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Conserved domains on  [gi|489520333|ref|WP_003425129|]
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signal peptidase I [Clostridioides difficile]

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 ...
 9-169 2.36e-52

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: 164.30  E-value: 2.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333    9 IVEWIKIIITALFFAFII-TRFIKPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTdllqENGRKKELVKR 87
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIrTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRP----PEGPGVPLIKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   88 VIGVPGDHLKIKDSKVYINGKLLNEVsYIHDNYTEGDIDM-------VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENI 160
Cdd:pfam10502  77 VIGLPGDRVEYKDDQLYINGKPVGEP-YLADRKGRPTFDLppwqgcrVVPEGEYFVMGDNRDNSLDSRY--FGFVPASNI 153


                  ....*....
gi 489520333  161 KGKVILRVF 169
Cdd:pfam10502 154 VGRAVFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 9-169 2.36e-52

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: 164.30  E-value: 2.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333    9 IVEWIKIIITALFFAFII-TRFIKPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTdllqENGRKKELVKR 87
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIrTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRP----PEGPGVPLIKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   88 VIGVPGDHLKIKDSKVYINGKLLNEVsYIHDNYTEGDIDM-------VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENI 160
Cdd:pfam10502  77 VIGLPGDRVEYKDDQLYINGKPVGEP-YLADRKGRPTFDLppwqgcrVVPEGEYFVMGDNRDNSLDSRY--FGFVPASNI 153


                  ....*....
gi 489520333  161 KGKVILRVF 169
Cdd:pfam10502 154 VGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 29-171 2.34e-44

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: 143.52  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   29 FIKPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKtdllQENGRKKELVKRVIGVPGDHLKIKDSKVYINGK 108
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFK----DPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520333  109 LLNEvSYIHDNYTEGDIDM----VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENIKGKVILRVFPF 171
Cdd:TIGR02227  78 KIDE-PYLKPNGYLDTSEFntpvKVPPGHYFVLGDNRDNSLDSRY--FGFVPIDQIIGKVSFVFYPF 141
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
6-173 2.18e-35

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 122.27  E-value: 2.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   6 KEEIVEWIKIIITALFFAFIITRFI-KPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTDllqeNGRKKEL 84
Cdd:COG0681    8 KRELREWLKSIVIALLLALLIRTFVfEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYP----EDPSKDY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  85 VKRVIGVPGDHLKIKDSKVYINGKLLNEVSYIHDNYTEGDIDMV----IPKGKVFAMGDNREVSLDSRYKEVGLVDEENI 160
Cdd:COG0681   84 IKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVevppGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDG 163

                        170
                 ....*....|...
gi 489520333 161 KGKVILRVFPFTD 173
Cdd:COG0681  164 VGVGGVVDVVVPD 176
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 32-164 3.87e-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: 77.24  E-value: 3.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  32 PTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTDllqeNGRKKELVKRVIGvpgdhlkikdskvyingklln 111
Cdd:cd06530    2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSP----GDPGKPIIKRVIG--------------------- 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489520333 112 evsyihdnytegdidmvipkgkVFAMGDNREVSLDSRYkeVGLVDEENIKGKV 164
Cdd:cd06530   57 ----------------------YFVLGDNRNNSLDSRY--WGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
20-163 6.25e-08

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 50.82  E-value: 6.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  20 LFFAFIITRFI-KPTLVNGESMYPTLKSHDYLVANRMTYKLS------------EPKCGDIMIFKTDLlqenGRKKELVK 86
Cdd:PRK10861  71 LAIVLIVRSFIyEPFQIPSGSMMPTLLIGDFILVEKFAYGIKdpitqttlietgHPKRGDIVVFKYPE----DPKLDYIK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  87 RVIGVPGDH-------------------------LKIKDSKVY------------------------INGKLLNEVSYIH 117
Cdd:PRK10861 147 RVVGLPGDKvtydpvskevtiqpgcssgqacenaLPVTYSNVEpsdfvqtfsrrnggeatsgffqvpLNETKENGIRLSE 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489520333 118 DNYTEGDI-----------DM---------------VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENIKGK 163
Cdd:PRK10861 227 RKETLGDVthriltvpgaqDQvgmyyqqpgqplatwVVPPGQYFMMGDNRDNSADSRY--WGFVPEANLVGK 296
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 9-169 2.36e-52

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: 164.30  E-value: 2.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333    9 IVEWIKIIITALFFAFII-TRFIKPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTdllqENGRKKELVKR 87
Cdd:pfam10502   1 LLEWVKAIVIALLLALLIrTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRP----PEGPGVPLIKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   88 VIGVPGDHLKIKDSKVYINGKLLNEVsYIHDNYTEGDIDM-------VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENI 160
Cdd:pfam10502  77 VIGLPGDRVEYKDDQLYINGKPVGEP-YLADRKGRPTFDLppwqgcrVVPEGEYFVMGDNRDNSLDSRY--FGFVPASNI 153


                  ....*....
gi 489520333  161 KGKVILRVF 169
Cdd:pfam10502 154 VGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 29-171 2.34e-44

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: 143.52  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   29 FIKPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKtdllQENGRKKELVKRVIGVPGDHLKIKDSKVYINGK 108
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFK----DPDTNKNIYVKRIIGLPGDKVEFRDGKLYINGK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520333  109 LLNEvSYIHDNYTEGDIDM----VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENIKGKVILRVFPF 171
Cdd:TIGR02227  78 KIDE-PYLKPNGYLDTSEFntpvKVPPGHYFVLGDNRDNSLDSRY--FGFVPIDQIIGKVSFVFYPF 141
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
6-173 2.18e-35

