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Conserved domains on  [gi|503769286|ref|WP_014003362|]
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MULTISPECIES: signal peptidase I [Acidithiobacillus]

Protein Classification

S26 family signal peptidase( domain architecture ID 1001159)

S26 family signal peptidase such as signal peptidase I, an S26 family membrane-bound serine protease which frees proteins tethered to inner or mitochondrial membranes by cleaving off signal peptides during polypeptide translocation

CATH:  2.170.230.10|2.10.109.10
EC:  3.4.21.89
Gene Ontology:  GO:0004252|GO:0006465|GO:0016485|GO:0006508
MEROPS:  S26
PubMed:  22031009|16126156

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10861 super family cl32593
signal peptidase I;
3-256 8.39e-78

signal peptidase I;


The actual alignment was detected with superfamily member PRK10861:

Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 238.42  E-value: 8.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   3 FTLGLFLAVVLTGLVWLLD-IVFFRARRA------------PDTKESVV-------VEYARSFFPVLLVVFLIRAFLFEP 62
Cdd:PRK10861   5 FALILVIATLVTGILWCVDrFKFAPARRArqaaaqaatgdaLDKATLAKvapkpgwLETGASVFPVLAIVLIVRSFIYEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  63 FQVPSGSMIPTIRVGDFLLVNKFAYGLRLPLIHTELTHGGPVQAGDIMVFRYPKNPRIDYIKRVIGLPGDTI-------E 135
Cdd:PRK10861  85 FQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVtydpvskE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 136 VK-----------GNDLYIN-GKLVPQKYIGPFAYRPEGQGDRGMV-IP---TKEYA-------QTIGGHTFHIIEfdTP 192
Cdd:PRK10861 165 VTiqpgcssgqacENALPVTySNVEPSDFVQTFSRRNGGEATSGFFqVPlneTKENGirlserkETLGDVTHRILT--VP 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503769286 193 EAHMDFGPYK-----------VPPNCYFMMGDDRDNSNDSRFWGCVPRANIVGKAMFVWFSWDSE--NW--SIRWNQIG 256
Cdd:PRK10861 243 GAQDQVGMYYqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQegEWptGVRLSRIG 321
 
Name Accession Description Interval E-value
PRK10861 PRK10861
signal peptidase I;
3-256 8.39e-78

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 238.42  E-value: 8.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   3 FTLGLFLAVVLTGLVWLLD-IVFFRARRA------------PDTKESVV-------VEYARSFFPVLLVVFLIRAFLFEP 62
Cdd:PRK10861   5 FALILVIATLVTGILWCVDrFKFAPARRArqaaaqaatgdaLDKATLAKvapkpgwLETGASVFPVLAIVLIVRSFIYEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  63 FQVPSGSMIPTIRVGDFLLVNKFAYGLRLPLIHTELTHGGPVQAGDIMVFRYPKNPRIDYIKRVIGLPGDTI-------E 135
Cdd:PRK10861  85 FQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVtydpvskE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 136 VK-----------GNDLYIN-GKLVPQKYIGPFAYRPEGQGDRGMV-IP---TKEYA-------QTIGGHTFHIIEfdTP 192
Cdd:PRK10861 165 VTiqpgcssgqacENALPVTySNVEPSDFVQTFSRRNGGEATSGFFqVPlneTKENGirlserkETLGDVTHRILT--VP 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503769286 193 EAHMDFGPYK-----------VPPNCYFMMGDDRDNSNDSRFWGCVPRANIVGKAMFVWFSWDSE--NW--SIRWNQIG 256
Cdd:PRK10861 243 GAQDQVGMYYqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQegEWptGVRLSRIG 321
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 40-241 1.19e-66

