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Conserved domains on  [gi|2540098533|ref|WP_296289408|]
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signal peptidase I [Lactobacillus sp.]

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

Gene Ontology:  GO:0004252|GO:0006465
MEROPS:  S26
PubMed:  10982814

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 18-181 5.43e-51

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: 161.60  E-value: 5.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  18 ILDFVIMVVVIFGIFYLLFHFVLVNVRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALIPPKranDPHALYVKRV 93
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIvnkfSYGLGEPKRGDIVVFRPPE---GPGVPLIKRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  94 IGLPGDKVTAKNDKMYVNGKLIPEPYLNNKFKKADNAAGyTYTNNFTyrVPSGHYWVMGDHRDISKDSRKFGPVSRGNLV 173
Cdd:pfam10502  78 IGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFDLP-PWQGCRV--VPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 2540098533 174 GKVVFRYW 181
Cdd:pfam10502 155 GRAVFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 18-181 5.43e-51

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: 161.60  E-value: 5.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  18 ILDFVIMVVVIFGIFYLLFHFVLVNVRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALIPPKranDPHALYVKRV 93
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIvnkfSYGLGEPKRGDIVVFRPPE---GPGVPLIKRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  94 IGLPGDKVTAKNDKMYVNGKLIPEPYLNNKFKKADNAAGyTYTNNFTyrVPSGHYWVMGDHRDISKDSRKFGPVSRGNLV 173
Cdd:pfam10502  78 IGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFDLP-PWQGCRV--VPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 2540098533 174 GKVVFRYW 181
Cdd:pfam10502 155 GRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 38-184 1.42e-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: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  38 FVLVNVRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALippKRANDPHALYVKRVIGLPGDKVTAKNDKMYVNGK 113
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILvnkfAYRTSDPKRGDIVVF---KDPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGK 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540098533 114 LIPEPYLNNkfkkadNAAGYTYTNNFTYRVPSGHYWVMGDHRDISKDSRKFGPVSRGNLVGKVVFRYWPFN 184
Cdd:TIGR02227  78 KIDEPYLKP------NGYLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 72-182 5.83e-29

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: 103.84  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  72 DVVALIPPKRAND------PHALYVKRVIGLPGDKVTAKNDKMYVNGKLIPEPylnnkfKKADNAAGYTYTNNFTYRVPS 145
Cdd:COG4959     3 DLVAFRPPEPLAAergylpRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEA------LERDRAGRPLPVWQGCGVVPE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2540098533 146 GHYWVMGDHRDISKDSRKFGPVSRGNLVGKVVFRYWP 182
Cdd:COG4959    77 GEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 43-176 2.80e-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: 67.61  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  43 VRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALIPPKranDPHALYVKRVIGlpgdkvtakndkmyvngklipep 118
Cdd:cd06530     3 VVVPGGSMEPTLQPGDLVLvnklSYGFREPKRGDVVVFKSPG---DPGKPIIKRVIG----------------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2540098533 119 ylnnkfkkadnaagytytnnftyrvpsghYWVMGDHRDISKDSRKFGPVSRGNLVGKV 176
Cdd:cd06530    57 -----------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
68-175 8.71e-13

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 65.08  E-value: 8.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  68 PKRYDVVALIPPKranDPHALYVKRVIGLPGDKVTAKndkmYVNGKLIPEPYLNNKfKKADNAAGYTYTNNF-------- 139
Cdd:PRK10861  126 PKRGDIVVFKYPE---DPKLDYIKRVVGLPGDKVTYD----PVSKEVTIQPGCSSG-QACENALPVTYSNVEpsdfvqtf 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533 140 ---------------------------------------------------------------TYRVPSGHYWVMGDHRD 156
Cdd:PRK10861  198 srrnggeatsgffqvplnetkengirlserketlgdvthriltvpgaqdqvgmyyqqpgqplaTWVVPPGQYFMMGDNRD 277

                         170
                  ....*....|....*....
gi 2540098533 157 ISKDSRKFGPVSRGNLVGK 175
Cdd:PRK10861  278 NSADSRYWGFVPEANLVGK 296
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 18-181 5.43e-51

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: 161.60  E-value: 5.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  18 ILDFVIMVVVIFGIFYLLFHFVLVNVRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALIPPKranDPHALYVKRV 93
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIvnkfSYGLGEPKRGDIVVFRPPE---GPGVPLIKRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  94 IGLPGDKVTAKNDKMYVNGKLIPEPYLNNKFKKADNAAGyTYTNNFTyrVPSGHYWVMGDHRDISKDSRKFGPVSRGNLV 173
Cdd:pfam10502  78 IGLPGDRVEYKDDQLYINGKPVGEPYLADRKGRPTFDLP-PWQGCRV--VPEGEYFVMGDNRDNSLDSRYFGFVPASNIV 154


                  ....*...
gi 2540098533 174 GKVVFRYW 181
Cdd:pfam10502 155 GRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 38-184 1.42e-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: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  38 FVLVNVRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALippKRANDPHALYVKRVIGLPGDKVTAKNDKMYVNGK 113
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILvnkfAYRTSDPKRGDIVVF---KDPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGK 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540098533 114 LIPEPYLNNkfkkadNAAGYTYTNNFTYRVPSGHYWVMGDHRDISKDSRKFGPVSRGNLVGKVVFRYWPFN 184
Cdd:TIGR02227  78 KIDEPYLKP------NGYLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPFD 142
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 72-182 5.83e-29

