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Entry version 131 (12 Aug 2020)
Sequence version 2 (23 Jan 2007)
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Protein

ATP-dependent RNA helicase DeaD

Gene

deaD

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

DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.UniRule annotation6 Publications

Miscellaneous

When overexpressed suppresses cold-sensitive mutants of rpsB (ribosomal protein S2) (PubMed:2045359) and pyrH/smbA2 (uridylate kinase) (PubMed:8190075).2 Publications

Caution

It is unclear whether it requires ATP: according to PubMed:8552679 and PubMed:10216955, it does not require ATP, while according to PubMed:15196029, PubMed:15554978 and PubMed:17259309, it requires ATP.Curated

<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

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 bindingi50 – 57ATPUniRule annotation8

<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 functionHelicase, Hydrolase, RNA-binding
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10215-MONOMER
ECOL316407:JW5531-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%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:
ATP-dependent RNA helicase DeaDUniRule annotation (EC:3.6.4.13UniRule annotation)
Alternative name(s):
Cold-shock DEAD box protein AUniRule annotation
Translation factor W2
<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:deaDUniRule annotation
Synonyms:csdA, mssB, rhlD
Ordered Locus Names:b3162, JW5531
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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

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

Cells lacking this gene grow very poorly at 15-20 degrees Celsius, and accumulate an abnormal large ribosomal subunit and precursor-23S rRNA (PubMed:15148362, PubMed:8552679, PubMed:25777676). A double bipA-deaD deletion has a more severe growth and ribosome phenotype than either single deletion, but the same level of pre-23S rRNA as the single deaD deletion (PubMed:25777676).3 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>Mutagenesisi157E → Q: Abolishes ATPase activity, drastically reduces helicase activity. In vivo acts as a dominant negative mutation in the presence of the wild-type protein at low temperature. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00000551012 – 629ATP-dependent RNA helicase DeaDAdd BLAST628

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9P6

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

More...
PaxDbi
P0A9P6

PRoteomics IDEntifications database

More...
PRIDEi
P0A9P6

2D gel databases

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

More...
SWISS-2DPAGEi
P0A9P6

<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

In response to low temperature (PubMed:8552679). Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389).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

Interacts with the 50S ribosomal subunit upon shifting to 15 degrees Celsius. Also found associated with the RNA degradosome at 15 degrees Celsius; binds RNase E (rne).

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262429, 170 interactors
851987, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-35752N

Protein interaction database and analysis system

More...
IntActi
P0A9P6, 86 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3162

<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

1629
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
P0A9P6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini37 – 208Helicase ATP-bindingUniRule annotationAdd BLAST172
Domaini232 – 379Helicase C-terminalUniRule annotationAdd BLAST148

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi6 – 34Q motifAdd BLAST29
Motifi156 – 159DEAD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi568 – 629Arg/Glu/Gly-richAdd BLAST62

<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 DEAD box helicase family. DeaD subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0513, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003041_21_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9P6

KEGG Orthology (KO)

More...
KOi
K05592

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9P6

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12499, RRM_EcCsdA_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.330, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00964, DEAD_helicase_DeaD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR021046, Cold-shock_DEAD_Abox_C
IPR034415, CsdA_RRM
IPR005580, DbpA/CsdA_RNA-bd_dom
IPR011545, DEAD/DEAH_box_helicase_dom
IPR028618, DEAD_helicase_DeaD
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR012677, Nucleotide-bd_a/b_plait_sf
IPR027417, P-loop_NTPase
IPR000629, RNA-helicase_DEAD-box_CS
IPR014014, RNA_helicase_DEAD_Q_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03880, DbpA, 1 hit
PF00270, DEAD, 1 hit
PF12343, DEADboxA, 1 hit
PF00271, Helicase_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00039, DEAD_ATP_HELICASE, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51195, Q_MOTIF, 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.

