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Conserved domains on  [gi|974226683|gb|KUO67326|]
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MAG: S26 family signal peptidase [Gracilibacter sp. BRH_c7a]

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 ...
 18-175 1.22e-62

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: 190.88  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   18 ILEWVEVVVIAFALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFFKhFGELHPGDVIVFHPPSEAHssDDFIKRL 97
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYG-LGEPKRGDIVVFRPPEGPG--VPLIKRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   98 IALPGDTVEIRDHKTYINGRVIDEPYVVEPQIKTMEL-------VVVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGRT 170
Cdd:pfam10502  78 IGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFDlppwqgcRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRA 157


                  ....*
gi 974226683  171 LFRYW 175
Cdd:pfam10502 158 VFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 18-175 1.22e-62

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: 190.88  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   18 ILEWVEVVVIAFALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFFKhFGELHPGDVIVFHPPSEAHssDDFIKRL 97
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYG-LGEPKRGDIVVFRPPEGPG--VPLIKRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   98 IALPGDTVEIRDHKTYINGRVIDEPYVVEPQIKTMEL-------VVVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGRT 170
Cdd:pfam10502  78 IGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFDlppwqgcRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRA 157


                  ....*
gi 974226683  171 LFRYW 175
Cdd:pfam10502 158 VFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 38-177 8.78e-51

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: 160.09  E-value: 8.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   38 FVIEPRYVPTGSMLPTIQLQDRLMVDKFFFKhFGELHPGDVIVFHPPSeaHSSDDFIKRLIALPGDTVEIRDHKTYINGR 117
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR-TSDPKRGDIVVFKDPD--TNKNIYVKRIIGLPGDKVEFRDGKLYINGK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974226683  118 VIDEPYV---VEPQIKTMEL-VVVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGRTLFRYWPL 177
Cdd:TIGR02227  78 KIDEPYLkpnGYLDTSEFNTpVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPF 141
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
12-162 2.78e-45

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 147.69  E-value: 2.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  12 KSTARKILEWVEVVVIAFALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFFkHFGELHPGDVIVFHPPSEahSSD 91
Cdd:COG0681    5 KKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY-GFGEPKRGDIVVFKYPED--PSK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974226683  92 DFIKRLIALPGDTVEIRDHKTYINGRVIDEPYVVEPQIKTM--ELVVVPEGYAFVMGDNRNNSNDSRVWGFLP 162
Cdd:COG0681   82 DYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSvdGDVEVPPGEEEVPGGGGDNSNDSRSGDPDD 154
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 41-169 6.22e-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: 89.57  E-value: 6.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  41 EPRYVPTGSMLPTIQLQDRLMVDKFFFkHFGELHPGDVIVFHPPSeaHSSDDFIKRLIALpgdtveirdhktyingrvid 120
Cdd:cd06530    1 EPVVVPGGSMEPTLQPGDLVLVNKLSY-GFREPKRGDVVVFKSPG--DPGKPIIKRVIGY-------------------- 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 974226683 121 epyvvepqiktmelvvvpegyaFVMGDNRNNSNDSRVWGFLPLDSITGR 169
Cdd:cd06530   58 ----------------------FVLGDNRNNSLDSRYWGPVPEDDIVGK 84
PRK10861 PRK10861
signal peptidase I;
21-169 8.47e-21

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 87.42  E-value: 8.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  21 WVEVVVIAF---ALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFF--------KHFGEL-HP--GDVIVFHPPSE 86
Cdd:PRK10861  60 WLETGASVFpvlAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYgikdpitqTTLIETgHPkrGDIVVFKYPED 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  87 ahSSDDFIKRLIALPGD---------TVEIR---------DHK---TYIN---------------------------GRV 118
Cdd:PRK10861 140 --PKLDYIKRVVGLPGDkvtydpvskEVTIQpgcssgqacENAlpvTYSNvepsdfvqtfsrrnggeatsgffqvplNET 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974226683 119 IDEPYVVEPQIKTMELV----------------------------VVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGR 169
Cdd:PRK10861 218 KENGIRLSERKETLGDVthriltvpgaqdqvgmyyqqpgqplatwVVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGK 296
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 18-175 1.22e-62

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: 190.88  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   18 ILEWVEVVVIAFALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFFKhFGELHPGDVIVFHPPSEAHssDDFIKRL 97
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYG-LGEPKRGDIVVFRPPEGPG--VPLIKRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   98 IALPGDTVEIRDHKTYINGRVIDEPYVVEPQIKTMEL-------VVVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGRT 170
Cdd:pfam10502  78 IGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFDlppwqgcRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRA 157


                  ....*
gi 974226683  171 LFRYW 175
Cdd:pfam10502 158 VFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 38-177 8.78e-51

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: 160.09  E-value: 8.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   38 FVIEPRYVPTGSMLPTIQLQDRLMVDKFFFKhFGELHPGDVIVFHPPSeaHSSDDFIKRLIALPGDTVEIRDHKTYINGR 117
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYR-TSDPKRGDIVVFKDPD--TNKNIYVKRIIGLPGDKVEFRDGKLYINGK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974226683  118 VIDEPYV---VEPQIKTMEL-VVVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGRTLFRYWPL 177
Cdd:TIGR02227  78 KIDEPYLkpnGYLDTSEFNTpVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPF 141
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
12-162 2.78e-45

