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39  structures 7394  species 0  interactions 16695  sequences 151  architectures

Family: LON_substr_bdg (PF02190)

Summary: ATP-dependent protease La (LON) substrate-binding domain

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This is the Wikipedia entry entitled "Lon protease family". More...

Lon protease family Edit Wikipedia article

ATP-dependent protease La (LON) domain
PDB 2ane EBI.jpg
crystal structure of n-terminal domain of e.coli lon protease
Symbol LON
Pfam PF02190
Pfam clan CL0178
InterPro IPR003111
SCOP 1zbo
Lon protease (S16) C-terminal proteolytic domain
Symbol LON
Pfam PF05362
Pfam clan CL0329
InterPro IPR008269
SCOP 1rr9

In molecular biology, the Lon protease family is a family of proteases. They are found in archaea, bacteria and eukaryotes. Lon proteases are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SJ). In the eukaryotes the majority of the Lon proteases are located in the mitochondrial matrix.[1][2] In yeast, the Lon protease PIM1 is located in the mitochondrial matrix. It is required for mitochondrial function, it is constitutively expressed but is increased after thermal stress, suggesting that PIM1 may play a role in the heat shock response.[3]

See also


  1. ^ Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR (December 1993). "A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 11247–51. doi:10.1073/pnas.90.23.11247. PMC 47959Freely accessible. PMID 8248235. 
  2. ^ Barakat S, Pearce DA, Sherman F, Rapp WD (May 1998). "Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant". Plant Mol. Biol. 37 (1): 141–54. doi:10.1023/A:1005912831051. PMID 9620272. 
  3. ^ Van Dyck L, Pearce DA, Sherman F (January 1994). "PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae". J. Biol. Chem. 269 (1): 238–42. PMID 8276800. 

External links

This article incorporates text from the public domain Pfam and InterPro IPR003111

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

ATP-dependent protease La (LON) substrate-binding domain Provide feedback

This domain has been shown to be part of the PUA superfamily [2]. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, PF05362. ATP-dependent Lon proteases are conserved in all living organisms and catalyse rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.

Literature references

  1. Li M, Rasulova F, Melnikov EE, Rotanova TV, Gustchina A, Maurizi MR, Wlodawer A;, Protein Sci. 2005;14:2895-2900.: Crystal structure of the N-terminal domain of E. coli Lon protease. PUBMED:16199667 EPMC:16199667

  2. Bertonati C, Punta M, Fischer M, Yachdav G, Forouhar F, Zhou W, Kuzin AP, Seetharaman J, Abashidze M, Ramelot TA, Kennedy MA, Cort JR, Belachew A, Hunt JF, Tong L, Montelione GT, Rost B;, Proteins. 2009;75:760-773.: Structural genomics reveals EVE as a new ASCH/PUA-related domain. PUBMED:19191354 EPMC:19191354

  3. Cha SS, An YJ, Lee CR, Lee HS, Kim YG, Kim SJ, Kwon KK, De Donatis GM, Lee JH, Maurizi MR, Kang SG;, EMBO J. 2010;29:3520-3530.: Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. PUBMED:20834233 EPMC:20834233

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003111

This signature defines the N-terminal substrate-binding domain of the archael, bacterial and eukaryotic lon proteases, which are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SF). In the eukaryotes the majority of the proteins are located in the mitochondrial matrix [ PUBMED:8248235 , PUBMED:9620272 ]. In yeast, Pim1, is located in the mitochondrial matrix, is required for mitochondrial function, is constitutively expressed but is increased after thermal stress, suggesting that Pim1 may play a role in the heat shock response [ PUBMED:8276800 ].

This structure of this domain has been determined [ PUBMED:16199667 , PUBMED:19191354 , PUBMED:20834233 ]. This domain also occurs in proteins which lack the peptidase domain, such as the SPBC14F5.10c gene product from Schizosaccharomyces pombe; these proteins are uncharacterized.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan PUA (CL0178), which has the following description:

This clan consists of the RNA binding PUA domain and ASCH domain. It also contains uncharacterised protein families.

The clan contains the following 18 members:

ASCH DUF2584 DUF365 DUF3850 EVE LON_substr_bdg Methyltranf_PUA PrgU PUA PUA_2 PUA_3 RE_AspBHI_N SAD_SRA SRA TruB-C_2 TruB_C UPF0113 YTH


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Curation and family details

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Seed source: Alignment kindly provided by SMART
Previous IDs: LON;
Type: Family
Sequence Ontology: SO:0100021
Author: SMART
Number in seed: 75
Number in full: 16695
Average length of the domain: 206.40 aa
Average identity of full alignment: 20 %
Average coverage of the sequence by the domain: 31.80 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.7 28.7
Trusted cut-off 28.7 28.7
Noise cut-off 28.6 28.6
Model length: 205
Family (HMM) version: 18
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Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 LON_substr_bdg domain has been found. There are 39 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 sequence.

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