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Conserved domains on  [gi|1946373|gb|AAB63091|]
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putative signal peptidase I [Arabidopsis thaliana]

Protein Classification

S26 family signal peptidase( domain architecture ID 12106434)

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|GO:0016020|GO:0006508|GO:0008236
MEROPS:  S26
PubMed:  22031009|16126156|10982814

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 67-227 9.75e-48

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: 155.44  E-value: 9.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373     67 AKAAFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFI 146
Cdd:pfam10502   5 VKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPE----------GPGVPLI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373    147 KRIVASEGDWVEVRDGKLFVNDIVQEEDFVLEPMSYEME--PMF-----VPKGYVFVLGDNRNKSFDSHNWGPLPIENIV 219
Cdd:pfam10502  75 KRVIGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFdlPPWqgcrvVPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 1946373    220 GRSVFRYW 227
Cdd:pfam10502 155 GRAVFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 67-227 9.75e-48

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: 155.44  E-value: 9.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373     67 AKAAFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFI 146
Cdd:pfam10502   5 VKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPE----------GPGVPLI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373    147 KRIVASEGDWVEVRDGKLFVNDIVQEEDFVLEPMSYEME--PMF-----VPKGYVFVLGDNRNKSFDSHNWGPLPIENIV 219
Cdd:pfam10502  75 KRVIGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFdlPPWqgcrvVPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 1946373    220 GRSVFRYW 227
Cdd:pfam10502 155 GRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 83-230 4.85e-42

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: 140.06  E-value: 4.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373     83 ALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFIKRIVASEGDWVEVRDG 162
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPD----------TNKNIYVKRIIGLPGDKVEFRDG 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946373    163 KLFVNDIVQEEDFVLEPMSYEMEPM----FVPKGYVFVLGDNRNKSFDSHNWGPLPIENIVGRSVFRYWPPS 230
Cdd:TIGR02227  71 KLYINGKKIDEPYLKPNGYLDTSEFntpvKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
65-239 6.00e-30

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 110.71  E-value: 6.00e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   65 EDAKAAFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDV 144
Cdd:COG0681  13 EWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPE----------DPSKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373  145 FIKRIVASEGDWVEVRDGKLFVNDIVQEEDFVLEP-----MSYEMEPMFVPKGYVFVLGDNRNKSFDSHNWGPLPIENIV 219
Cdd:COG0681  83 YIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYyypvsVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVD 162

                       170       180
                ....*....|....*....|
gi 1946373  220 GRSVFRYWPPSKVSDTIYHD 239
Cdd:COG0681 163 GVGVGGVVDVVVPDVDSRLV 182
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 86-221 1.61e-22

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: 88.03  E-value: 1.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   86 EPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFIKRIVAsegdwvevrdgklf 165
Cdd:cd06530   1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPG----------DPGKPIIKRVIG-------------- 56

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1946373  166 vndivqeedfvlepmsyemepmfvpkgyVFVLGDNRNKSFDSHNWGPLPIENIVGR 221
Cdd:cd06530  57 ----------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGK 84
PRK10861 PRK10861
signal peptidase I;
54-223 5.85e-13

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 67.39  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373    54 GWVNKLLSVcsedakaaFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFR------------KPEVSD 121
Cdd:PRK10861  59 GWLETGASV--------FPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKdpitqttlietgHPKRGD 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   122 IVIFKappilleYPEygYSSNDvFIKRIVASEGDWV-------EVR-----------DGKLFVN-DIVQEEDFVL----- 177
Cdd:PRK10861 131 IVVFK-------YPE--DPKLD-YIKRVVGLPGDKVtydpvskEVTiqpgcssgqacENALPVTySNVEPSDFVQtfsrr 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   178 ---------------EPMSYEM------EPM-------------------------------FVPKGYVFVLGDNRNKSF 205
Cdd:PRK10861 201 nggeatsgffqvplnETKENGIrlserkETLgdvthriltvpgaqdqvgmyyqqpgqplatwVVPPGQYFMMGDNRDNSA 280

                        250
                 ....*....|....*...
gi 1946373   206 DSHNWGPLPIENIVGRSV 223
Cdd:PRK10861 281 DSRYWGFVPEANLVGKAT 298
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 67-227 9.75e-48

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: 155.44  E-value: 9.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373     67 AKAAFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFI 146
Cdd:pfam10502   5 VKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPE----------GPGVPLI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373    147 KRIVASEGDWVEVRDGKLFVNDIVQEEDFVLEPMSYEME--PMF-----VPKGYVFVLGDNRNKSFDSHNWGPLPIENIV 219
Cdd:pfam10502  75 KRVIGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFdlPPWqgcrvVPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 1946373    220 GRSVFRYW 227
Cdd:pfam10502 155 GRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 83-230 4.85e-42

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: 140.06  E-value: 4.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373     83 ALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFIKRIVASEGDWVEVRDG 162
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPD----------TNKNIYVKRIIGLPGDKVEFRDG 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946373    163 KLFVNDIVQEEDFVLEPMSYEMEPM----FVPKGYVFVLGDNRNKSFDSHNWGPLPIENIVGRSVFRYWPPS 230
Cdd:TIGR02227  71 KLYINGKKIDEPYLKPNGYLDTSEFntpvKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
65-239 6.00e-30

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 110.71  E-value: 6.00e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   65 EDAKAAFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDV 144
Cdd:COG0681  13 EWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPE----------DPSKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373  145 FIKRIVASEGDWVEVRDGKLFVNDIVQEEDFVLEP-----MSYEMEPMFVPKGYVFVLGDNRNKSFDSHNWGPLPIENIV 219
Cdd:COG0681  83 YIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYyypvsVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVD 162

