320 330 340 350
PRLPMPIVEN VVEAFGVLPR IIEASAEELD EVEGIGEVRA QKIKKGLKRL
360
QEKHYLDRQL
Length:360
Mass (Da):40,734
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:i92994B4A916026A9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D26185 Genomic DNA Translation: BAA05322.1
AL009126 Genomic DNA Translation: CAB11864.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S66117

NCBI Reference Sequences

More...
RefSeqi
NP_387969.1, NC_000964.3
WP_003225736.1, NZ_JNCM01000029.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB11864; CAB11864; BSU00880

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
51994641
936868

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU00880

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.89

<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
D26185 Genomic DNA Translation: BAA05322.1
AL009126 Genomic DNA Translation: CAB11864.1
PIRiS66117
RefSeqiNP_387969.1, NC_000964.3
WP_003225736.1, NZ_JNCM01000029.1

3D structure databases

SMRiP37573
ModBaseiSearch...

Protein-protein interaction databases

STRINGi224308.BSU00880

Proteomic databases

PaxDbiP37573
PRIDEiP37573

Genome annotation databases

EnsemblBacteriaiCAB11864; CAB11864; BSU00880
GeneIDi51994641
936868
KEGGibsu:BSU00880
PATRICifig|224308.179.peg.89

Phylogenomic databases

eggNOGiCOG1623, Bacteria
InParanoidiP37573
KOiK07067
OMAiMRLIALY
PhylomeDBiP37573

Enzyme and pathway databases

BioCyciBSUB:BSU00880-MONOMER
MetaCyc:BSU00880-MONOMER
BRENDAi2.7.7.85, 658

Family and domain databases

Gene3Di1.20.1260.110, 1 hit
3.40.1700.10, 1 hit
HAMAPiMF_01438, DisA, 1 hit
InterProiView protein in InterPro
IPR038331, DisA_sf
IPR036888, DNA_integrity_DisA_N_sf
IPR018906, DNA_integrity_scan_DisA_link
IPR003390, DNA_integrity_scan_DisA_N
IPR023763, DNA_integrity_scanning_protein
IPR010994, RuvA_2-like
PfamiView protein in Pfam
PF10635, DisA-linker, 1 hit
PF02457, DisA_N, 1 hit
SUPFAMiSSF143597, SSF143597, 1 hit
SSF47781, SSF47781, 1 hit
PROSITEiView protein in PROSITE
PS51794, DAC, 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 nameiDISA_BACSU
<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: P37573
<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: August 12, 2020
This is version 134 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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