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Conserved domains on  [gi|985494063|ref|WP_060792036|]
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MULTISPECIES: signal peptidase I [Enterococcus]

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 ...
 8-181 2.18e-53

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: 167.38  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063    8 NWLLLFFIVA--VVLIRLFVLTPVQVSGHSMDPTLADKQRLIASKISSYDRQ----DIVICVEPDDPSKIAVKRLIGLPG 81
Cdd:pfam10502   3 EWVKAIVIALllALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEpkrgDIVVFRPPEGPGVPLIKRVIGLPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   82 DTIEMKDDVLTINGEVYEEPYLDEFKEKFADDqlqdeysyremFQQIAAGaehftddftVTVPEGSYFVMGDNRLISRDS 161
Cdd:pfam10502  83 DRVEYKDDQLYINGKPVGEPYLADRKGRPTFD-----------LPPWQGC---------RVVPEGEYFVMGDNRDNSLDS 142

                         170       180
                  ....*....|....*....|
gi 985494063  162 RSFGVVTEDQMEGKVLLRFW 181
Cdd:pfam10502 143 RYFGFVPASNIVGRAVFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 8-181 2.18e-53

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: 167.38  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063    8 NWLLLFFIVA--VVLIRLFVLTPVQVSGHSMDPTLADKQRLIASKISSYDRQ----DIVICVEPDDPSKIAVKRLIGLPG 81
Cdd:pfam10502   3 EWVKAIVIALllALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEpkrgDIVVFRPPEGPGVPLIKRVIGLPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   82 DTIEMKDDVLTINGEVYEEPYLDEFKEKFADDqlqdeysyremFQQIAAGaehftddftVTVPEGSYFVMGDNRLISRDS 161
Cdd:pfam10502  83 DRVEYKDDQLYINGKPVGEPYLADRKGRPTFD-----------LPPWQGC---------RVVPEGEYFVMGDNRDNSLDS 142

                         170       180
                  ....*....|....*....|
gi 985494063  162 RSFGVVTEDQMEGKVLLRFW 181
Cdd:pfam10502 143 RYFGFVPASNIVGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 24-184 1.20e-45

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: 146.99  E-value: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   24 FVLTPVQVSGHSMDPTLADKQRLIASKI----SSYDRQDIVICVEPDDPSKIAVKRLIGLPGDTIEMKDDVLTINGEVYE 99
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFayrtSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  100 EPYLDEFKEKFADDQLqdeysyremfqqiaagaehftddFTVTVPEGSYFVMGDNRLISRDSRSFGVVTEDQMEGKVLLR 179
Cdd:TIGR02227  81 EPYLKPNGYLDTSEFN-----------------------TPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFV 137


                  ....*
gi 985494063  180 FWPLN 184
Cdd:TIGR02227 138 FYPFD 142
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
3-170 5.54e-31

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 111.10  E-value: 5.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   3 KILKENWLLLFF-IVAVVLIRLFVLTPVQVSGHSMDPTLADKQRLIASKIS----SYDRQDIVICVEPDDPSKIAVKRLI 77
Cdd:COG0681    9 RELREWLKSIVIaLLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSygfgEPKRGDIVVFKYPEDPSKDYIKRVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  78 GLPGDTIEMKDDVLTINGEVYEEPYLDEFKEKFADDQLQDEYSYRE-----MFQQIAAGAEHFTDDFTVTVPEGSYFVMG 152
Cdd:COG0681   89 GLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEevpggGGDNSNDSRSGDPDDGGGGVGVDGVGVGG 168

                        170
                 ....*....|....*...
gi 985494063 153 DNRLISRDSRSFGVVTED 170
Cdd:COG0681  169 VVDVVVPDVDSRLVDVGD 186
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 28-176 9.20e-15

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: 66.07  E-value: 9.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  28 PVQVSGHSMDPTLADKQRLIASKIS----SYDRQDIVICVEPDDPSKIAVKRLIGlpgdtiemkddvltingevyeepyl 103
Cdd:cd06530    2 PVVVPGGSMEPTLQPGDLVLVNKLSygfrEPKRGDVVVFKSPGDPGKPIIKRVIG------------------------- 56

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985494063 104 defkekfaddqlqdeysyremfqqiaagaehftddftvtvpegsYFVMGDNRLISRDSRSFGVVTEDQMEGKV 176
Cdd:cd06530   57 --------------------------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
12-175 2.56e-14

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 69.70  E-value: 2.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  12 LFFIVAVVLI-RLFVLTPVQVSGHSMDPTLadkqrLIASKI----SSY-----------------DRQDIVICVEPDDPS 69
Cdd:PRK10861  67 VFPVLAIVLIvRSFIYEPFQIPSGSMMPTL-----LIGDFIlvekFAYgikdpitqttlietghpKRGDIVVFKYPEDPK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  70 KIAVKRLIGLPGD--------------------------------TIEMKDDVLTINGE--------VYEEPY------- 102
Cdd:PRK10861 142 LDYIKRVVGLPGDkvtydpvskevtiqpgcssgqacenalpvtysNVEPSDFVQTFSRRnggeatsgFFQVPLnetkeng 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063 103 --LDEFKEKFAD--------DQLQDEYS--YREMFQQIAagaehftddfTVTVPEGSYFVMGDNRLISRDSRSFGVVTED 170
Cdd:PRK10861 222 irLSERKETLGDvthriltvPGAQDQVGmyYQQPGQPLA----------TWVVPPGQYFMMGDNRDNSADSRYWGFVPEA 291


