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Conserved domains on  [gi|2088352412|ref|WP_222582723|]
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signal peptidase I [Algoriphagus marincola]

Protein Classification

S26 family signal peptidase( domain architecture ID 12792757)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
13-166 4.64e-38

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


:

Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 134.59  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  13 REWLDALVFAVVAASLIRWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYgtripktplqvplthqkiwgteipsysdaiq 92
Cdd:COG0681    12 REWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY------------------------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088352412  93 lpymrlpGFADVERNDVVVFNYPVefeypsDLKTNYIKRAVAVPGDVLEIKDGVLYINGESAMQPEEMQFSYNV 166
Cdd:COG0681    61 -------GFGEPKRGDIVVFKYPE------DPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPV 121
PRK10861 super family cl32593
signal peptidase I;
15-352 2.63e-35

signal peptidase I;


The actual alignment was detected with superfamily member PRK10861:

Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 131.33  E-value: 2.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  15 WLD--ALVFAVVAASLI-RWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYGtripktpLQVPLTHQKIWGTEIPsysdai 91
Cdd:PRK10861   60 WLEtgASVFPVLAIVLIvRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYG-------IKDPITQTTLIETGHP------ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  92 qlpymrlpgfadvERNDVVVFNYPVefeypsDLKTNYIKRAVAVPGDvleikdGVLY--INGESAMQP---------EEM 160
Cdd:PRK10861  127 -------------KRGDIVVFKYPE------DPKLDYIKRVVGLPGD------KVTYdpVSKEVTIQPgcssgqaceNAL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 161 QFSYNVVASrmlnADFFAEYGINPASfhIMSDGSYVVfatdlvierlqgsPLITTVrkqimskrgedrifPDGMKMGWNR 240
Cdd:PRK10861  182 PVTYSNVEP----SDFVQTFSRRNGG--EATSGFFQV-------------PLNETK--------------ENGIRLSERK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 241 DQYGP-----LTIPGEgttielnADNILRYgstiknyegHEQveirenelliNGQKVDSYTFKQNYYFMMGDNRHDSLDS 315
Cdd:PRK10861  229 ETLGDvthriLTVPGA-------QDQVGMY---------YQQ----------PGQPLATWVVPPGQYFMMGDNRDNSADS 282

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2088352412 316 RYWGFVPEDHVVGKAWFLWLSLDEFESFF-NKIRWSRI 352
Cdd:PRK10861  283 RYWGFVPEANLVGKATAIWMSFEKQEGEWpTGVRLSRI 320
 
Name Accession Description Interval E-value
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
13-166 4.64e-38

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 134.59  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  13 REWLDALVFAVVAASLIRWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYgtripktplqvplthqkiwgteipsysdaiq 92
Cdd:COG0681    12 REWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY------------------------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088352412  93 lpymrlpGFADVERNDVVVFNYPVefeypsDLKTNYIKRAVAVPGDVLEIKDGVLYINGESAMQPEEMQFSYNV 166
Cdd:COG0681    61 -------GFGEPKRGDIVVFKYPE------DPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPV 121
PRK10861 PRK10861
signal peptidase I;
15-352 2.63e-35

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 131.33  E-value: 2.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  15 WLD--ALVFAVVAASLI-RWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYGtripktpLQVPLTHQKIWGTEIPsysdai 91
Cdd:PRK10861   60 WLEtgASVFPVLAIVLIvRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYG-------IKDPITQTTLIETGHP------ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  92 qlpymrlpgfadvERNDVVVFNYPVefeypsDLKTNYIKRAVAVPGDvleikdGVLY--INGESAMQP---------EEM 160
Cdd:PRK10861  127 -------------KRGDIVVFKYPE------DPKLDYIKRVVGLPGD------KVTYdpVSKEVTIQPgcssgqaceNAL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 161 QFSYNVVASrmlnADFFAEYGINPASfhIMSDGSYVVfatdlvierlqgsPLITTVrkqimskrgedrifPDGMKMGWNR 240
Cdd:PRK10861  182 PVTYSNVEP----SDFVQTFSRRNGG--EATSGFFQV-------------PLNETK--------------ENGIRLSERK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 241 DQYGP-----LTIPGEgttielnADNILRYgstiknyegHEQveirenelliNGQKVDSYTFKQNYYFMMGDNRHDSLDS 315
Cdd:PRK10861  229 ETLGDvthriLTVPGA-------QDQVGMY---------YQQ----------PGQPLATWVVPPGQYFMMGDNRDNSADS 282

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2088352412 316 RYWGFVPEDHVVGKAWFLWLSLDEFESFF-NKIRWSRI 352
Cdd:PRK10861  283 RYWGFVPEANLVGKATAIWMSFEKQEGEWpTGVRLSRI 320
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 13-334 2.03e-32

