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Conserved domains on  [gi|375135609|ref|YP_004996259|]
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leader peptidase (signal peptidase I), serine protease [Acinetobacter pittii PHEA-2]

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;
5-257 7.90e-76

signal peptidase I;


The actual alignment was detected with superfamily member PRK10861:

Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 233.79  E-value: 7.90e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   5 FNLILVPVTLILFAVWLLDKLVL--KQRANKGRGNE------------------NFVITWAYDFwPVLAVVLVLRSFLYE 64
Cdd:PRK10861   5 FALILVIATLVTGILWCVDRFKFapARRARQAAAQAatgdaldkatlakvapkpGWLETGASVF-PVLAIVLIVRSFIYE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  65 PFNIPSDSMVPTLETGDFILVNKFDYGVRLPIVNKKIIDVGEPKRGDVIVFRYPPQPTISYIKRVIGLPGDHIVYD--HG 142
Cdd:PRK10861  84 PFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVTYDpvSK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 143 QLIIN-----GQKVPKVLT-------------QFSREKD-----------VMDT-PTSIY---HKETIGAHTFTMRELEG 189
Cdd:PRK10861 164 EVTIQpgcssGQACENALPvtysnvepsdfvqTFSRRNGgeatsgffqvpLNETkENGIRlseRKETLGDVTHRILTVPG 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375135609 190 vnVARQApfinyvenGKYANQDGL---YWevTVPKGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVWM 257
Cdd:PRK10861 244 --AQDQV--------GMYYQQPGQplaTW--VVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWM 302
 
Name Accession Description Interval E-value
PRK10861 PRK10861
signal peptidase I;
5-257 7.90e-76

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 233.79  E-value: 7.90e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   5 FNLILVPVTLILFAVWLLDKLVL--KQRANKGRGNE------------------NFVITWAYDFwPVLAVVLVLRSFLYE 64
Cdd:PRK10861   5 FALILVIATLVTGILWCVDRFKFapARRARQAAAQAatgdaldkatlakvapkpGWLETGASVF-PVLAIVLIVRSFIYE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  65 PFNIPSDSMVPTLETGDFILVNKFDYGVRLPIVNKKIIDVGEPKRGDVIVFRYPPQPTISYIKRVIGLPGDHIVYD--HG 142
Cdd:PRK10861  84 PFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVTYDpvSK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 143 QLIIN-----GQKVPKVLT-------------QFSREKD-----------VMDT-PTSIY---HKETIGAHTFTMRELEG 189
Cdd:PRK10861 164 EVTIQpgcssGQACENALPvtysnvepsdfvqTFSRRNGgeatsgffqvpLNETkENGIRlseRKETLGDVTHRILTVPG 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375135609 190 vnVARQApfinyvenGKYANQDGL---YWevTVPKGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVWM 257
Cdd:PRK10861 244 --AQDQV--------GMYYQQPGQplaTW--VVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWM 302
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 42-257 5.67e-60

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: 187.41  E-value: 5.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   42 ITWAYDFWPVLAVVLVLRSFLYEPFNIPSDSMVPTLETGDFILVNKFDYGVrlpivnkkiidvGEPKRGDVIVFRYPPQP 121
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGL------------GEPKRGDIVVFRPPEGP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  122 TISYIKRVIGLPGDHIVYDHGQLIINGQKVPKVltqfsrekdvmdtptsiYHKETIGAHTFTMRELEGvnvarqapfiny 201
Cdd:pfam10502  70 GVPLIKRVIGLPGDRVEYKDDQLYINGKPVGEP-----------------YLADRKGRPTFDLPPWQG------------ 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 375135609  202 vengkyanqdglywEVTVPKGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVWM 257
Cdd:pfam10502 121 --------------CRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 61-256 1.73e-46

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: 152.38  E-value: 1.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   61 FLYEPFNIPSDSMVPTLETGDFILVNKFDYGVrlpivnkkiidvGEPKRGDVIVFRYPPQPTISYIKRVIGLPGDHIVYD 140
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRT------------SDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  141 HGQLIINGQKVPKvltqfsrekdvmdtptsiyhketigahtftmrelegvnvarqapfiNYVENGKYANQDGLYWEVTVP 220
Cdd:TIGR02227  69 DGKLYINGKKIDE----------------------------------------------PYLKPNGYLDTSEFNTPVKVP 102

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 375135609  221 KGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVW 256
Cdd:TIGR02227 103 PGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVF 138
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
32-225 2.16e-43

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 146.15  E-value: 2.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  32 NKGRGNENFVITWAYDFWPVLAVVLVLRSFLYEPFNIPSDSMVPTLETGDFILVNKFDYGVrlpivnkkiidvGEPKRGD 111
Cdd:COG0681    2 SKKKKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGF------------GEPKRGD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 112 VIVFRYPPQPTISYIKRVIGLPGDHIVYDHGQLIINGQKV--PKVLTQFSREKDVMDTPTSIYHKETIGAHTFTMRELEG 189
Cdd:COG0681   70 IVVFKYPEDPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLnePYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRS 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 375135609 190 VNVARQAPFINYVENGKYANQDGLYWEVTVPKGHYF 225
Cdd:COG0681  150 GDPDDGGGGVGVDGVGVGGVVDVVVPDVDSRLVDVG 185
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 64-252 6.03e-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: 86.87  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  64 EPFNIPSDSMVPTLETGDFILVNKFDYGVRlpivnkkiidvgEPKRGDVIVFRYPPQPTISYIKRVIGlpgdhivydhgq 143
Cdd:cd06530    1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFR------------EPKRGDVVVFKSPGDPGKPIIKRVIG------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 144 liingqkvpkvltqfsrekdvmdtptsiyhketigahtftmrelegvnvarqapfinyvengkyanqdglywevtvpkgh 223
Cdd:cd06530      --------------------------------------------------------------------------------

                        170       180
                 ....*....|....*....|....*....
gi 375135609 224 YFAMGDNRDQSADSRFWGFVPEENLTGRA 252
Cdd:cd06530   57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
 
Name Accession Description Interval E-value
PRK10861 PRK10861
signal peptidase I;
5-257 7.90e-76

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 233.79  E-value: 7.90e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   5 FNLILVPVTLILFAVWLLDKLVL--KQRANKGRGNE------------------NFVITWAYDFwPVLAVVLVLRSFLYE 64
Cdd:PRK10861   5 FALILVIATLVTGILWCVDRFKFapARRARQAAAQAatgdaldkatlakvapkpGWLETGASVF-PVLAIVLIVRSFIYE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  65 PFNIPSDSMVPTLETGDFILVNKFDYGVRLPIVNKKIIDVGEPKRGDVIVFRYPPQPTISYIKRVIGLPGDHIVYD--HG 142
Cdd:PRK10861  84 PFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVTYDpvSK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 143 QLIIN-----GQKVPKVLT-------------QFSREKD-----------VMDT-PTSIY---HKETIGAHTFTMRELEG 189
Cdd:PRK10861 164 EVTIQpgcssGQACENALPvtysnvepsdfvqTFSRRNGgeatsgffqvpLNETkENGIRlseRKETLGDVTHRILTVPG 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375135609 190 vnVARQApfinyvenGKYANQDGL---YWevTVPKGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVWM 257
Cdd:PRK10861 244 --AQDQV--------GMYYQQPGQplaTW--VVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWM 302
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 42-257 5.67e-60

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: 187.41  E-value: 5.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   42 ITWAYDFWPVLAVVLVLRSFLYEPFNIPSDSMVPTLETGDFILVNKFDYGVrlpivnkkiidvGEPKRGDVIVFRYPPQP 121
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGL------------GEPKRGDIVVFRPPEGP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  122 TISYIKRVIGLPGDHIVYDHGQLIINGQKVPKVltqfsrekdvmdtptsiYHKETIGAHTFTMRELEGvnvarqapfiny 201
Cdd:pfam10502  70 GVPLIKRVIGLPGDRVEYKDDQLYINGKPVGEP-----------------YLADRKGRPTFDLPPWQG------------ 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 375135609  202 vengkyanqdglywEVTVPKGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVWM 257
Cdd:pfam10502 121 --------------CRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 61-256 1.73e-46

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: 152.38  E-value: 1.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   61 FLYEPFNIPSDSMVPTLETGDFILVNKFDYGVrlpivnkkiidvGEPKRGDVIVFRYPPQPTISYIKRVIGLPGDHIVYD 140
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRT------------SDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  141 HGQLIINGQKVPKvltqfsrekdvmdtptsiyhketigahtftmrelegvnvarqapfiNYVENGKYANQDGLYWEVTVP 220
Cdd:TIGR02227  69 DGKLYINGKKIDE----------------------------------------------PYLKPNGYLDTSEFNTPVKVP 102

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 375135609  221 KGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVW 256
Cdd:TIGR02227 103 PGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVF 138
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
32-225 2.16e-43

