HAMAP rule MF_03120
General rule information
[?]
| Accession | MF_03120 |
| Dates | 18-JUN-2010 (Created) 19-NOV-2022 (Last updated, Version 16) |
| Name | lonm_euk |
| Scope | Eukaryota |
| Templates | P36776 (LONM_HUMAN); Q59HJ6 (LONM_BOVIN); P36775 (LONM_YEAST): [Recover all] |
| Triggered by |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier |
|
case <OC:Mammalia>
| Protein name |
|
||||||||||||||||||||||||||||
else case <OC:Saccharomyces>
| Protein name |
|
||||||||||||
else
| Protein name |
|
||||||||
end case
case <OC:Vertebrata>
| Gene name |
|
else case <OC:Fungi>
| Gene name |
|
end case
Comments
[?]
case <OC:Mammalia>
| Function | ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. |
else
| Function | ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner. |
end case
| Catalytic activity | Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; |
case <OC:Mammalia>
| Subunit | Homohexamer. Organized in a ring with a central cavity. The ATP-binding and proteolytic domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with @gn(TWNK) and mitochondrial DNA polymerase subunit @gn(POLG). |
else case <OC:Saccharomyces>
| Subunit | Homoheptamer. Organized in a ring with a central cavity. Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits. |
else
| Subunit | Homohexamer or homoheptamer. Organized in a ring with a central cavity. |
end case
| Subcellular location | Mitochondrion matrix. |
case not <OC:Mammalia> and not <OC:Saccharomyces> and not <AnyFeature:TransitM>
| Miscellaneous | This protein may be expected to contain an N-terminal transit peptide but none has been predicted. |
end case
| Similarity | Belongs to the peptidase S16 family. |
Keywords
[?]
case <FTTag:ATP>
end case
case <OC:Mammalia> or <OC:Saccharomyces>
end case
Gene Ontology
[?]
GO:0005759; Cellular component: mitochondrial matrix.
GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATP hydrolysis activity.
GO:0004176; Molecular function: ATP-dependent peptidase activity.
GO:0004252; Molecular function: serine-type endopeptidase activity.
GO:0043565; Molecular function: sequence-specific DNA binding.
GO:0034599; Biological process: cellular response to oxidative stress.
GO:0070407; Biological process: oxidation-dependent protein catabolic process.
GO:0006515; Biological process: protein quality control for misfolded or incompletely synthesized proteins.
GO:0051131; Biological process: chaperone-mediated protein complex assembly.
GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATP hydrolysis activity.
GO:0004176; Molecular function: ATP-dependent peptidase activity.
GO:0004252; Molecular function: serine-type endopeptidase activity.
GO:0043565; Molecular function: sequence-specific DNA binding.
GO:0034599; Biological process: cellular response to oxidative stress.
GO:0070407; Biological process: oxidation-dependent protein catabolic process.
GO:0006515; Biological process: protein quality control for misfolded or incompletely synthesized proteins.
GO:0051131; Biological process: chaperone-mediated protein complex assembly.
Cross-references
[?]
| PROSITE | PS51787; LON_N; 1; trigger=PRU01123; |
| PS51786; LON_PROTEOLYTIC; 1; trigger=PRU01122; | |
| PS01046; LON_SER; 1; | |
| Pfam | PF00004; AAA; 1; |
| PF02190; LON; 1; | |
| PF03357; Snf7; 1; | |
| PRINTS | PR00830; ENDOLAPTASE; 1; |
| TIGRFAMs | TIGR00763; lon; 1; |
Computed features
[?]
case not <OC:Mammalia> and not <OC:Saccharomyces>
| General | TransitM; -; 0-1; trigger=yes; |
end case
Features
[?]
case <OC:Mammalia>
| From: LONM_BOVIN (Q59HJ6) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| TRANSIT | Nter | 67 | Mitochondrion | |||||||||
| CHAIN | 68 | Cter | Lon protease homolog, mitochondrial | |||||||||
end case
case <OC:Saccharomyces>
| From: LONM_YEAST (P36775) | ||||||||||||
| TRANSIT | Nter | 37 | Mitochondrion | |||||||||
| PROPEP | 38 | 98 | Removed in mature form; by autocatalysis | |||||||||
| CHAIN | 99 | Cter | Lon protease homolog, mitochondrial | |||||||||
end case
| From: LONM_HUMAN (P36776) | ||||||||||||
| BINDING | 523 | 530 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | ATP | G-P-[PT]-G-[TV]-G-K-T | |||||||
| ACT_SITE | 855 | 855 | S | |||||||||
| ACT_SITE | 898 | 898 | K | |||||||||
Additional information
[?]