                 ....*
gi 985494063 171 QMEGK 175
Cdd:PRK10861 292 NLVGK 296
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 8-181 2.18e-53

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: 167.38  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063    8 NWLLLFFIVA--VVLIRLFVLTPVQVSGHSMDPTLADKQRLIASKISSYDRQ----DIVICVEPDDPSKIAVKRLIGLPG 81
Cdd:pfam10502   3 EWVKAIVIALllALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEpkrgDIVVFRPPEGPGVPLIKRVIGLPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   82 DTIEMKDDVLTINGEVYEEPYLDEFKEKFADDqlqdeysyremFQQIAAGaehftddftVTVPEGSYFVMGDNRLISRDS 161
Cdd:pfam10502  83 DRVEYKDDQLYINGKPVGEPYLADRKGRPTFD-----------LPPWQGC---------RVVPEGEYFVMGDNRDNSLDS 142

                         170       180
                  ....*....|....*....|
gi 985494063  162 RSFGVVTEDQMEGKVLLRFW 181
Cdd:pfam10502 143 RYFGFVPASNIVGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 24-184 1.20e-45

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: 146.99  E-value: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   24 FVLTPVQVSGHSMDPTLADKQRLIASKI----SSYDRQDIVICVEPDDPSKIAVKRLIGLPGDTIEMKDDVLTINGEVYE 99
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFayrtSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  100 EPYLDEFKEKFADDQLqdeysyremfqqiaagaehftddFTVTVPEGSYFVMGDNRLISRDSRSFGVVTEDQMEGKVLLR 179
Cdd:TIGR02227  81 EPYLKPNGYLDTSEFN-----------------------TPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFV 137


                  ....*
gi 985494063  180 FWPLN 184
Cdd:TIGR02227 138 FYPFD 142
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
3-170 5.54e-31

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 111.10  E-value: 5.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063   3 KILKENWLLLFF-IVAVVLIRLFVLTPVQVSGHSMDPTLADKQRLIASKIS----SYDRQDIVICVEPDDPSKIAVKRLI 77
Cdd:COG0681    9 RELREWLKSIVIaLLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSygfgEPKRGDIVVFKYPEDPSKDYIKRVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  78 GLPGDTIEMKDDVLTINGEVYEEPYLDEFKEKFADDQLQDEYSYRE-----MFQQIAAGAEHFTDDFTVTVPEGSYFVMG 152
Cdd:COG0681   89 GLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEevpggGGDNSNDSRSGDPDDGGGGVGVDGVGVGG 168

                        170
                 ....*....|....*...
gi 985494063 153 DNRLISRDSRSFGVVTED 170
Cdd:COG0681  169 VVDVVVPDVDSRLVDVGD 186
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 73-182 5.35e-23

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: 88.43  E-value: 5.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  73 VKRLIGLPGDTIEMKDDVLTINGEVYEEPyldefkeKFADDQLQDEYSYremfqqiaagaehftdDFTVTVPEGSYFVMG 152
Cdd:COG4959   27 IKRVAALPGDTVCIKGGQVYINGKPVAEA-------LERDRAGRPLPVW----------------QGCGVVPEGEYFLLG 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 985494063 153 DNRLISRDSRSFGVVTEDQMEGKVLLRFWP 182
Cdd:COG4959   84 DNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 28-176 9.20e-15

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: 66.07  E-value: 9.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  28 PVQVSGHSMDPTLADKQRLIASKIS----SYDRQDIVICVEPDDPSKIAVKRLIGlpgdtiemkddvltingevyeepyl 103
Cdd:cd06530    2 PVVVPGGSMEPTLQPGDLVLVNKLSygfrEPKRGDVVVFKSPGDPGKPIIKRVIG------------------------- 56

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985494063 104 defkekfaddqlqdeysyremfqqiaagaehftddftvtvpegsYFVMGDNRLISRDSRSFGVVTEDQMEGKV 176
Cdd:cd06530   57 --------------------------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
12-175 2.56e-14

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 69.70  E-value: 2.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  12 LFFIVAVVLI-RLFVLTPVQVSGHSMDPTLadkqrLIASKI----SSY-----------------DRQDIVICVEPDDPS 69
Cdd:PRK10861  67 VFPVLAIVLIvRSFIYEPFQIPSGSMMPTL-----LIGDFIlvekFAYgikdpitqttlietghpKRGDIVVFKYPEDPK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063  70 KIAVKRLIGLPGD--------------------------------TIEMKDDVLTINGE--------VYEEPY------- 102
Cdd:PRK10861 142 LDYIKRVVGLPGDkvtydpvskevtiqpgcssgqacenalpvtysNVEPSDFVQTFSRRnggeatsgFFQVPLnetkeng 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494063 103 --LDEFKEKFAD--------DQLQDEYS--YREMFQQIAagaehftddfTVTVPEGSYFVMGDNRLISRDSRSFGVVTED 170
Cdd:PRK10861 222 irLSERKETLGDvthriltvPGAQDQVGmyYQQPGQPLA----------TWVVPPGQYFMMGDNRDNSADSRYWGFVPEA 291


                 ....*
gi 985494063 171 QMEGK 175
Cdd:PRK10861 292 NLVGK 296
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 28-82 4.73e-06

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: 43.02  E-value: 4.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 985494063  28 PVQVSGHSMDPTLADKQRLIASKIS-SYDRQDIVICVEPDDpsKIAVKRLIGLPGD 82
Cdd:cd06462    2 ALRVEGDSMEPTIPDGDLVLVDKSSyEPKRGDIVVFRLPGG--ELTVKRVIGLPGE 55
 
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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