NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039742210|ref|XP_017170750|]
View 

mitochondrial inner membrane protease subunit 2 isoform X1 [Mus musculus]

Protein Classification

S26 family signal peptidase( domain architecture ID 1011306)

S26 family signal peptidase is a membrane-bound serine protease which frees proteins tethered to inner or mitochondrial membranes by cleaving off signal peptides during polypeptide translocation

EC:  3.4.21.-
Gene Ontology:  GO:0004252|GO:0006465
MEROPS:  S26
PubMed:  10982814

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Peptidase_S26 super family cl37809
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 53-124 6.10e-12

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.


The actual alignment was detected with superfamily member pfam10502:

Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 59.53  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVR---------------------------TIGHKNRLVKVPRGHMWVEGDHHGHSFDSN 105
Cdd:pfam10502  64 RPPEGPGVPLIKRVIGLPGDRVEykddqlyingkpvgepyladrkgrptfDLPPWQGCRVVPEGEYFVMGDNRDNSLDSR 143

                          90
                  ....*....|....*....
gi 1039742210 106 SFGPVSLGLLHAHATHILW 124
Cdd:pfam10502 144 YFGFVPASNIVGRAVFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 53-124 6.10e-12

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: 59.53  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVR---------------------------TIGHKNRLVKVPRGHMWVEGDHHGHSFDSN 105
Cdd:pfam10502  64 RPPEGPGVPLIKRVIGLPGDRVEykddqlyingkpvgepyladrkgrptfDLPPWQGCRVVPEGEYFVMGDNRDNSLDSR 143

                          90
                  ....*....|....*....
gi 1039742210 106 SFGPVSLGLLHAHATHILW 124
Cdd:pfam10502 144 YFGFVPASNIVGRAVFPVW 162
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 53-125 3.59e-11

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: 56.46  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVRTIGHK----NRLV--------------------KVPRGHMWVEGDHHGHSFDSNSFG 108
Cdd:COG4959    17 RGYLPRGVPLIKRVAALPGDTVCIKGGQvyinGKPVaealerdragrplpvwqgcgVVPEGEYFLLGDNRPNSFDSRYFG 96

                          90
                  ....*....|....*..
gi 1039742210 109 PVSLGLLHAHATHILWP 125
Cdd:COG4959    97 PVPRSQIIGRAVPLWTP 113
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 53-125 6.02e-11

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: 56.47  E-value: 6.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVRTI-------GHK-----------------NRLVKVPRGHMWVEGDHHGHSFDSNSFG 108
Cdd:TIGR02227  44 KDPDTNKNIYVKRIIGLPGDKVEFRdgklyinGKKidepylkpngyldtsefNTPVKVPPGHYFVLGDNRDNSLDSRYFG 123

                          90
                  ....*....|....*..
gi 1039742210 109 PVSLGLLHAHATHILWP 125
Cdd:TIGR02227 124 FVPIDQIIGKVSFVFYP 140
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 53-119 1.12e-08

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: 49.12  E-value: 1.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039742210  53 RSPKNPEQKIIKRVIALegdivrtighknrlvkvprghmWVEGDHHGHSFDSNSFGPVSLGLLHAHA 119
Cdd:cd06530    41 KSPGDPGKPIIKRVIGY----------------------FVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 53-124 6.10e-12

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: 59.53  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVR---------------------------TIGHKNRLVKVPRGHMWVEGDHHGHSFDSN 105
Cdd:pfam10502  64 RPPEGPGVPLIKRVIGLPGDRVEykddqlyingkpvgepyladrkgrptfDLPPWQGCRVVPEGEYFVMGDNRDNSLDSR 143

                          90
                  ....*....|....*....
gi 1039742210 106 SFGPVSLGLLHAHATHILW 124
Cdd:pfam10502 144 YFGFVPASNIVGRAVFPVW 162
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 53-125 3.59e-11

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: 56.46  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVRTIGHK----NRLV--------------------KVPRGHMWVEGDHHGHSFDSNSFG 108
Cdd:COG4959    17 RGYLPRGVPLIKRVAALPGDTVCIKGGQvyinGKPVaealerdragrplpvwqgcgVVPEGEYFLLGDNRPNSFDSRYFG 96

                          90
                  ....*....|....*..
gi 1039742210 109 PVSLGLLHAHATHILWP 125
Cdd:COG4959    97 PVPRSQIIGRAVPLWTP 113
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 53-125 6.02e-11

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: 56.47  E-value: 6.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVRTI-------GHK-----------------NRLVKVPRGHMWVEGDHHGHSFDSNSFG 108
Cdd:TIGR02227  44 KDPDTNKNIYVKRIIGLPGDKVEFRdgklyinGKKidepylkpngyldtsefNTPVKVPPGHYFVLGDNRDNSLDSRYFG 123

                          90
                  ....*....|....*..
gi 1039742210 109 PVSLGLLHAHATHILWP 125
Cdd:TIGR02227 124 FVPIDQIIGKVSFVFYP 140
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 53-119 1.12e-08

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: 49.12  E-value: 1.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039742210  53 RSPKNPEQKIIKRVIALegdivrtighknrlvkvprghmWVEGDHHGHSFDSNSFGPVSLGLLHAHA 119
Cdd:cd06530    41 KSPGDPGKPIIKRVIGY----------------------FVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 53-115 6.19e-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: 36.66  E-value: 6.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039742210  53 RSPKNPEQKIIKRVIAlegdivrtighknrlvkVPRGHMWVEGDHHGHSFDSNSFGPVSLGLL 115
Cdd:TIGR02754  39 RHPLQPYGLIIKRLAA-----------------VDDNGLFLLGDNPKASTDSRQLGPVPRSLL 84
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
53-113 1.02e-03

Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 37.52  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742210  53 RSPKNPEQKIIKRVIALEGDIVR----------------------TIGHKNRLVKVPRGHMWVEGDHHGHSFDSNSFGPV 110
Cdd:COG0681    74 KYPEDPSKDYIKRVIGLPGDTVEirdgqvyvngkplnepyleeyyYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPD 153


                  ...
gi 1039742210 111 SLG 113
Cdd:COG0681   154 DGG 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH