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Conserved domains on  [gi|1261289014|ref|WP_097816569.1|]
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signal peptidase I

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 ...
 10-175 2.01e-76

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: 225.93  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  10 IEWIRTILIGVLLAVFFRTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGLP 87
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPpeGPGVPLIKRVIGLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  88 GDQIEYKHDKLYINGQFLDEPYLETYKKEIngrqltgDFKLEELTKEKSVPPGYIFVVGDNRLGSWDSRHFGFVKADTVV 167
Cdd:pfam10502  82 GDRVEYKDDQLYINGKPVGEPYLADRKGRP-------TFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 1261289014 168 GKVDLRYW 175
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 ...
 10-175 2.01e-76

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: 225.93  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  10 IEWIRTILIGVLLAVFFRTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGLP 87
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPpeGPGVPLIKRVIGLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  88 GDQIEYKHDKLYINGQFLDEPYLETYKKEIngrqltgDFKLEELTKEKSVPPGYIFVVGDNRLGSWDSRHFGFVKADTVV 167
Cdd:pfam10502  82 GDRVEYKDDQLYINGKPVGEPYLADRKGRP-------TFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 1261289014 168 GKVDLRYW 175
Cdd:pfam10502 155 GRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 29-176 1.83e-53

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: 167.02  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  29 FFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGLPGDQIEYKHDKLYINGQFLD 106
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDpdTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014 107 EPYLETYKKEINGRQLTGDfkleeltkekSVPPGYIFVVGDNRLGSWDSRHFGFVKADTVVGKVDLRYWP 176
Cdd:TIGR02227  81 EPYLKPNGYLDTSEFNTPV----------KVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYP 140
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
2-176 1.60e-47

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 153.47  E-value: 1.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014   2 KKTLKKEGIEWIRTILIGVLLAVFFRTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDY 79
Cdd:COG0681     4 KKKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYpeDPSKDY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  80 VKRIIGLPGDQIEYKHDKLYINGQFLDEPYLETYKKEINGRQLTGDFKLEELTKEKSVPPGYIFVVGDNRLGSWDSRHFG 159
Cdd:COG0681    84 IKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDG 163

                         170
                  ....*....|....*..
gi 1261289014 160 FVKADTVVGKVDLRYWP 176
Cdd:COG0681   164 VGVGGVVDVVVPDVDSR 180
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 32-170 9.67e-23

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: 86.87  E-value: 9.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  32 STYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGlpgdqieykhdklyingqfldepy 109
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSpgDPGKPIIKRVIG------------------------ 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261289014 110 letykkeingrqltgdfkleeltkeksvppgyIFVVGDNRLGSWDSRHFGFVKADTVVGKV 170
Cdd:cd06530    57 --------------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
2-169 3.14e-20

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 85.88  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014   2 KKTLKKEGieWIRTI--LIGVLLAVFF-RTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSY------------QVGDLNRF 66
Cdd:PRK10861   52 AKVAPKPG--WLETGasVFPVLAIVLIvRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYgikdpitqttliETGHPKRG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  67 DVVVFH--ANKKEDYVKRIIGLPGDQIEYK--HDKLYIN-----GQFLDEPYLETY-----------------KKEING- 119
Cdd:PRK10861  130 DIVVFKypEDPKLDYIKRVVGLPGDKVTYDpvSKEVTIQpgcssGQACENALPVTYsnvepsdfvqtfsrrngGEATSGf 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014 120 ------RQLTGDFKLEELTK-------------------------------EKSVPPGYIFVVGDNRLGSWDSRHFGFVK 162
Cdd:PRK10861  210 fqvplnETKENGIRLSERKEtlgdvthriltvpgaqdqvgmyyqqpgqplaTWVVPPGQYFMMGDNRDNSADSRYWGFVP 289


                  ....*..
gi 1261289014 163 ADTVVGK 169
Cdd:PRK10861  290 EANLVGK 296
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 10-175 2.01e-76