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: 203.98  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   40 EYARSFFPVLLVVFLIRAFLFEPFQVPSGSMIPTIRVGDFLLVNKFAYGLrlplihtelthgGPVQAGDIMVFRYPKNPR 119
Cdd:pfam10502   3 EWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGL------------GEPKRGDIVVFRPPEGPG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  120 IDYIKRVIGLPGDTIEVKGNDLYINGKLVPQKYIGPFAYRpegqgdrgmviPTKEYAQTIGGHTfhiiefdtpeahmdfg 199
Cdd:pfam10502  71 VPLIKRVIGLPGDRVEYKDDQLYINGKPVGEPYLADRKGR-----------PTFDLPPWQGCRV---------------- 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 503769286  200 pykVPPNCYFMMGDDRDNSNDSRFWGCVPRANIVGKAMFVWF 241
Cdd:pfam10502 124 ---VPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
34-225 1.90e-51

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 166.57  E-value: 1.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  34 KESVVVEYARSFFPVLLVVFLIRAFLFEPFQVPSGSMIPTIRVGDFLLVNKFAYGLRLPlihtelthggpvQAGDIMVFR 113
Cdd:COG0681    7 KKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEP------------KRGDIVVFK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 114 YPKNPRIDYIKRVIGLPGDTIEVKGNDLYINGKLVPQKYIGPFAYRPEGQGDRGMViptkEYAQTIGGHTFHIIEFDTPE 193
Cdd:COG0681   75 YPEDPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVP----PGEEEVPGGGGDNSNDSRSG 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 503769286 194 AHMDFGPYKVPPNCYFMMGDDRDNSNDSRFWG 225
Cdd:COG0681  151 DPDDGGGGVGVDGVGVGGVVDVVVPDVDSRLV 182
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 58-244 1.92e-50

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: 162.01  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   58 FLFEPFQVPSGSMIPTIRVGDFLLVNKFAYGlrlplihtelthGGPVQAGDIMVFRYPKNPRIDYIKRVIGLPGDTIEVK 137
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR------------TSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  138 GNDLYINGKLVPQKYIGPFAYRPEGqgdrGMViptkeyaqtigghtfhiiefdtpeahmdfGPYKVPPNCYFMMGDDRDN 217
Cdd:TIGR02227  69 DGKLYINGKKIDEPYLKPNGYLDTS----EFN-----------------------------TPVKVPPGHYFVLGDNRDN 115

                         170       180
                  ....*....|....*....|....*..
gi 503769286  218 SNDSRFWGCVPRANIVGKAMFVWFSWD 244
Cdd:TIGR02227 116 SLDSRYFGFVPIDQIIGKVSFVFYPFD 142
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 61-236 7.91e-24

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: 91.88  E-value: 7.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  61 EPFQVPSGSMIPTIRVGDFLLVNKFAYglrlplihteltHGGPVQAGDIMVFRYPKNPRIDYIKRVIGlpgdtievkgnd 140
Cdd:cd06530    1 EPVVVPGGSMEPTLQPGDLVLVNKLSY------------GFREPKRGDVVVFKSPGDPGKPIIKRVIG------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 141 lyingklvpqkyigpfayrpegqgdrgmviptkeyaqtigghtfhiiefdtpeahmdfgpykvppncYFMMGDDRDNSND 220
Cdd:cd06530   57 -------------------------------------------------------------------YFVLGDNRNNSLD 69

                        170
                 ....*....|....*.
gi 503769286 221 SRFWGCVPRANIVGKA 236
Cdd:cd06530   70 SRYWGPVPEDDIVGKV 85
 
Name Accession Description Interval E-value
PRK10861 PRK10861
signal peptidase I;
3-256 8.39e-78