                       170       180
                ....*....|....*....|
gi 1946373  220 GRSVFRYWPPSKVSDTIYHD 239
Cdd:COG0681 163 GVGVGGVVDVVVPDVDSRLV 182
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 121-228 1.48e-27

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: 101.91  E-value: 1.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373  121 DIVIFKAPPILLEypEYGYSSNDV-FIKRIVASEGDWVEVRDGKLFVNDIVQEE----DFVLEPMSYEMEPMFVPKGYVF 195
Cdd:COG4959   3 DLVAFRPPEPLAA--ERGYLPRGVpLIKRVAALPGDTVCIKGGQVYINGKPVAEalerDRAGRPLPVWQGCGVVPEGEYF 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 1946373  196 VLGDNRNKSFDSHNWGPLPIENIVGRSVFRYWP 228
Cdd:COG4959  81 LLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 86-221 1.61e-22

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: 88.03  E-value: 1.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   86 EPKSIPSTSMYPTLDKGDRVMAEKVSYFFRKPEVSDIVIFKAPPilleypeygySSNDVFIKRIVAsegdwvevrdgklf 165
Cdd:cd06530   1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPG----------DPGKPIIKRVIG-------------- 56

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1946373  166 vndivqeedfvlepmsyemepmfvpkgyVFVLGDNRNKSFDSHNWGPLPIENIVGR 221
Cdd:cd06530  57 ----------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGK 84
PRK10861 PRK10861
signal peptidase I;
54-223 5.85e-13

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 67.39  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373    54 GWVNKLLSVcsedakaaFTAVTVSILFRSALAEPKSIPSTSMYPTLDKGDRVMAEKVSYFFR------------KPEVSD 121
Cdd:PRK10861  59 GWLETGASV--------FPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKdpitqttlietgHPKRGD 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   122 IVIFKappilleYPEygYSSNDvFIKRIVASEGDWV-------EVR-----------DGKLFVN-DIVQEEDFVL----- 177
Cdd:PRK10861 131 IVVFK-------YPE--DPKLD-YIKRVVGLPGDKVtydpvskEVTiqpgcssgqacENALPVTySNVEPSDFVQtfsrr 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   178 ---------------EPMSYEM------EPM-------------------------------FVPKGYVFVLGDNRNKSF 205
Cdd:PRK10861 201 nggeatsgffqvplnETKENGIrlserkETLgdvthriltvpgaqdqvgmyyqqpgqplatwVVPPGQYFMMGDNRDNSA 280

                        250
                 ....*....|....*...
gi 1946373   206 DSHNWGPLPIENIVGRSV 223
Cdd:PRK10861 281 DSRYWGFVPEANLVGKAT 298
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 115-221 3.95e-09

conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding elements of conjugative transfer systems. This family is homologous to a broader family of signal (leader) peptidases such as lepB. This family is present in both Ti-type and I-type conjugative systems.


Pssm-ID: 131818 [Multi-domain]  Cd Length: 171  Bit Score: 54.41  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373    115 RKPEVSDIVIFKAP--PILLEYPEYGYSSNDV-------FIKRIVASEGDWVEVRDGKLFVNDIVQEEDFVLE--PMSYE 183
Cdd:TIGR02771  45 KPVERGDYVVFCPPdnPQFEEARERGYLREGLcpggfgpLLKRVLGLPGDRVTVRADVVAINGQLLPYSKPLAtdSSGRP 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1946373    184 MEPM---FVPKGYvFVLGDNRNKSFDSHNWGPLPIENIVGR 221
Cdd:TIGR02771 125 LPPFpegVIPPGF-FVVHDTSPTSFDSRYFGPISREQVIGR 164
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 90-221 5.63e-09

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 51.88  E-value: 5.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   90 IPSTSMYPTLDKGDRVMAEKVSYFfrkPEVSDIVIFKAPpilleypeygysSNDVFIKRIVASEGdwvevrdgklfvndi 169
Cdd:cd06462   5 VEGDSMEPTIPDGDLVLVDKSSYE---PKRGDIVVFRLP------------GGELTVKRVIGLPG--------------- 54

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 1946373  170 vqeedfvlepmsyemepmfvpKGYVFVLGDNRNkSFDSHNWGPlPIENIVGR 221
Cdd:cd06462  55 ---------------------EGHYFLLGDNPN-SPDSRIDGP-PELDIVGV 83
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 146-228 2.42e-03

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 37.66  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946373   146 IKRIVASEGDWVEVR-----DGKLFVNDIVQEEDFVLEPMSyemePM---FVPKGYVFVLGDNRNkSFDSHNWGPLPIEN 217
Cdd:PRK13838  89 IKTVAALAGQRVEIGgsvsiDGRPLPSSSVRRRDGEGRPLT----PFpggVVPPGHLFLHSSFAG-SYDSRYFGPVPASG 163

                         90
                 ....*....|...
gi 1946373   218 IVG--RSVFRYWP 228
Cdd:PRK13838 164 LLGlaRPVLTFDP 176
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 54-128 7.23e-03

signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, a subunit of the eukaryotic endoplasmic reticulum signal peptidase I complex, and an apparent signal peptidase I from a small number of bacteria. It is related to but does not overlap in hits with TIGR02227, the bacterial and mitochondrial signal peptidase I.


Pssm-ID: 131283  Cd Length: 158  Bit Score: 36.26  E-value: 7.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946373     54 GWVNKLLSVCSEDAKAAFTAVtvSILFRSALAEPK-SIPSTSMYPTLDKGDRVMAEKVSYffRKPEVSDIVIFKAP 128
Cdd:TIGR02228   1 KKISNVIYFILIILLVILLLY--GLVSKASGPDPVvVVLSGSMEPTFNTGDLILVTGADP--NDIQVGDVITYKSP 72
 
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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