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: 225.93  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  10 IEWIRTILIGVLLAVFFRTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGLP 87
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPpeGPGVPLIKRVIGLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  88 GDQIEYKHDKLYINGQFLDEPYLETYKKEIngrqltgDFKLEELTKEKSVPPGYIFVVGDNRLGSWDSRHFGFVKADTVV 167
Cdd:pfam10502  82 GDRVEYKDDQLYINGKPVGEPYLADRKGRP-------TFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 1261289014 168 GKVDLRYW 175
Cdd:pfam10502 155 GRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 29-176 1.83e-53

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: 167.02  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  29 FFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGLPGDQIEYKHDKLYINGQFLD 106
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDpdTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014 107 EPYLETYKKEINGRQLTGDfkleeltkekSVPPGYIFVVGDNRLGSWDSRHFGFVKADTVVGKVDLRYWP 176
Cdd:TIGR02227  81 EPYLKPNGYLDTSEFNTPV----------KVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYP 140
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
2-176 1.60e-47

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 153.47  E-value: 1.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014   2 KKTLKKEGIEWIRTILIGVLLAVFFRTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDY 79
Cdd:COG0681     4 KKKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYpeDPSKDY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  80 VKRIIGLPGDQIEYKHDKLYINGQFLDEPYLETYKKEINGRQLTGDFKLEELTKEKSVPPGYIFVVGDNRLGSWDSRHFG 159
Cdd:COG0681    84 IKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDG 163

                         170
                  ....*....|....*..
gi 1261289014 160 FVKADTVVGKVDLRYWP 176
Cdd:COG0681   164 VGVGGVVDVVVPDVDSR 180
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 65-176 6.39e-28

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: 101.14  E-value: 6.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  65 RFDVVVFHA-----------NKKEDYVKRIIGLPGDQIEYKHDKLYINGQFLDEPYLetykKEINGRQLTGdfkleeLTK 133
Cdd:COG4959     1 RGDLVAFRPpeplaaergylPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALE----RDRAGRPLPV------WQG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1261289014 134 EKSVPPGYIFVVGDNRLGSWDSRHFGFVKADTVVGKVDLRYWP 176
Cdd:COG4959    71 CGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 32-170 9.67e-23

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: 86.87  E-value: 9.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  32 STYVVEGKSMMPTLQDGNMLVVNKVSYQVGDLNRFDVVVFHA--NKKEDYVKRIIGlpgdqieykhdklyingqfldepy 109
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSpgDPGKPIIKRVIG------------------------ 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261289014 110 letykkeingrqltgdfkleeltkeksvppgyIFVVGDNRLGSWDSRHFGFVKADTVVGKV 170
Cdd:cd06530    57 --------------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
2-169 3.14e-20

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 85.88  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014   2 KKTLKKEGieWIRTI--LIGVLLAVFF-RTFFFSTYVVEGKSMMPTLQDGNMLVVNKVSY------------QVGDLNRF 66
Cdd:PRK10861   52 AKVAPKPG--WLETGasVFPVLAIVLIvRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYgikdpitqttliETGHPKRG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  67 DVVVFH--ANKKEDYVKRIIGLPGDQIEYK--HDKLYIN-----GQFLDEPYLETY-----------------KKEING- 119
Cdd:PRK10861  130 DIVVFKypEDPKLDYIKRVVGLPGDKVTYDpvSKEVTIQpgcssGQACENALPVTYsnvepsdfvqtfsrrngGEATSGf 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014 120 ------RQLTGDFKLEELTK-------------------------------EKSVPPGYIFVVGDNRLGSWDSRHFGFVK 162
Cdd:PRK10861  210 fqvplnETKENGIRLSERKEtlgdvthriltvpgaqdqvgmyyqqpgqplaTWVVPPGQYFMMGDNRDNSADSRYWGFVP 289