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: 118.85  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  13 REWLDALVFAVVAASLIRWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYGTRipktplqvplthqkiwgteipsysdaiq 92
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLG---------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  93 lpymrlpgfaDVERNDVVVFNYPvefeypSDLKTNYIKRAVAVPGDVLEIKDGVLYINGEsamqpeemqfsynvvasrml 172
Cdd:pfam10502  54 ----------EPKRGDIVVFRPP------EGPGVPLIKRVIGLPGDRVEYKDDQLYINGK-------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 173 nadffaeyginpasfhimsdgsyvvfatdlvierlqgsplittvrkqimskrgedrifpdgmkmgwnrdqygPLTIPgeg 252
Cdd:pfam10502  98 ------------------------------------------------------------------------PVGEP--- 102

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 253 ttieLNADNILRYGSTIKNYEGHEQVeirenellingqkvdsytfKQNYYFMMGDNRHDSLDSRYWGFVPEDHVVGKAWF 332
Cdd:pfam10502 103 ----YLADRKGRPTFDLPPWQGCRVV-------------------PEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVF 159


                  ..
gi 2088352412 333 LW 334
Cdd:pfam10502 160 PV 161
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 33-338 6.53e-23

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: 93.06  E-value: 6.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  33 LLEPFTIPTASMEKSLLVGDFLFVSKMHYGtripktplqvplthqkiwgteipsysdaiqlpymrlpgFADVERNDVVVF 112
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGDRILVNKFAYR--------------------------------------TSDPKRGDIVVF 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 113 nypvefEYPSDLKTNYIKRAVAVPGDVLEIKDGVLYINGEsamQPEEMQFSYNVvasrmlnadffaeyginpasfhimsd 192
Cdd:TIGR02227  44 ------KDPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGK---KIDEPYLKPNG-------------------------- 88

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 193 gsyvvfatdlvierlqgsplittvrkqimskrgedriFPDGMKMgwnrdqYGPLTIPgegttielnadnilrygstikny 272
Cdd:TIGR02227  89 -------------------------------------YLDTSEF------NTPVKVP----------------------- 102

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2088352412 273 EGHeqveirenellingqkvdsytfkqnyYFMMGDNRHDSLDSRYWGFVPEDHVVGKAWFLWLSLD 338
Cdd:TIGR02227 103 PGH--------------------------YFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 276-336 2.66e-21

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: 87.66  E-value: 2.66e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088352412 276 EQVEIRENELLINGQKVD-----------------SYTFKQNYYFMMGDNRHDSLDSRYWGFVPEDHVVGKAWFLWLS 336
Cdd:COG4959    36 DTVCIKGGQVYINGKPVAealerdragrplpvwqgCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 302-330 7.38e-13

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: 63.37  E-value: 7.38e-13
                          10        20
                  ....*....|....*....|....*....
gi 2088352412 302 YFMMGDNRHDSLDSRYWGFVPEDHVVGKA 330
Cdd:cd06530    57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 35-135 4.75e-08

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: 49.89  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  35 EPFTIPTASMEKSLLVGDFLFVSKMHYGTRIPKtplqvplthqkiwgteipsysdaiqlpymrlpgfadveRNDVVVFNy 114
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPK--------------------------------------RGDVVVFK- 41

                          90       100
                  ....*....|....*....|.
gi 2088352412 115 pvefeYPSDLKTNYIKRAVAV 135
Cdd:cd06530    42 -----SPGDPGKPIIKRVIGY 57
 
Name Accession Description Interval E-value
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
13-166 4.64e-38

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 134.59  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  13 REWLDALVFAVVAASLIRWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYgtripktplqvplthqkiwgteipsysdaiq 92
Cdd:COG0681    12 REWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY------------------------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088352412  93 lpymrlpGFADVERNDVVVFNYPVefeypsDLKTNYIKRAVAVPGDVLEIKDGVLYINGESAMQPEEMQFSYNV 166
Cdd:COG0681    61 -------GFGEPKRGDIVVFKYPE------DPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPV 121
PRK10861 PRK10861
signal peptidase I;
15-352 2.63e-35

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 131.33  E-value: 2.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  15 WLD--ALVFAVVAASLI-RWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYGtripktpLQVPLTHQKIWGTEIPsysdai 91
Cdd:PRK10861   60 WLEtgASVFPVLAIVLIvRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYG-------IKDPITQTTLIETGHP------ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  92 qlpymrlpgfadvERNDVVVFNYPVefeypsDLKTNYIKRAVAVPGDvleikdGVLY--INGESAMQP---------EEM 160
Cdd:PRK10861  127 -------------KRGDIVVFKYPE------DPKLDYIKRVVGLPGD------KVTYdpVSKEVTIQPgcssgqaceNAL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 161 QFSYNVVASrmlnADFFAEYGINPASfhIMSDGSYVVfatdlvierlqgsPLITTVrkqimskrgedrifPDGMKMGWNR 240
Cdd:PRK10861  182 PVTYSNVEP----SDFVQTFSRRNGG--EATSGFFQV-------------PLNETK--------------ENGIRLSERK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 241 DQYGP-----LTIPGEgttielnADNILRYgstiknyegHEQveirenelliNGQKVDSYTFKQNYYFMMGDNRHDSLDS 315
Cdd:PRK10861  229 ETLGDvthriLTVPGA-------QDQVGMY---------YQQ----------PGQPLATWVVPPGQYFMMGDNRDNSADS 282