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 122.27  E-value: 2.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   6 KEEIVEWIKIIITALFFAFIITRFI-KPTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTDllqeNGRKKEL 84
Cdd:COG0681    8 KRELREWLKSIVIALLLALLIRTFVfEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYP----EDPSKDY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  85 VKRVIGVPGDHLKIKDSKVYINGKLLNEVSYIHDNYTEGDIDMV----IPKGKVFAMGDNREVSLDSRYKEVGLVDEENI 160
Cdd:COG0681   84 IKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVevppGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDG 163

                        170
                 ....*....|...
gi 489520333 161 KGKVILRVFPFTD 173
Cdd:COG0681  164 VGVGGVVDVVVPD 176
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 65-170 2.39e-26

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 96.52  E-value: 2.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  65 GDIMIFKT--DLLQENG---RKKELVKRVIGVPGDHLKIKDSKVYINGKLLNEvSYIHD----NYTEGDIDMVIPKGKVF 135
Cdd:COG4959    2 GDLVAFRPpePLAAERGylpRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAE-ALERDragrPLPVWQGCGVVPEGEYF 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489520333 136 AMGDNREVSLDSRYkeVGLVDEENIKGKVILRVFP 170
Cdd:COG4959   81 LLGDNRPNSFDSRY--FGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 32-164 3.87e-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: 77.24  E-value: 3.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  32 PTLVNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTDllqeNGRKKELVKRVIGvpgdhlkikdskvyingklln 111
Cdd:cd06530    2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSP----GDPGKPIIKRVIG--------------------- 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489520333 112 evsyihdnytegdidmvipkgkVFAMGDNREVSLDSRYkeVGLVDEENIKGKV 164
Cdd:cd06530   57 ----------------------YFVLGDNRNNSLDSRY--WGPVPEDDIVGKV 85
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 35-164 2.67e-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: 48.80  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  35 VNGESMYPTLKSHDYLVANRMTYklsEPKCGDIMIFKTDllqengRKKELVKRVIGVPGdhlkikdskvyingkllnevs 114
Cdd:cd06462    5 VEGDSMEPTIPDGDLVLVDKSSY---EPKRGDIVVFRLP------GGELTVKRVIGLPG--------------------- 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489520333 115 yihdnytegdidmvipKGKVFAMGDNREvSLDSRYKEvglVDEENIKGKV 164
Cdd:cd06462   55 ----------------EGHYFLLGDNPN-SPDSRIDG---PPELDIVGVV 84
PRK10861 PRK10861
signal peptidase I;
20-163 6.25e-08

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 50.82  E-value: 6.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  20 LFFAFIITRFI-KPTLVNGESMYPTLKSHDYLVANRMTYKLS------------EPKCGDIMIFKTDLlqenGRKKELVK 86
Cdd:PRK10861  71 LAIVLIVRSFIyEPFQIPSGSMMPTLLIGDFILVEKFAYGIKdpitqttlietgHPKRGDIVVFKYPE----DPKLDYIK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  87 RVIGVPGDH-------------------------LKIKDSKVY------------------------INGKLLNEVSYIH 117
Cdd:PRK10861 147 RVVGLPGDKvtydpvskevtiqpgcssgqacenaLPVTYSNVEpsdfvqtfsrrnggeatsgffqvpLNETKENGIRLSE 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489520333 118 DNYTEGDI-----------DM---------------VIPKGKVFAMGDNREVSLDSRYkeVGLVDEENIKGK 163
Cdd:PRK10861 227 RKETLGDVthriltvpgaqDQvgmyyqqpgqplatwVVPPGQYFMMGDNRDNSADSRY--WGFVPEANLVGK 296
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 79-164 3.17e-07

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: 47.86  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   79 GRKKELVKRVIGVPGDHLKIKDSKVYINGKLLnEVSYIHDNYTEGDI-----DMVIPKGkVFAMGDNREVSLDSRYkeVG 153
Cdd:TIGR02771  79 GGFGPLLKRVLGLPGDRVTVRADVVAINGQLL-PYSKPLATDSSGRPlppfpEGVIPPG-FFVVHDTSPTSFDSRY--FG 154

                          90
                  ....*....|.
gi 489520333  154 LVDEENIKGKV 164
Cdd:TIGR02771 155 PISREQVIGRV 165
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
 84-169 3.95e-05

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 41.93  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333  84 LVKRVIGVPGDHLKIKDSKVYINGKLL------------NEV-SYIHDNYTEGDidmvipkGKVFAMGDNREVSLDSRYk 150
Cdd:PRK13884  88 MMKRVLAAKGDAVSVTDDGVRVNGELLplskpiladgagRPLpRYQANSYTLGE-------SELLLMSDVSATSFDGRY- 159

                         90
                 ....*....|....*....
gi 489520333 151 eVGLVDEENIKGkVILRVF 169
Cdd:PRK13884 160 -FGPINRSQIKT-VIRPVI 176
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 35-164 2.29e-04

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: 38.59  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520333   35 VNGESMYPTLKSHDYLVANRMTYKLSEPKCGDIMIFKTDlLQENGRkkeLVKRVIGVpgdhlkikdskvyingkllnevs 114
Cdd:TIGR02754   3 VTGVSMSPTLPPGDRIIVVPWLKIFRVPPIGNVVVVRHP-LQPYGL---IIKRLAAV----------------------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489520333  115 yihDNytegdidmvipkGKVFAMGDNREVSLDSRykEVGLVDEENIKGKV 164
Cdd:TIGR02754  56 ---DD------------NGLFLLGDNPKASTDSR--QLGPVPRSLLLGKV 88
 
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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