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 146.15  E-value: 2.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  32 NKGRGNENFVITWAYDFWPVLAVVLVLRSFLYEPFNIPSDSMVPTLETGDFILVNKFDYGVrlpivnkkiidvGEPKRGD 111
Cdd:COG0681    2 SKKKKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGF------------GEPKRGD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 112 VIVFRYPPQPTISYIKRVIGLPGDHIVYDHGQLIINGQKV--PKVLTQFSREKDVMDTPTSIYHKETIGAHTFTMRELEG 189
Cdd:COG0681   70 IVVFKYPEDPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLnePYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRS 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 375135609 190 VNVARQAPFINYVENGKYANQDGLYWEVTVPKGHYF 225
Cdd:COG0681  150 GDPDDGGGGVGVDGVGVGGVVDVVVPDVDSRLVDVG 185
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 109-257 1.97e-25

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: 96.90  E-value: 1.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 109 RGDVIVFRYPPQPTIS---------YIKRVIGLPGDHIVYDHGQLIINGQKVPkvltqFSREKDVMDTPTSIYHketiga 179
Cdd:COG4959    1 RGDLVAFRPPEPLAAErgylprgvpLIKRVAALPGDTVCIKGGQVYINGKPVA-----EALERDRAGRPLPVWQ------ 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375135609 180 htftmrelegvnvarqapfinyvengkyanqdglyWEVTVPKGHYFAMGDNRDQSADSRFWGFVPEENLTGRAFYVWM 257
Cdd:COG4959   70 -----------------------------------GCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWT 112
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 64-252 6.03e-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: 86.87  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609  64 EPFNIPSDSMVPTLETGDFILVNKFDYGVRlpivnkkiidvgEPKRGDVIVFRYPPQPTISYIKRVIGlpgdhivydhgq 143
Cdd:cd06530    1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFR------------EPKRGDVVVFKSPGDPGKPIIKRVIG------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609 144 liingqkvpkvltqfsrekdvmdtptsiyhketigahtftmrelegvnvarqapfinyvengkyanqdglywevtvpkgh 223
Cdd:cd06530      --------------------------------------------------------------------------------

                        170       180
                 ....*....|....*....|....*....
gi 375135609 224 YFAMGDNRDQSADSRFWGFVPEENLTGRA 252
Cdd:cd06530   57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 64-139 1.25e-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: 61.90  E-value: 1.25e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375135609  64 EPFNIPSDSMVPTLETGDFILVNKFDYgvrlpivnkkiidvgEPKRGDVIVFRYPPQptISYIKRVIGLPGDHIVY 139
Cdd:cd06462    1 FALRVEGDSMEPTIPDGDLVLVDKSSY---------------EPKRGDIVVFRLPGG--ELTVKRVIGLPGEGHYF 59
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 71-141 4.21e-06

nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair]


Pssm-ID: 274282 [Multi-domain]  Cd Length: 90  Bit Score: 44.37  E-value: 4.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375135609   71 DSMVPTLETGDFILVNKFDYGVRLpivnkkiidvgePKRGDVIVFRYPPQPTISYIKRVIGLP--GDHIVYDH 141
Cdd:TIGR02754   6 VSMSPTLPPGDRIIVVPWLKIFRV------------PPIGNVVVVRHPLQPYGLIIKRLAAVDdnGLFLLGDN 66
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 66-138 3.07e-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: 39.56  E-value: 3.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375135609  66 FNIPSDSMVPTLETGDFILVNKfdygvrlpivnkkiiDVGEPKRGDVIVFRYPPQptiSYIKRVIGLPGDHIV 138
Cdd:COG2932   38 VRVSGDSMEPTIRDGDIVLVDP---------------SDTEIRDGGIYVVRTDGE---LLVKRLQRRPDGKLR 92
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 51-131 8.66e-04

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: 38.96  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375135609   51 VLAVVLVLRSFLYEP-FNIPSDSMVPTLETGDFILVnkfdygvrlpivnkKIIDVGEPKRGDVIVFRYPPQPTIsYIKRV 129
Cdd:TIGR02228  18 LLLYGLVSKASGPDPvVVVLSGSMEPTFNTGDLILV--------------TGADPNDIQVGDVITYKSPGFNTP-VTHRV 82


                  ..
gi 375135609  130 IG 131
Cdd:TIGR02228  83 IE 84
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 71-138 4.25e-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: 35.23  E-value: 4.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375135609  71 DSMVPTLETGDFILVNKFDygvrlpivnkkiidvgEPKRGDVIVFRYPPQPTisyIKRVIGLPGDHIV 138
Cdd:cd06529    8 DSMEPTIPDGDLVLVDPSD----------------TPRDGDIVVARLDGELT---VKRLQRRGGGRLR 56
 
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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