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2088352412 316 RYWGFVPEDHVVGKAWFLWLSLDEFESFF-NKIRWSRI 352
Cdd:PRK10861  283 RYWGFVPEANLVGKATAIWMSFEKQEGEWpTGVRLSRI 320
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 13-334 2.03e-32

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: 118.85  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  13 REWLDALVFAVVAASLIRWLLLEPFTIPTASMEKSLLVGDFLFVSKMHYGTRipktplqvplthqkiwgteipsysdaiq 92
Cdd:pfam10502   2 LEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLG---------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  93 lpymrlpgfaDVERNDVVVFNYPvefeypSDLKTNYIKRAVAVPGDVLEIKDGVLYINGEsamqpeemqfsynvvasrml 172
Cdd:pfam10502  54 ----------EPKRGDIVVFRPP------EGPGVPLIKRVIGLPGDRVEYKDDQLYINGK-------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 173 nadffaeyginpasfhimsdgsyvvfatdlvierlqgsplittvrkqimskrgedrifpdgmkmgwnrdqygPLTIPgeg 252
Cdd:pfam10502  98 ------------------------------------------------------------------------PVGEP--- 102

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 253 ttieLNADNILRYGSTIKNYEGHEQVeirenellingqkvdsytfKQNYYFMMGDNRHDSLDSRYWGFVPEDHVVGKAWF 332
Cdd:pfam10502 103 ----YLADRKGRPTFDLPPWQGCRVV-------------------PEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVF 159


                  ..
gi 2088352412 333 LW 334
Cdd:pfam10502 160 PV 161
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 33-338 6.53e-23

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: 93.06  E-value: 6.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  33 LLEPFTIPTASMEKSLLVGDFLFVSKMHYGtripktplqvplthqkiwgteipsysdaiqlpymrlpgFADVERNDVVVF 112
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGDRILVNKFAYR--------------------------------------TSDPKRGDIVVF 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 113 nypvefEYPSDLKTNYIKRAVAVPGDVLEIKDGVLYINGEsamQPEEMQFSYNVvasrmlnadffaeyginpasfhimsd 192
Cdd:TIGR02227  44 ------KDPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGK---KIDEPYLKPNG-------------------------- 88

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412 193 gsyvvfatdlvierlqgsplittvrkqimskrgedriFPDGMKMgwnrdqYGPLTIPgegttielnadnilrygstikny 272
Cdd:TIGR02227  89 -------------------------------------YLDTSEF------NTPVKVP----------------------- 102

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2088352412 273 EGHeqveirenellingqkvdsytfkqnyYFMMGDNRHDSLDSRYWGFVPEDHVVGKAWFLWLSLD 338
Cdd:TIGR02227 103 PGH--------------------------YFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 276-336 2.66e-21

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: 87.66  E-value: 2.66e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088352412 276 EQVEIRENELLINGQKVD-----------------SYTFKQNYYFMMGDNRHDSLDSRYWGFVPEDHVVGKAWFLWLS 336
Cdd:COG4959    36 DTVCIKGGQVYINGKPVAealerdragrplpvwqgCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 302-330 7.38e-13

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: 63.37  E-value: 7.38e-13
                          10        20
                  ....*....|....*....|....*....
gi 2088352412 302 YFMMGDNRHDSLDSRYWGFVPEDHVVGKA 330
Cdd:cd06530    57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 35-135 4.75e-08

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: 49.89  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088352412  35 EPFTIPTASMEKSLLVGDFLFVSKMHYGTRIPKtplqvplthqkiwgteipsysdaiqlpymrlpgfadveRNDVVVFNy 114
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPK--------------------------------------RGDVVVFK- 41

                          90       100
                  ....*....|....*....|.
gi 2088352412 115 pvefeYPSDLKTNYIKRAVAV 135
Cdd:cd06530    42 -----SPGDPGKPIIKRVIGY 57
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 299-330 1.94e-04

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: 39.55  E-value: 1.94e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2088352412 299 QNYYFMMGDNrHDSLDSRYWGFvPEDHVVGKA 330
Cdd:cd06462    55 EGHYFLLGDN-PNSPDSRIDGP-PELDIVGVV 84
 
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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