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signal peptidase I [Enterococcus ureilyticus]

Protein Classification

S26 family signal peptidase( domain architecture ID 11493928)

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
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 34-173 9.99e-36

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: 121.57  E-value: 9.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  34 AFLRTHQVSGNSMLPTLNDGDKILVWKGRV----PNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLKGNYLRISyvtnk 109
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYrtsdPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRDGKLYIN----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005939245 110 GKEYEEINVT---DGVAMILERQDEIPMDKYFVLGDNRSHSNDSRSLGLINRTQIEGVVGWRYYPFN 173
Cdd:TIGR02227  76 GKKIDEPYLKpngYLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 34-173 9.99e-36

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: 121.57  E-value: 9.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  34 AFLRTHQVSGNSMLPTLNDGDKILVWKGRV----PNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLKGNYLRISyvtnk 109
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYrtsdPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRDGKLYIN----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005939245 110 GKEYEEINVT---DGVAMILERQDEIPMDKYFVLGDNRSHSNDSRSLGLINRTQIEGVVGWRYYPFN 173
Cdd:TIGR02227  76 GKKIDEPYLKpngYLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 40-170 3.63e-30

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: 108.06  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILV----WKGRVPNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLKGNYLRISyvtnkGKEYEE 115
Cdd:pfam10502  27 VVPGGSMSPTLPIGDYLIVnkfsYGLGEPKRGDIVVFRPPEGPGVPLIKRVIGLPGDRVEYKDDQLYIN-----GKPVGE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005939245 116 INVTDGVAMI------LERQDEIPMDKYFVLGDNRSHSNDSRSLGLINRTQIEGVVGWRYY 170
Cdd:pfam10502 102 PYLADRKGRPtfdlppWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 40-165 1.45e-19

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: 78.40  E-value: 1.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWK----GRVPNRFAIITLEPMDNPQESYVKRVIGmpgdkldlkgnylrisyvtnkgkeyee 115
Cdd:cd06530     4 VVPGGSMEPTLQPGDLVLVNKlsygFREPKRGDVVVFKSPGDPGKPIIKRVIG--------------------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2005939245 116 invtdgvamilerqdeipmdkYFVLGDNRSHSNDSRSLGLINRTQIEGVV 165
Cdd:cd06530    57 ---------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 82-171 2.46e-17

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: 73.41  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  82 YVKRVIGMPGDKLDLKGNYLRIsyvtNkGKEYEEINVTDGVAMILERQDE---IPMDKYFVLGDNRSHSNDSRSLGLINR 158
Cdd:COG4959    26 LIKRVAALPGDTVCIKGGQVYI----N-GKPVAEALERDRAGRPLPVWQGcgvVPEGEYFLLGDNRPNSFDSRYFGPVPR 100

                          90
                  ....*....|...
gi 2005939245 159 TQIEGVVGWRYYP 171
Cdd:COG4959   101 SQIIGRAVPLWTP 113
PRK10861 PRK10861
signal peptidase I;
40-156 9.88e-08

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 50.44  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWK-----------------GRvPNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLK----- 97
Cdd:PRK10861   86 QIPSGSMMPTLLIGDFILVEKfaygikdpitqttlietGH-PKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVTYDpvske 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  98 -------------GNYLRISYVT------------NKGKE--------------------YEEI----NVTDGVAMILER 128
Cdd:PRK10861  165 vtiqpgcssgqacENALPVTYSNvepsdfvqtfsrRNGGEatsgffqvplnetkengirlSERKetlgDVTHRILTVPGA 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2005939245 129 QDE----------------IPMDKYFVLGDNRSHSNDSRSLGLI 156
Cdd:PRK10861  245 QDQvgmyyqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFV 288
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 34-173 9.99e-36

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: 121.57  E-value: 9.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  34 AFLRTHQVSGNSMLPTLNDGDKILVWKGRV----PNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLKGNYLRISyvtnk 109
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYrtsdPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRDGKLYIN----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005939245 110 GKEYEEINVT---DGVAMILERQDEIPMDKYFVLGDNRSHSNDSRSLGLINRTQIEGVVGWRYYPFN 173
Cdd:TIGR02227  76 GKKIDEPYLKpngYLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 40-170 3.63e-30

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: 108.06  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILV----WKGRVPNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLKGNYLRISyvtnkGKEYEE 115
Cdd:pfam10502  27 VVPGGSMSPTLPIGDYLIVnkfsYGLGEPKRGDIVVFRPPEGPGVPLIKRVIGLPGDRVEYKDDQLYIN-----GKPVGE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005939245 116 INVTDGVAMI------LERQDEIPMDKYFVLGDNRSHSNDSRSLGLINRTQIEGVVGWRYY 170
Cdd:pfam10502 102 PYLADRKGRPtfdlppWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 40-165 1.45e-19

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: 78.40  E-value: 1.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWK----GRVPNRFAIITLEPMDNPQESYVKRVIGmpgdkldlkgnylrisyvtnkgkeyee 115
Cdd:cd06530     4 VVPGGSMEPTLQPGDLVLVNKlsygFREPKRGDVVVFKSPGDPGKPIIKRVIG--------------------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2005939245 116 invtdgvamilerqdeipmdkYFVLGDNRSHSNDSRSLGLINRTQIEGVV 165
Cdd:cd06530    57 ---------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 82-171 2.46e-17

