Summary: Endonuclease I
Endonuclease I Provide feedback
Bacterial periplasmic or secreted endonuclease I ( EC:22.214.171.124) E. coli endonuclease I (EndoI) is a sequence independent endonuclease located in the periplasm. It is inhibited by different RNA species. It is thought to normally generate double strand breaks in DNA, except in the presence of high salt concentrations and RNA, when it generates single strand breaks in DNA. Its biological role is unknown . Other family members are known to be extracellular . This family also includes a non-specific, Mg2+ activated ribonuclease precursor (Q03091) .
Jekel M, Wackernagel W; , Gene 1995;154:55-59.: The periplasmic endonuclease I of Escherichia coli has amino-acid sequence homology to the extracellular DNases of Vibrio cholerae and Aeromonas hydrophila. PUBMED:7867949 EPMC:7867949
Focareta T, Manning PA; , Gene 1987;53:31-40.: Extracellular proteins of Vibrio cholerae: molecular cloning, nucleotide sequence and characterization of the deoxyribonuclease (DNase) together with its periplasmic localization in Escherichia coli K-12. PUBMED:3036665 EPMC:3036665
Nakamura A, Koide Y, Miyazaki H, Kitamura A, Masaki H, Beppu T, Uozumi T; , Eur J Biochem 1992;209:121-127.: Gene cloning and characterization of a novel extracellular ribonuclease of Bacillus subtilis. PUBMED:1396690 EPMC:1396690
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007346Bacterial periplasmic or secreted (EC) Escherichia coli endonuclease I (EndoI) is a sequence independent endonuclease located in the periplasm. It is inhibited by different RNA species. It is thought to normally generate double strand breaks in DNA, except in the presence of high salt concentrations and RNA, when it generates single strand breaks in DNA. Its biological role is unknown [PUBMED:7867949]. Other family members are known to be extracellular [PUBMED:3036665]. This family also includes a non-specific, Mg2+-activated ribonuclease precursor (SWISSPROT) [PUBMED:1396690].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||nuclease activity (GO:0004518)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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This superfamily defined originally by SCOP contains a diverse range of endonucleases. Later Grishin identified the MH1 domain as belonging to the superfamily .
The clan contains the following 22 members:AHH Colicin-DNase DUF1524 DUF968 Endonuclea_NS_2 Endonuclease_1 Endonuclease_7 Endonuclease_NS GH-E HNH HNH_2 HNH_3 HNH_4 HNH_5 HNHc_6 ICEA LHH MH1 NinG RecA_dep_nuc WHH zf-His_Me_endon
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Kerrison ND, Finn RD|
|Number in seed:||14|
|Number in full:||714|
|Average length of the domain:||203.50 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||48.55 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Endonuclease_1 domain has been found. There are 11 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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