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 238.42  E-value: 8.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   3 FTLGLFLAVVLTGLVWLLD-IVFFRARRA------------PDTKESVV-------VEYARSFFPVLLVVFLIRAFLFEP 62
Cdd:PRK10861   5 FALILVIATLVTGILWCVDrFKFAPARRArqaaaqaatgdaLDKATLAKvapkpgwLETGASVFPVLAIVLIVRSFIYEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  63 FQVPSGSMIPTIRVGDFLLVNKFAYGLRLPLIHTELTHGGPVQAGDIMVFRYPKNPRIDYIKRVIGLPGDTI-------E 135
Cdd:PRK10861  85 FQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVtydpvskE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 136 VK-----------GNDLYIN-GKLVPQKYIGPFAYRPEGQGDRGMV-IP---TKEYA-------QTIGGHTFHIIEfdTP 192
Cdd:PRK10861 165 VTiqpgcssgqacENALPVTySNVEPSDFVQTFSRRNGGEATSGFFqVPlneTKENGirlserkETLGDVTHRILT--VP 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503769286 193 EAHMDFGPYK-----------VPPNCYFMMGDDRDNSNDSRFWGCVPRANIVGKAMFVWFSWDSE--NW--SIRWNQIG 256
Cdd:PRK10861 243 GAQDQVGMYYqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQegEWptGVRLSRIG 321
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 40-241 1.19e-66

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: 203.98  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   40 EYARSFFPVLLVVFLIRAFLFEPFQVPSGSMIPTIRVGDFLLVNKFAYGLrlplihtelthgGPVQAGDIMVFRYPKNPR 119
Cdd:pfam10502   3 EWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGL------------GEPKRGDIVVFRPPEGPG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  120 IDYIKRVIGLPGDTIEVKGNDLYINGKLVPQKYIGPFAYRpegqgdrgmviPTKEYAQTIGGHTfhiiefdtpeahmdfg 199
Cdd:pfam10502  71 VPLIKRVIGLPGDRVEYKDDQLYINGKPVGEPYLADRKGR-----------PTFDLPPWQGCRV---------------- 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 503769286  200 pykVPPNCYFMMGDDRDNSNDSRFWGCVPRANIVGKAMFVWF 241
Cdd:pfam10502 124 ---VPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
34-225 1.90e-51

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 166.57  E-value: 1.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  34 KESVVVEYARSFFPVLLVVFLIRAFLFEPFQVPSGSMIPTIRVGDFLLVNKFAYGLRLPlihtelthggpvQAGDIMVFR 113
Cdd:COG0681    7 KKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEP------------KRGDIVVFK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 114 YPKNPRIDYIKRVIGLPGDTIEVKGNDLYINGKLVPQKYIGPFAYRPEGQGDRGMViptkEYAQTIGGHTFHIIEFDTPE 193
Cdd:COG0681   75 YPEDPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVP----PGEEEVPGGGGDNSNDSRSG 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 503769286 194 AHMDFGPYKVPPNCYFMMGDDRDNSNDSRFWG 225
Cdd:COG0681  151 DPDDGGGGVGVDGVGVGGVVDVVVPDVDSRLV 182
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 58-244 1.92e-50

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: 162.01  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   58 FLFEPFQVPSGSMIPTIRVGDFLLVNKFAYGlrlplihtelthGGPVQAGDIMVFRYPKNPRIDYIKRVIGLPGDTIEVK 137
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR------------TSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  138 GNDLYINGKLVPQKYIGPFAYRPEGqgdrGMViptkeyaqtigghtfhiiefdtpeahmdfGPYKVPPNCYFMMGDDRDN 217
Cdd:TIGR02227  69 DGKLYINGKKIDEPYLKPNGYLDTS----EFN-----------------------------TPVKVPPGHYFVLGDNRDN 115

                         170       180
                  ....*....|....*....|....*..
gi 503769286  218 SNDSRFWGCVPRANIVGKAMFVWFSWD 244
Cdd:TIGR02227 116 SLDSRYFGFVPIDQIIGKVSFVFYPFD 142
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 107-242 3.39e-31

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: 111.93  E-value: 3.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 107 GDIMVFRYPKNPR---------IDYIKRVIGLPGDTIEVKGNDLYINGKLVPQKYIGPFAYRPEGQGdrgmviptkeyaq 177
Cdd:COG4959    2 GDLVAFRPPEPLAaergylprgVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPLPVW------------- 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503769286 178 tigghtfhiiefdtpeahmdFGPYKVPPNCYFMMGDDRDNSNDSRFWGCVPRANIVGKAMFVWFS 242
Cdd:COG4959   69 --------------------QGCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 61-236 7.91e-24