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: 73.41  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  82 YVKRVIGMPGDKLDLKGNYLRIsyvtNkGKEYEEINVTDGVAMILERQDE---IPMDKYFVLGDNRSHSNDSRSLGLINR 158
Cdd:COG4959    26 LIKRVAALPGDTVCIKGGQVYI----N-GKPVAEALERDRAGRPLPVWQGcgvVPEGEYFLLGDNRPNSFDSRYFGPVPR 100

                          90
                  ....*....|...
gi 2005939245 159 TQIEGVVGWRYYP 171
Cdd:COG4959   101 SQIIGRAVPLWTP 113
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
35-177 3.78e-17

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 74.89  E-value: 3.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  35 FLRTHQVSGNSMLPTLNDGDKILVWK----GRVPNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLKGNYLRISYVTNKG 110
Cdd:COG0681    32 VFEPFVIPSGSMEPTLLVGDRLLVNKlsygFGEPKRGDIVVFKYPEDPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNE 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005939245 111 KEYEEINVTDGVAMILERqDEIPMDKYFVLGDNRSHSNDSRSLGLINRTQIEGVVGWRYYPFNRIGH 177
Cdd:COG0681   112 PYLEEYYYPVSVDGDVEV-PPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDGVGVGGVVDVVVPDV 177
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 40-165 5.76e-10

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: 53.42  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWKG-RVPNRFAIITLEPMDNpqESYVKRVIGMPGDkldlkgnylrisyvtnkgkeyeeinv 118
Cdd:cd06462     4 RVEGDSMEPTIPDGDLVLVDKSsYEPKRGDIVVFRLPGG--ELTVKRVIGLPGE-------------------------- 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2005939245 119 tdgvamilerqdeipmDKYFVLGDNrSHSNDSRSLGlINRTQIEGVV 165
Cdd:cd06462    56 ----------------GHYFLLGDN-PNSPDSRIDG-PPELDIVGVV 84
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 83-165 1.59e-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: 51.33  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  83 VKRVIGMPGDKLDLKGNYLRISYVTnkgKEYEEINVTDGVAMILERQDE--IPmDKYFVLGDNRSHSNDSRSLGLINRTQ 160
Cdd:TIGR02771  85 LKRVLGLPGDRVTVRADVVAINGQL---LPYSKPLATDSSGRPLPPFPEgvIP-PGFFVVHDTSPTSFDSRYFGPISREQ 160


                  ....*
gi 2005939245 161 IEGVV 165
Cdd:TIGR02771 161 VIGRV 165
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 40-97 6.07e-08

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 48.80  E-value: 6.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWKGR---VPNRFAIITLEpmdnpQESYVKRVIGMPGDKLDLK 97
Cdd:COG2932    39 RVSGDSMEPTIRDGDIVLVDPSDteiRDGGIYVVRTD-----GELLVKRLQRRPDGKLRLI 94
PRK10861 PRK10861
signal peptidase I;
40-156 9.88e-08

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 50.44  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWK-----------------GRvPNRFAIITLEPMDNPQESYVKRVIGMPGDKLDLK----- 97
Cdd:PRK10861   86 QIPSGSMMPTLLIGDFILVEKfaygikdpitqttlietGH-PKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVTYDpvske 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  98 -------------GNYLRISYVT------------NKGKE--------------------YEEI----NVTDGVAMILER 128
Cdd:PRK10861  165 vtiqpgcssgqacENALPVTYSNvepsdfvqtfsrRNGGEatsgffqvplnetkengirlSERKetlgDVTHRILTVPGA 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2005939245 129 QDE----------------IPMDKYFVLGDNRSHSNDSRSLGLI 156
Cdd:PRK10861  245 QDQvgmyyqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFV 288
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 40-167 1.19e-07

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: 47.45  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILV----WKGRVPNRFAIITLEPMDNPQESYVKRVIGMpgdkldlkgnylrisyvTNKGkeyee 115
Cdd:TIGR02754   2 KVTGVSMSPTLPPGDRIIVvpwlKIFRVPPIGNVVVVRHPLQPYGLIIKRLAAV-----------------DDNG----- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2005939245 116 invtdgvamilerqdeipmdkYFVLGDNRSHSNDSRSLGLINRTQIEGVVGW 167
Cdd:TIGR02754  60 ---------------------LFLLGDNPKASTDSRQLGPVPRSLLLGKVLW 90
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 40-128 1.59e-06

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: 44.09  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005939245  40 QVSGNSMLPTLNDGDKILVWKGRVP--NRFAIITLEpmdnpQESYVKRVIGMPGDKLDLkgnylrISYvtNkgKEYEEIN 117
Cdd:cd06529     4 RVKGDSMEPTIPDGDLVLVDPSDTPrdGDIVVARLD-----GELTVKRLQRRGGGRLRL------ISD--N--PAYPPIE 68

                          90
                  ....*....|.
gi 2005939245 118 VTDGVAMILER 128
Cdd:cd06529    69 IDEEELEIVGV 79
Peptidase_S24 pfam00717
Peptidase S24-like;
41-97 5.33e-04

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 37.95  E-value: 5.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2005939245  41 VSGNSMLPTLNDGDKILVWKGRVP--NRFAIITLEpmdnpQESYVKRVIgMPGDKLDLK 97
Cdd:pfam00717  40 VKGDSMEPGIPDGDLVLVDPSREArnGDIVVARLD-----GEATVKRLY-RDGGGIRLI 92
 
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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