                  ....*..
gi 1261289014 163 ADTVVGK 169
Cdd:PRK10861  290 EANLVGK 296
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 34-120 1.79e-15

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: 68.06  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  34 YVVEGKSMMPTLQDGNMLVVNKVSYqvgDLNRFDVVVFHANKKEDYVKRIIGLPGdqieykHDKLYI---NGQFLDEPYL 110
Cdd:cd06462     3 LRVEGDSMEPTIPDGDLVLVDKSSY---EPKRGDIVVFRLPGGELTVKRVIGLPG------EGHYFLlgdNPNSPDSRID 73

                          90
                  ....*....|
gi 1261289014 111 ETYKKEINGR 120
Cdd:cd06462    74 GPPELDIVGV 83
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 17-170 6.37e-10

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: 55.56  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  17 LIGVLLAVFFRTFFFSTYVVEGK-SMMPTLQDGNMLVVNKVSYQVGDLNRF---DVVVFHANKKEDYV------------ 80
Cdd:TIGR02771   5 VLGIAGLALSGLTILGLYCVGARiNTTKSLPLGLYWTTSSKPVERGDYVVFcppDNPQFEEARERGYLreglcpggfgpl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  81 -KRIIGLPGDQIEYKHDKLYINGQFLdePYLETYKKEINGRqltgdfKLEELTKEKsVPPGYIFVVGDNRlGSWDSRHFG 159
Cdd:TIGR02771  85 lKRVLGLPGDRVTVRADVVAINGQLL--PYSKPLATDSSGR------PLPPFPEGV-IPPGFFVVHDTSP-TSFDSRYFG 154

                         170
                  ....*....|.
gi 1261289014 160 FVKADTVVGKV 170
Cdd:TIGR02771 155 PISREQVIGRV 165
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 36-92 2.20e-04

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: 38.31  E-value: 2.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1261289014  36 VEGKSMMPTLQDGNMLVVNK-VSYQVGDLnrfdVVVFHANkkEDYVKRIIGLPGDQIE 92
Cdd:cd06529     5 VKGDSMEPTIPDGDLVLVDPsDTPRDGDI----VVARLDG--ELTVKRLQRRGGGRLR 56
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 80-168 4.20e-04

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 39.21  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  80 VKRIIGLPGDQIEYKhDKLYINGQFLdePYLETYKKEINGRQLTGDfkleeltKEKSVPPGYIFVVGDNRlGSWDSRHFG 159
Cdd:PRK13838   89 IKTVAALAGQRVEIG-GSVSIDGRPL--PSSSVRRRDGEGRPLTPF-------PGGVVPPGHLFLHSSFA-GSYDSRYFG 157


                  ....*....
gi 1261289014 160 FVKADTVVG 168
Cdd:PRK13838  158 PVPASGLLG 166
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 36-92 6.51e-04

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 38.02  E-value: 6.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1261289014  36 VEGKSMMPTLQDGNMLVVNKvsyQVGDLNRFDVVVFHANKKEdYVKRIIGLPGDQIE 92
Cdd:COG2932    40 VSGDSMEPTIRDGDIVLVDP---SDTEIRDGGIYVVRTDGEL-LVKRLQRRPDGKLR 92
Peptidase_S24 pfam00717
Peptidase S24-like;
36-120 3.41e-03

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 35.64  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261289014  36 VEGKSMMPTLQDGNMLVVNK-VSYQVGdlnrfDVVVFHANkKEDYVKRIIgLPGDQIEYKHDklyiNGQFLDEPYLETYK 114
Cdd:pfam00717  40 VKGDSMEPGIPDGDLVLVDPsREARNG-----DIVVARLD-GEATVKRLY-RDGGGIRLISL----NPEYPPIELPAEDD 108


                  ....*.
gi 1261289014 115 KEINGR 120
Cdd:pfam00717 109 VEIIGR 114
 
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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