P0A9P6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEFETTFAD LGLKAPILEA LNDLGYEKPS PIQAECIPHL LNGRDVLGMA
60 70 80 90 100
QTGSGKTAAF SLPLLQNLDP ELKAPQILVL APTRELAVQV AEAMTDFSKH
110 120 130 140 150
MRGVNVVALY GGQRYDVQLR ALRQGPQIVV GTPGRLLDHL KRGTLDLSKL
160 170 180 190 200
SGLVLDEADE MLRMGFIEDV ETIMAQIPEG HQTALFSATM PEAIRRITRR
210 220 230 240 250
FMKEPQEVRI QSSVTTRPDI SQSYWTVWGM RKNEALVRFL EAEDFDAAII
260 270 280 290 300
FVRTKNATLE VAEALERNGY NSAALNGDMN QALREQTLER LKDGRLDILI
310 320 330 340 350
ATDVAARGLD VERISLVVNY DIPMDSESYV HRIGRTGRAG RAGRALLFVE
360 370 380 390 400
NRERRLLRNI ERTMKLTIPE VELPNAELLG KRRLEKFAAK VQQQLESSDL
410 420 430 440 450
DQYRALLSKI QPTAEGEELD LETLAAALLK MAQGERTLIV PPDAPMRPKR
460 470 480 490 500
EFRDRDDRGP RDRNDRGPRG DREDRPRRER RDVGDMQLYR IEVGRDDGVE
510 520 530 540 550
VRHIVGAIAN EGDISSRYIG NIKLFASHST IELPKGMPGE VLQHFTRTRI
560 570 580 590 600
LNKPMNMQLL GDAQPHTGGE RRGGGRGFGG ERREGGRNFS GERREGGRGD
610 620
GRRFSGERRE GRAPRRDDST GRRRFGGDA
Length:629
Mass (Da):70,546
Last modified:January 23, 2007 - 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:i9DB692D41C38D17C
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 AAA23674 differs from that shown. Reason: Frameshift.Curated
The sequence AAA23674 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAA57965 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti444A → G in AAA23674 (PubMed:2045359).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
M63288 Genomic DNA Translation: AAA23674.1 Sequence problems.
U18997 Genomic DNA Translation: AAA57965.1 Different initiation.
U00096 Genomic DNA Translation: AAC76196.2
AP009048 Genomic DNA Translation: BAE77208.1
U03750 Genomic DNA Translation: AAA03626.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F65106

NCBI Reference Sequences

More...
RefSeqi
NP_417631.2, NC_000913.3
WP_001295553.1, NZ_STEB01000012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76196; AAC76196; b3162
BAE77208; BAE77208; BAE77208

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
49582877
947674

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5531
eco:b3162

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3568

<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
M63288 Genomic DNA Translation: AAA23674.1 Sequence problems.
U18997 Genomic DNA Translation: AAA57965.1 Different initiation.
U00096 Genomic DNA Translation: AAC76196.2
AP009048 Genomic DNA Translation: BAE77208.1
U03750 Genomic DNA Translation: AAA03626.1
PIRiF65106
RefSeqiNP_417631.2, NC_000913.3
WP_001295553.1, NZ_STEB01000012.1

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
5B88NMR-A482-564[»]
5GI4X-ray2.24A/B218-445[»]
5GJUX-ray1.60A6-210[»]
SMRiP0A9P6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262429, 170 interactors
851987, 1 interactor
DIPiDIP-35752N
IntActiP0A9P6, 86 interactors
STRINGi511145.b3162

2D gel databases

SWISS-2DPAGEiP0A9P6

Proteomic databases

jPOSTiP0A9P6
PaxDbiP0A9P6
PRIDEiP0A9P6

Genome annotation databases

EnsemblBacteriaiAAC76196; AAC76196; b3162
BAE77208; BAE77208; BAE77208
GeneIDi49582877
947674
KEGGiecj:JW5531
eco:b3162
PATRICifig|1411691.4.peg.3568

Organism-specific databases

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

More...
EchoBASEi
EB0211

Phylogenomic databases

eggNOGiCOG0513, Bacteria
HOGENOMiCLU_003041_21_1_6
InParanoidiP0A9P6
KOiK05592
PhylomeDBiP0A9P6

Enzyme and pathway databases

BioCyciEcoCyc:EG10215-MONOMER
ECOL316407:JW5531-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A9P6

Family and domain databases

CDDicd12499, RRM_EcCsdA_like, 1 hit
Gene3Di3.30.70.330, 1 hit
HAMAPiMF_00964, DEAD_helicase_DeaD, 1 hit
InterProiView protein in InterPro
IPR021046, Cold-shock_DEAD_Abox_C
IPR034415, CsdA_RRM
IPR005580, DbpA/CsdA_RNA-bd_dom
IPR011545, DEAD/DEAH_box_helicase_dom
IPR028618, DEAD_helicase_DeaD
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR012677, Nucleotide-bd_a/b_plait_sf
IPR027417, P-loop_NTPase
IPR000629, RNA-helicase_DEAD-box_CS
IPR014014, RNA_helicase_DEAD_Q_motif
PfamiView protein in Pfam
PF03880, DbpA, 1 hit
PF00270, DEAD, 1 hit
PF12343, DEADboxA, 1 hit
PF00271, Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00039, DEAD_ATP_HELICASE, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51195, Q_MOTIF, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<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 nameiDEAD_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: P0A9P6
Secondary accession number(s): P23304, Q2M948, Q8FD90
<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: July 19, 2005
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 131 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, 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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