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Entry version 183 (07 Oct 2020)
Sequence version 2 (01 Feb 1994)
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Protein

Exodeoxyribonuclease I

Gene

sbcB

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

Degrades single-stranded DNA (ssDNA) in a highly processive manner (PubMed:23609540). Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase (PubMed:1329027).2 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+4 PublicationsNote: Binds 2 Mg2+ ions per monomer.1 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

Inhibited by 10 mM EDTA.1 Publication

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 bindingi15Magnesium 15 Publications1
Metal bindingi17Magnesium 21 Publication1
<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 sitei17Substrate1 Publication1
<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>Sitei148Important for interaction with ssb1 Publication1
Binding sitei165Substrate1 Publication1
Sitei181Important for activity1 Publication1
Metal bindingi186Magnesium 21 Publication1
Sitei207Important for interaction with ssb1 Publication1
Sitei311Important for interaction with ssb1 Publication1
Sitei338Important for interaction with ssb1 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

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, Exonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10926-MONOMER
MetaCyc:EG10926-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.11.1, 2026

<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:
Exodeoxyribonuclease I (EC:3.1.11.13 Publications)
Short name:
ExoI1 Publication
Short name:
Exonuclease I1 Publication
Alternative name(s):
DNA deoxyribophosphodiesterase
Short name:
dRPase
<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:sbcB
Synonyms:cpeA, xonA
Ordered Locus Names:b2011, JW1993
<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 disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%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>Mutagenesisi148R → A: Strongly reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi150E → A: About 2-fold increased ssb-binding. Weakly increased ssb-independent and ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi181H → A: Residual nuclease activity. 1 Publication1
Mutagenesisi207Y → A: Strongly reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi227K → A: 7-fold reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi311Q → A: 2-fold reduced ssb-binding. Weakly reduced ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi316R → A: Strongly reduced ssb-binding. Strongly reduced ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi318E → A: About 2-fold increased ssb-binding. No effect on ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi319D → A: 2-fold reduced ssb-binding. No effect on ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi327R → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi331L → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi338R → A: 3-fold reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi448Q → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication1
Mutagenesisi452Q → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 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_00000871101 – 475Exodeoxyribonuclease IAdd BLAST475

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P04995

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

More...
PaxDbi
P04995

PRoteomics IDEntifications database

More...
PRIDEi
P04995

<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

Monomer (PubMed:23609540).

Interacts with ssb (via C-terminus); this interaction stimulates the exonuclease activity by recruiting the enzyme to its substrate (PubMed:18591666, PubMed:20018747).

3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei18Interaction with single-stranded DNA1 Publication1
Sitei66Interaction with single-stranded DNA1 Publication1
Sitei113Interaction with single-stranded DNA1 Publication1
Sitei124Interaction with single-stranded DNA1 Publication1
Sitei128Interaction with single-stranded DNA1 Publication1
Sitei142Interaction with single-stranded DNA1 Publication1
Sitei164Interaction with single-stranded DNACombined sources1 Publication1
Sitei214Interaction with single-stranded DNA1 Publication1
Sitei257Interaction with single-stranded DNACombined sources1 Publication1
Sitei284Interaction with single-stranded DNA1 Publication1
Sitei304Interaction with single-stranded DNACombined sources1 Publication1
Sitei368Interaction with single-stranded DNA1 Publication1
Sitei371Interaction with single-stranded DNA1 Publication1

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260414, 102 interactors

Database of interacting proteins

More...
DIPi
DIP-10827N

Protein interaction database and analysis system

More...
IntActi
P04995, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2011

<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

1475
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
P04995

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
P04995

<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>Domaini13 – 192ExonucleaseSequence analysisAdd BLAST180
Domaini202 – 355ExoI SH3-likePROSITE-ProRule annotationAdd BLAST154
Domaini358 – 475ExoI C-terminalPROSITE-ProRule annotationAdd BLAST118

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal exonuclease domain and the exonuclease C-terminal domain form a central positively charged groove which binds the DNA.2 Publications2 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2925, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_043508_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04995

KEGG Orthology (KO)

More...
KOi
K01141

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P04995

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.30.450, 1 hit
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023607, Exodeoxyribonuclease_I
IPR034748, EXOI_C
IPR034747, EXOI_SH3
IPR038649, EXOI_SH3_sf
IPR013620, Exonuc_1_C
IPR013520, Exonuclease_RNaseT/DNA_pol3
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08411, Exonuc_X-T_C, 1 hit
PF00929, RNase_T, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000977, Exodeoxyribonuclease_I, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00479, EXOIII, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098, SSF53098, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51785, EXOI_C, 1 hit
PS51784, EXOI_SH3, 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.