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: 91.88  E-value: 7.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  61 EPFQVPSGSMIPTIRVGDFLLVNKFAYglrlplihteltHGGPVQAGDIMVFRYPKNPRIDYIKRVIGlpgdtievkgnd 140
Cdd:cd06530    1 EPVVVPGGSMEPTLQPGDLVLVNKLSY------------GFREPKRGDVVVFKSPGDPGKPIIKRVIG------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286 141 lyingklvpqkyigpfayrpegqgdrgmviptkeyaqtigghtfhiiefdtpeahmdfgpykvppncYFMMGDDRDNSND 220
Cdd:cd06530   57 -------------------------------------------------------------------YFVLGDNRNNSLD 69

                        170
                 ....*....|....*.
gi 503769286 221 SRFWGCVPRANIVGKA 236
Cdd:cd06530   70 SRYWGPVPEDDIVGKV 85
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 61-142 3.18e-12

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: 60.74  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  61 EPFQVPSGSMIPTIRVGDFLLVNKFAYglrlplihtelthggPVQAGDIMVFRYPKNprIDYIKRVIGLPG-DTIEVKG- 138
Cdd:cd06462    1 FALRVEGDSMEPTIPDGDLVLVDKSSY---------------EPKRGDIVVFRLPGG--ELTVKRVIGLPGeGHYFLLGd 63


                 ....
gi 503769286 139 NDLY 142
Cdd:cd06462   64 NPNS 67
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 91-240 1.77e-08

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: 52.87  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286   91 LPLIHTELTHGGPVQAGDIMVFRYPKNPRIDY-------------------IKRVIGLPGDTIEVKGNDLYINGKLVPqk 151
Cdd:TIGR02771  34 LPLGLYWTTSSKPVERGDYVVFCPPDNPQFEEarergylreglcpggfgplLKRVLGLPGDRVTVRADVVAINGQLLP-- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503769286  152 YIGPFAYRPEGqgdRGMViptkeyaqtigghtfhiiefdtpeahmDFGPYKVPPNcYFMMGDDRDNSNDSRFWGCVPRAN 231
Cdd:TIGR02771 112 YSKPLATDSSG---RPLP---------------------------PFPEGVIPPG-FFVVHDTSPTSFDSRYFGPISREQ 160

                         170
                  ....*....|.
gi 503769286  232 IVGKA--MFVW 240
Cdd:TIGR02771 161 VIGRVkpLFTW 171
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 65-128 2.03e-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: 37.80  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503769286   65 VPSGSMIPTIRVGDFLLVnkfayglrlplihtELTHGGPVQAGDIMVFRYPkNPRIDYIKRVIG 128
Cdd:TIGR02228  36 VLSGSMEPTFNTGDLILV--------------TGADPNDIQVGDVITYKSP-GFNTPVTHRVIE 84
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 69-137 6.56e-03

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: 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 LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are 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. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 34.84  E-value: 6.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503769286  69 SMIPTIRVGDFLLVNKfayglrlplihtelthGGPVQAGDIMVFRYPKNPridYIKRVIGLPGDTIEVK 137
Cdd:cd06529    9 SMEPTIPDGDLVLVDP----------------SDTPRDGDIVVARLDGEL---TVKRLQRRGGGRLRLI 58
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 63-137 7.40e-03

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 35.71  E-value: 7.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503769286  63 FQVPSGSMIPTIRVGDFLLVNkfayglrlplihtelTHGGPVQAGDIMVFRYPKNPridYIKRVIGLPGDTIEVK 137
Cdd:COG2932   38 VRVSGDSMEPTIRDGDIVLVD---------------PSDTEIRDGGIYVVRTDGEL---LVKRLQRRPDGKLRLI 94
 
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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