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Conserved domains on  [gi|2161086936|ref|WP_231117415|]
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signal peptidase I [Piscirickettsia salmonis]

Protein Classification

S26 family signal peptidase( domain architecture ID 1000376)

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

CATH:  2.10.109.10
EC:  3.4.21.-
Gene Ontology:  GO:0006465|GO:0004252
PubMed:  7845208|12475201

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sigpep_I_bact super family cl37079
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 54-189 2.56e-17

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]


The actual alignment was detected with superfamily member TIGR02227:

Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 74.57  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGlvspvggrswwhWQEPKINDLV----AAFDNKWLVRRVIALPGDEITQL 129
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR------------TSDPKRGDIVvfkdPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2161086936 130 HHVLYVNGEAVDGVTLPVDQKRADQYF-----IPAEHVLLVantkaGVN-----------LVPRTAIIGRISPAFW 189
Cdd:TIGR02227  69 DGKLYINGKKIDEPYLKPNGYLDTSEFntpvkVPPGHYFVL-----GDNrdnsldsryfgFVPIDQIIGKVSFVFY 139
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 54-189 2.56e-17

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: 74.57  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGlvspvggrswwhWQEPKINDLV----AAFDNKWLVRRVIALPGDEITQL 129
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR------------TSDPKRGDIVvfkdPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2161086936 130 HHVLYVNGEAVDGVTLPVDQKRADQYF-----IPAEHVLLVantkaGVN-----------LVPRTAIIGRISPAFW 189
Cdd:TIGR02227  69 DGKLYINGKKIDEPYLKPNGYLDTSEFntpvkVPPGHYFVL-----GDNrdnsldsryfgFVPIDQIIGKVSFVFY 139
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 54-189 2.35e-13

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: 64.53  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGLvspvggrswwhwQEPKINDLVA----AFDNKWLVRRVIALPGDEITQL 129
Cdd:pfam10502  21 FLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGL------------GEPKRGDIVVfrppEGPGVPLIKRVIGLPGDRVEYK 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2161086936 130 HHVLYVNGEAVDGVTLPVDQKRADQYF--------IPAEHVLL----VANTKAG--VNLVPRTAIIGRISPAFW 189
Cdd:pfam10502  89 DDQLYINGKPVGEPYLADRKGRPTFDLppwqgcrvVPEGEYFVmgdnRDNSLDSryFGFVPASNIVGRAVFPVW 162
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
54-158 6.65e-11

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 58.33  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGLvspvggrswwhwQEPKINDLVaAFD-----NKWLVRRVIALPGDEITQ 128
Cdd:COG0681    31 FVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGF------------GEPKRGDIV-VFKypedpSKDYIKRVIGLPGDTVEI 97

                          90       100       110
                  ....*....|....*....|....*....|
gi 2161086936 129 LHHVLYVNGEAVDGVTLPVDQKRADQYFIP 158
Cdd:COG0681    98 RDGQVYVNGKPLNEPYLEEYYYPVSVDGDV 127
PRK10861 PRK10861
signal peptidase I;
54-127 1.21e-08

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 53.13  E-value: 1.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGLVSPVGGRSWWHWQEPKINDlVAAF---DNKWL--VRRVIALPGDEIT 127
Cdd:PRK10861   80 FIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGD-IVVFkypEDPKLdyIKRVVGLPGDKVT 157
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 57-121 3.53e-03

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: 35.25  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161086936  57 QPIYIQTNDMQPELSRGDFTLLERYAYglvspvggrswwHWQEPKINDLVAA----FDNKWLVRRVIAL 121
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSY------------GFREPKRGDVVVFkspgDPGKPIIKRVIGY 57
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 54-189 2.56e-17

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: 74.57  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGlvspvggrswwhWQEPKINDLV----AAFDNKWLVRRVIALPGDEITQL 129
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR------------TSDPKRGDIVvfkdPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2161086936 130 HHVLYVNGEAVDGVTLPVDQKRADQYF-----IPAEHVLLVantkaGVN-----------LVPRTAIIGRISPAFW 189
Cdd:TIGR02227  69 DGKLYINGKKIDEPYLKPNGYLDTSEFntpvkVPPGHYFVL-----GDNrdnsldsryfgFVPIDQIIGKVSFVFY 139
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 54-189 2.35e-13

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: 64.53  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGLvspvggrswwhwQEPKINDLVA----AFDNKWLVRRVIALPGDEITQL 129
Cdd:pfam10502  21 FLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGL------------GEPKRGDIVVfrppEGPGVPLIKRVIGLPGDRVEYK 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2161086936 130 HHVLYVNGEAVDGVTLPVDQKRADQYF--------IPAEHVLL----VANTKAG--VNLVPRTAIIGRISPAFW 189
Cdd:pfam10502  89 DDQLYINGKPVGEPYLADRKGRPTFDLppwqgcrvVPEGEYFVmgdnRDNSLDSryFGFVPASNIVGRAVFPVW 162
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
54-158 6.65e-11

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 58.33  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGLvspvggrswwhwQEPKINDLVaAFD-----NKWLVRRVIALPGDEITQ 128
Cdd:COG0681    31 FVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGF------------GEPKRGDIV-VFKypedpSKDYIKRVIGLPGDTVEI 97

                          90       100       110
                  ....*....|....*....|....*....|
gi 2161086936 129 LHHVLYVNGEAVDGVTLPVDQKRADQYFIP 158
Cdd:COG0681    98 RDGQVYVNGKPLNEPYLEEYYYPVSVDGDV 127
PRK10861 PRK10861
signal peptidase I;
54-127 1.21e-08

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 53.13  E-value: 1.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161086936  54 FVVQPIYIQTNDMQPELSRGDFTLLERYAYGLVSPVGGRSWWHWQEPKINDlVAAF---DNKWL--VRRVIALPGDEIT 127
Cdd:PRK10861   80 FIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGD-IVVFkypEDPKLdyIKRVVGLPGDKVT 157
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 110-189 2.06e-06

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: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161086936 110 DNKWLVRRVIALPGDEITQLHHVLYVNGEAV--------DGVTLPVDQKradQYFIPAEHVLLVANTKA--------Gvn 173
Cdd:COG4959    22 RGVPLIKRVAALPGDTVCIKGGQVYINGKPVaealerdrAGRPLPVWQG---CGVVPEGEYFLLGDNRPnsfdsryfG-- 96

                          90
                  ....*....|....*.
gi 2161086936 174 LVPRTAIIGRISPAFW 189
Cdd:COG4959    97 PVPRSQIIGRAVPLWT 112
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 57-121 3.53e-03

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: 35.25  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161086936  57 QPIYIQTNDMQPELSRGDFTLLERYAYglvspvggrswwHWQEPKINDLVAA----FDNKWLVRRVIAL 121
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSY------------GFREPKRGDVVVFkspgDPGKPIIKRVIGY 57
 
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.
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