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: 103.84  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  72 DVVALIPPKRAND------PHALYVKRVIGLPGDKVTAKNDKMYVNGKLIPEPylnnkfKKADNAAGYTYTNNFTYRVPS 145
Cdd:COG4959     3 DLVAFRPPEPLAAergylpRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEA------LERDRAGRPLPVWQGCGVVPE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2540098533 146 GHYWVMGDHRDISKDSRKFGPVSRGNLVGKVVFRYWP 182
Cdd:COG4959    77 GEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
9-186 1.29e-26

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 99.93  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533   9 DEEESLGKFILDFVIMVVVIFGIFYLLFHFVLVNVRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALIPPKranD 84
Cdd:COG0681     2 SKKKKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLvnklSYGFGEPKRGDIVVFKYPE---D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  85 PHALYVKRVIGLPGDKVTAKNDKMYVNGKLIPEPYLNNKFkkadnaagYTYTNNFTYRVPSGHYWVMGDHRDISKDSRKF 164
Cdd:COG0681    79 PSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYY--------YPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSG 150

                         170       180
                  ....*....|....*....|..
gi 2540098533 165 GPVSRGNLVGKVVFRYWPFNRV 186
Cdd:COG0681   151 DPDDGGGGVGVDGVGVGGVVDV 172
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 43-176 2.80e-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: 67.61  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  43 VRVSGISMQPTFENNERMI----SVRHFTPKRYDVVALIPPKranDPHALYVKRVIGlpgdkvtakndkmyvngklipep 118
Cdd:cd06530     3 VVVPGGSMEPTLQPGDLVLvnklSYGFREPKRGDVVVFKSPG---DPGKPIIKRVIG----------------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2540098533 119 ylnnkfkkadnaagytytnnftyrvpsghYWVMGDHRDISKDSRKFGPVSRGNLVGKV 176
Cdd:cd06530    57 -----------------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
68-175 8.71e-13

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 65.08  E-value: 8.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  68 PKRYDVVALIPPKranDPHALYVKRVIGLPGDKVTAKndkmYVNGKLIPEPYLNNKfKKADNAAGYTYTNNF-------- 139
Cdd:PRK10861  126 PKRGDIVVFKYPE---DPKLDYIKRVVGLPGDKVTYD----PVSKEVTIQPGCSSG-QACENALPVTYSNVEpsdfvqtf 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533 140 ---------------------------------------------------------------TYRVPSGHYWVMGDHRD 156
Cdd:PRK10861  198 srrnggeatsgffqvplnetkengirlserketlgdvthriltvpgaqdqvgmyyqqpgqplaTWVVPPGQYFMMGDNRD 277

                         170
                  ....*....|....*....
gi 2540098533 157 ISKDSRKFGPVSRGNLVGK 175
Cdd:PRK10861  278 NSADSRYWGFVPEANLVGK 296
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 90-177 9.43e-10

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: 55.18  E-value: 9.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  90 VKRVIGLPGDKVTAKNDKMYVNGKLIPEPylnnkFKKADNAAGYTYTNNFTYRVPSGhYWVMGDHRDISKDSRKFGPVSR 169
Cdd:TIGR02771  85 LKRVLGLPGDRVTVRADVVAINGQLLPYS-----KPLATDSSGRPLPPFPEGVIPPG-FFVVHDTSPTSFDSRYFGPISR 158


                  ....*...
gi 2540098533 170 GNLVGKVV 177
Cdd:TIGR02771 159 EQVIGRVK 166
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 43-176 9.33e-08

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: 47.64  E-value: 9.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  43 VRVSGISMQPTFENNERMISVRH-FTPKRYDVVALIPPKrandpHALYVKRVIGLPGDkvtakndkmyvngklipepyln 121
Cdd:cd06462     3 LRVEGDSMEPTIPDGDLVLVDKSsYEPKRGDIVVFRLPG-----GELTVKRVIGLPGE---------------------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2540098533 122 nkfkkadnaagytytnnftyrvpsGHYWVMGDHRDiSKDSRKFGPvSRGNLVGKV 176
Cdd:cd06462    56 ------------------------GHYFLLGDNPN-SPDSRIDGP-PELDIVGVV 84
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 44-177 2.02e-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: 47.06  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  44 RVSGISMQPTFENNERMISV---RHF-TPKRYDVVALIPPKRandPHALYVKRVIGlpgdkvtakndkmyvngklipepy 119
Cdd:TIGR02754   2 KVTGVSMSPTLPPGDRIIVVpwlKIFrVPPIGNVVVVRHPLQ---PYGLIIKRLAA------------------------ 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2540098533 120 lnnkfkkadnaagytytnnftyrVPSGHYWVMGDHRDISKDSRKFGPVSRGNLVGKVV 177
Cdd:TIGR02754  55 -----------------------VDDNGLFLLGDNPKASTDSRQLGPVPRSLLLGKVL 89
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
 91-174 7.49e-07

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 46.94  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540098533  91 KRVIGLPGDKVTAKNDKMYVNGKLIPepylNNKFKKADnAAGYTYT--NNFTYRVPSGHYWVMGDHRDISKDSRKFGPVS 168
Cdd:PRK13884   90 KRVLAAKGDAVSVTDDGVRVNGELLP----LSKPILAD-GAGRPLPryQANSYTLGESELLLMSDVSATSFDGRYFGPIN 164


                  ....*.
gi 2540098533 169 RGNLVG 174
Cdd:PRK13884  165 RSQIKT 170
 
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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