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 147.69  E-value: 2.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  12 KSTARKILEWVEVVVIAFALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFFkHFGELHPGDVIVFHPPSEahSSD 91
Cdd:COG0681    5 KKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY-GFGEPKRGDIVVFKYPED--PSK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974226683  92 DFIKRLIALPGDTVEIRDHKTYINGRVIDEPYVVEPQIKTM--ELVVVPEGYAFVMGDNRNNSNDSRVWGFLP 162
Cdd:COG0681   82 DYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSvdGDVEVPPGEEEVPGGGGDNSNDSRSGDPDD 154
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 76-176 1.78e-34

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: 117.70  E-value: 1.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  76 GDVIVFHPPSEAH-------SSDDFIKRLIALPGDTVEIRDHKTYINGRVIDEPYVVEPQIKTMEL----VVVPEGYAFV 144
Cdd:COG4959    2 GDLVAFRPPEPLAaergylpRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPLPVwqgcGVVPEGEYFL 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 974226683 145 MGDNRNNSNDSRVWGFLPLDSITGRTLFRYWP 176
Cdd:COG4959   82 LGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 41-169 6.22e-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: 89.57  E-value: 6.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  41 EPRYVPTGSMLPTIQLQDRLMVDKFFFkHFGELHPGDVIVFHPPSeaHSSDDFIKRLIALpgdtveirdhktyingrvid 120
Cdd:cd06530    1 EPVVVPGGSMEPTLQPGDLVLVNKLSY-GFREPKRGDVVVFKSPG--DPGKPIIKRVIGY-------------------- 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 974226683 121 epyvvepqiktmelvvvpegyaFVMGDNRNNSNDSRVWGFLPLDSITGR 169
Cdd:cd06530   58 ----------------------FVLGDNRNNSLDSRYWGPVPEDDIVGK 84
PRK10861 PRK10861
signal peptidase I;
21-169 8.47e-21

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 87.42  E-value: 8.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  21 WVEVVVIAF---ALSWLIRTFVIEPRYVPTGSMLPTIQLQDRLMVDKFFF--------KHFGEL-HP--GDVIVFHPPSE 86
Cdd:PRK10861  60 WLETGASVFpvlAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYgikdpitqTTLIETgHPkrGDIVVFKYPED 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  87 ahSSDDFIKRLIALPGD---------TVEIR---------DHK---TYIN---------------------------GRV 118
Cdd:PRK10861 140 --PKLDYIKRVVGLPGDkvtydpvskEVTIQpgcssgqacENAlpvTYSNvepsdfvqtfsrrnggeatsgffqvplNET 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974226683 119 IDEPYVVEPQIKTMELV----------------------------VVPEGYAFVMGDNRNNSNDSRVWGFLPLDSITGR 169
Cdd:PRK10861 218 KENGIRLSERKETLGDVthriltvpgaqdqvgmyyqqpgqplatwVVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGK 296
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 44-169 7.04e-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: 58.43  E-value: 7.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  44 YVPTGSMLPTIQLQDRLMVDKFFFkhfgELHPGDVIVFHPPSEahssDDFIKRLIALPGdtveirdhktyingrvidepy 123
Cdd:cd06462    4 RVEGDSMEPTIPDGDLVLVDKSSY----EPKRGDIVVFRLPGG----ELTVKRVIGLPG--------------------- 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 974226683 124 vvepqiktmelvvvpEGYAFVMGDNrNNSNDSRVWGFlPLDSITGR 169
Cdd:cd06462   55 ---------------EGHYFLLGDN-PNSPDSRIDGP-PELDIVGV 83
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 71-169 1.27e-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: 51.71  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683   71 GELHPGDVIVFHPPSEA-----------------HSSDDFIKRLIALPGDTVEIRDHKTYINGRVID--EPYVVEPQIKT 131
Cdd:TIGR02771  45 KPVERGDYVVFCPPDNPqfeearergylreglcpGGFGPLLKRVLGLPGDRVTVRADVVAINGQLLPysKPLATDSSGRP 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 974226683  132 MELV---VVPEGYaFVMGDNRNNSNDSRVWGFLPLDSITGR 169
Cdd:TIGR02771 125 LPPFpegVIPPGF-FVVHDTSPTSFDSRYFGPISREQVIGR 164
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 94-176 1.83e-05

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 43.06  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  94 IKRLIALPGDTVEIRDHKTyINGRVIDEPYVVEPQIKTMELV-----VVPEGYAFVMGDNRnNSNDSRVWGFLPLDSITG 168
Cdd:PRK13838  89 IKTVAALAGQRVEIGGSVS-IDGRPLPSSSVRRRDGEGRPLTpfpggVVPPGHLFLHSSFA-GSYDSRYFGPVPASGLLG 166

                         90
                 ....*....|
gi 974226683 169 --RTLFRYWP 176
Cdd:PRK13838 167 laRPVLTFDP 176
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 49-119 4.36e-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: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974226683  49 SMLPTIQLQDRLMVDkfffKHFGELHPGDVIVFHPPSEAhssddFIKRLIALPGDTVEIR-DHKTY-------------- 113
Cdd:COG2932   44 SMEPTIRDGDIVLVD----PSDTEIRDGGIYVVRTDGEL-----LVKRLQRRPDGKLRLIsDNPAYppieippedadeie 114


                 ....*.
gi 974226683 114 INGRVI 119
Cdd:COG2932  115 IIGRVV 120
 
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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