mitochondrial inner membrane protease subunit 2 isoform X2 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| TraF super family | cl44169 | Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ... |
76-117 | 8.35e-07 | ||
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport]; The actual alignment was detected with superfamily member COG4959: Pssm-ID: 443985 [Multi-domain] Cd Length: 114 Bit Score: 44.90 E-value: 8.35e-07
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| Name | Accession | Description | Interval | E-value | ||
| TraF | COG4959 | Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ... |
76-117 | 8.35e-07 | ||
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443985 [Multi-domain] Cd Length: 114 Bit Score: 44.90 E-value: 8.35e-07
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| sigpep_I_bact | TIGR02227 | signal peptidase I, bacterial type; This model represents signal peptidase I from most ... |
73-117 | 6.37e-06 | ||
signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274044 [Multi-domain] Cd Length: 142 Bit Score: 42.99 E-value: 6.37e-06
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| Peptidase_S26 | pfam10502 | Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ... |
78-116 | 1.82e-05 | ||
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base. Pssm-ID: 431321 [Multi-domain] Cd Length: 162 Bit Score: 41.81 E-value: 1.82e-05
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| S26_SPase_I | cd06530 | The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ... |
84-111 | 1.65e-04 | ||
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism. Pssm-ID: 119398 [Multi-domain] Cd Length: 85 Bit Score: 37.95 E-value: 1.65e-04
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| Name | Accession | Description | Interval | E-value | ||
| TraF | COG4959 | Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ... |
76-117 | 8.35e-07 | ||
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443985 [Multi-domain] Cd Length: 114 Bit Score: 44.90 E-value: 8.35e-07
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| sigpep_I_bact | TIGR02227 | signal peptidase I, bacterial type; This model represents signal peptidase I from most ... |
73-117 | 6.37e-06 | ||
signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274044 [Multi-domain] Cd Length: 142 Bit Score: 42.99 E-value: 6.37e-06
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| Peptidase_S26 | pfam10502 | Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ... |
78-116 | 1.82e-05 | ||
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base. Pssm-ID: 431321 [Multi-domain] Cd Length: 162 Bit Score: 41.81 E-value: 1.82e-05
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| S26_SPase_I | cd06530 | The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ... |
84-111 | 1.65e-04 | ||
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism. Pssm-ID: 119398 [Multi-domain] Cd Length: 85 Bit Score: 37.95 E-value: 1.65e-04
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| sod_Ni_protease | TIGR02754 | nickel-type superoxide dismutase maturation protease; Members of this protein family are ... |
74-107 | 2.24e-04 | ||
nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair] Pssm-ID: 274282 [Multi-domain] Cd Length: 90 Bit Score: 37.82 E-value: 2.24e-04
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