P04995-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMNDGKQQST FLFHDYETFG THPALDRPAQ FAAIRTDSEF NVIGEPEVFY
60 70 80 90 100
CKPADDYLPQ PGAVLITGIT PQEARAKGEN EAAFAARIHS LFTVPKTCIL
110 120 130 140 150
GYNNVRFDDE VTRNIFYRNF YDPYAWSWQH DNSRWDLLDV MRACYALRPE
160 170 180 190 200
GINWPENDDG LPSFRLEHLT KANGIEHSNA HDAMADVYAT IAMAKLVKTR
210 220 230 240 250
QPRLFDYLFT HRNKHKLMAL IDVPQMKPLV HVSGMFGAWR GNTSWVAPLA
260 270 280 290 300
WHPENRNAVI MVDLAGDISP LLELDSDTLR ERLYTAKTDL GDNAAVPVKL
310 320 330 340 350
VHINKCPVLA QANTLRPEDA DRLGINRQHC LDNLKILREN PQVREKVVAI
360 370 380 390 400
FAEAEPFTPS DNVDAQLYNG FFSDADRAAM KIVLETEPRN LPALDITFVD
410 420 430 440 450
KRIEKLLFNY RARNFPGTLD YAEQQRWLEH RRQVFTPEFL QGYADELQML
460 470
VQQYADDKEK VALLKALWQY AEEIV
Length:475
Mass (Da):54,501
Last modified:February 1, 1994 - 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:iA6A02AC17922C313
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 conflicti210 – 218Missing in AAA19938 (PubMed:3539937).Curated9
Sequence conflicti225Q → H in AAA19938 (PubMed:3539937).Curated1
Sequence conflicti343V → E in AAA19938 (PubMed:3539937).Curated1
Sequence conflicti475V → A in AAA19938 (PubMed:3539937).Curated1

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
J02641 Unassigned DNA Translation: AAA19938.1
U00009 Genomic DNA Translation: AAA16417.1
U00096 Genomic DNA Translation: AAC75072.1
AP009048 Genomic DNA Translation: BAA15839.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B64966, NCECX1

NCBI Reference Sequences

More...
RefSeqi
NP_416515.1, NC_000913.3
WP_000980589.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75072; AAC75072; b2011
BAA15839; BAA15839; BAA15839

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946529

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1993
eco:b2011

<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
J02641 Unassigned DNA Translation: AAA19938.1
U00009 Genomic DNA Translation: AAA16417.1
U00096 Genomic DNA Translation: AAC75072.1
AP009048 Genomic DNA Translation: BAA15839.1
PIRiB64966, NCECX1
RefSeqiNP_416515.1, NC_000913.3
WP_000980589.1, 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
1FXXX-ray2.40A1-475[»]
2QXFX-ray1.50A1-475[»]
3C94X-ray2.70A1-475[»]
3C95X-ray1.70A1-475[»]
3HL8X-ray1.55A1-475[»]
3HP9X-ray1.60A1-475[»]
4HCBX-ray2.00A/B1-475[»]
4HCCX-ray2.96A/B1-475[»]
4JRPX-ray1.95A/B1-475[»]
4JRQX-ray3.00A/B1-475[»]
4JS4X-ray3.10A/B1-475[»]
4JS5X-ray3.50A/B1-475[»]
SMRiP04995
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260414, 102 interactors
DIPiDIP-10827N
IntActiP04995, 7 interactors
STRINGi511145.b2011

Proteomic databases

jPOSTiP04995
PaxDbiP04995
PRIDEiP04995

Genome annotation databases

EnsemblBacteriaiAAC75072; AAC75072; b2011
BAA15839; BAA15839; BAA15839
GeneIDi946529
KEGGiecj:JW1993
eco:b2011

Organism-specific databases

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

More...
EchoBASEi
EB0919

Phylogenomic databases

eggNOGiCOG2925, Bacteria
HOGENOMiCLU_043508_1_1_6
InParanoidiP04995
KOiK01141
PhylomeDBiP04995

Enzyme and pathway databases

BioCyciEcoCyc:EG10926-MONOMER
MetaCyc:EG10926-MONOMER
BRENDAi3.1.11.1, 2026

Miscellaneous databases

EvolutionaryTraceiP04995

Protein Ontology

More...
PROi
PR:P04995

Family and domain databases

Gene3Di2.30.30.450, 1 hit
3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR023607, Exodeoxyribonuclease_I
IPR034748, EXOI_C
IPR034747, EXOI_SH3
IPR038649, EXOI_SH3_sf
IPR013620, Exonuc_1_C
IPR013520, Exonuclease_RNaseT/DNA_pol3
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
PfamiView protein in Pfam
PF08411, Exonuc_X-T_C, 1 hit
PF00929, RNase_T, 1 hit
PIRSFiPIRSF000977, Exodeoxyribonuclease_I, 1 hit
SMARTiView protein in SMART
SM00479, EXOIII, 1 hit
SUPFAMiSSF53098, SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS51785, EXOI_C, 1 hit
PS51784, EXOI_SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiEX1_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: P04995
<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: August 13, 1987
Last sequence update: February 1, 1994
Last modified: October 7, 2020
This is version 183 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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